An adaptor protein complex found primarily on perinuclear compartments.
A clathrin adaptor protein complex primarily involved in clathrin-related transport at the TRANS-GOLGI NETWORK.
An adaptor protein complex primarily involved in the formation of clathrin-related endocytotic vesicles (ENDOSOMES) at the CELL MEMBRANE.
An adaptor protein complex involved in transport of molecules between the TRANS-GOLGI NETWORK and the endosomal-lysosomal system.
The subunits that make up the large, medium and small chains of adaptor proteins.
A family of large adaptin protein subunits of approximately 130-kDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 3.
A family of medium adaptin protein subunits of approximately 45 KDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 3 and ADAPTOR PROTEIN COMPLEX 4.
A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. They perform functions such as binding to the cell membrane, capturing cargo molecules and promoting the assembly of CLATHRIN. The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found.
A family of large adaptin protein subunits of approximately 90 KDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 1.
A family of large adaptin protein complex subunits of approximately 90-130 kDa in size.
A family of large adaptin protein subunits of approximately 100 kDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 2.
A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymes
The main structural coat protein of COATED VESICLES which play a key role in the intracellular transport between membranous organelles. Each molecule of clathrin consists of three light chains (CLATHRIN LIGHT CHAINS) and three heavy chains (CLATHRIN HEAVY CHAINS) that form a structure called a triskelion. Clathrin also interacts with cytoskeletal proteins.
The fundamental dispositions and traits of humans. (Merriam-Webster's Collegiate Dictionary, 10th ed)
A subclass of clathrin assembly proteins that occur as monomers.
A signal transducing adaptor protein that links extracellular signals to the MAP KINASE SIGNALING SYSTEM. Grb2 associates with activated EPIDERMAL GROWTH FACTOR RECEPTOR and PLATELET-DERIVED GROWTH FACTOR RECEPTORS via its SH2 DOMAIN. It also binds to and translocates the SON OF SEVENLESS PROTEINS through its SH3 DOMAINS to activate PROTO-ONCOGENE PROTEIN P21(RAS).
A family of signaling adaptor proteins that contain SRC HOMOLOGY DOMAINS. Many members of this family are involved in transmitting signals from CELL SURFACE RECEPTORS to MITOGEN-ACTIVATED PROTEIN KINASES.
A family of small adaptin protein complex subunits of approximately 19 KDa in size.
Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.
Vesicles formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles are covered with a lattice-like network of coat proteins, such as CLATHRIN, coat protein complex proteins, or CAVEOLINS.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
A network of membrane compartments, located at the cytoplasmic side of the GOLGI APPARATUS, where proteins and lipids are sorted for transport to various locations in the cell or cell membrane.
Vesicles formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles is covered with a lattice-like network of the protein CLATHRIN. Shortly after formation, however, the clathrin coat is removed and the vesicles are referred to as ENDOSOMES.
Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
Transport proteins that carry specific substances in the blood or across cell membranes.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Vesicles that are involved in shuttling cargo from the interior of the cell to the cell surface, from the cell surface to the interior, across the cell or around the cell to various locations.
Specialized regions of the cell membrane composed of pits coated with a bristle covering made of the protein CLATHRIN. These pits are the entry route for macromolecules bound by cell surface receptors. The pits are then internalized into the cytoplasm to form the COATED VESICLES.
A binding partner for several RECEPTOR PROTEIN-TYROSINE KINASES, including INSULIN RECEPTOR and INSULIN-LIKE GROWTH FACTOR RECEPTOR. It contains a C-terminal SH2 DOMAIN and mediates various SIGNAL TRANSDUCTION pathways.
Products of the retroviral NEF GENE. They play a role as accessory proteins that influence the rate of viral infectivity and the destruction of the host immune system. nef gene products were originally found as factors that trans-suppress viral replication and function as negative regulators of transcription. nef stands for negative factor.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Regions of AMINO ACID SEQUENCE similarity in the SRC-FAMILY TYROSINE KINASES that fold into specific functional tertiary structures. The SH1 domain is a CATALYTIC DOMAIN. SH2 and SH3 domains are protein interaction domains. SH2 usually binds PHOSPHOTYROSINE-containing proteins and SH3 interacts with CYTOSKELETAL PROTEINS.
Macromolecular complexes formed from the association of defined protein subunits.
Established cell cultures that have the potential to propagate indefinitely.
A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Proteins encoded by the NEF GENES of the HUMAN IMMUNODEFICIENCY VIRUS.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
Signal transducing adaptor proteins that contain SRC HOMOLOGY DOMAINS and play a role in CYTOSKELETON reorganization. c-crk protein is closely related to ONCOGENE PROTEIN V-CRK and includes several alternatively spliced isoforms.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Methods for determining interaction between PROTEINS.
A death domain receptor signaling adaptor protein that plays a role in signaling the activation of INITIATOR CASPASES such as CASPASE 2. It contains a death domain that is specific for RIP SERINE-THEONINE KINASES and a caspase-binding domain that binds to and activates CASPASES such as CASPASE 2.
An intracellular signaling adaptor protein that plays a role in TOLL-LIKE RECEPTOR and INTERLEUKIN 1 RECEPTORS signal transduction. It forms a signaling complex with the activated cell surface receptors and members of the IRAK KINASES.
Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.
Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.
Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.
CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
A SH2 DOMAIN-containing protein that mediates SIGNAL TRANSDUCTION pathways from multiple CELL SURFACE RECEPTORS, including the EPHB1 RECEPTOR. It interacts with FOCAL ADHESION KINASE and is involved in CELL MIGRATION.
Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible.
Protein modules with conserved ligand-binding surfaces which mediate specific interaction functions in SIGNAL TRANSDUCTION PATHWAYS and the specific BINDING SITES of their cognate protein LIGANDS.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
A CELL LINE derived from human T-CELL LEUKEMIA and used to determine the mechanism of differential susceptibility to anti-cancer drugs and radiation.
Crk-associated substrate was originally identified as a highly phosphorylated 130 kDa protein that associates with ONCOGENE PROTEIN CRK and ONCOGENE PROTEIN SRC. It is a signal transducing adaptor protein that undergoes tyrosine PHOSPHORYLATION in signaling pathways that regulate CELL MIGRATION and CELL PROLIFERATION.
A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.
Proteins coded by oncogenes. They include proteins resulting from the fusion of an oncogene and another gene (ONCOGENE PROTEINS, FUSION).
A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.
Proto-oncogene proteins that negatively regulate RECEPTOR PROTEIN-TYROSINE KINASE signaling. It is a UBIQUITIN-PROTEIN LIGASE and the cellular homologue of ONCOGENE PROTEIN V-CBL.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Cell surface receptors that are specific for INTERLEUKIN-1. Included under this heading are signaling receptors, non-signaling receptors and accessory proteins required for receptor signaling. Signaling from interleukin-1 receptors occurs via interaction with SIGNAL TRANSDUCING ADAPTOR PROTEINS such as MYELOID DIFFERENTIATION FACTOR 88.
An amino acid that occurs in endogenous proteins. Tyrosine phosphorylation and dephosphorylation plays a role in cellular signal transduction and possibly in cell growth control and carcinogenesis.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
A class of RAS GUANINE NUCLEOTIDE EXCHANGE FACTORS that are genetically related to the Son of Sevenless gene from DROSOPHILA. Sevenless refers to genetic mutations in DROSOPHILA that cause loss of the R7 photoreceptor which is required to see UV light.
Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions.
A family of intracellular signaling adaptor proteins that contain caspase activation and recruitment domains. Proteins that contain this domain play a role in APOPTOSIS-related signal transduction by associating with other CARD domain-containing members and in activating INITIATOR CASPASES that contain CARD domains within their N-terminal pro-domain region.
Proteins prepared by recombinant DNA technology.
Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity.
Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.
A PROTEIN-TYROSINE KINASE family that was originally identified by homology to the Rous sarcoma virus ONCOGENE PROTEIN PP60(V-SRC). They interact with a variety of cell-surface receptors and participate in intracellular signal transduction pathways. Oncogenic forms of src-family kinases can occur through altered regulation or expression of the endogenous protein and by virally encoded src (v-src) genes.
Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.
The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)
A phosphoinositide phospholipase C subtype that is primarily regulated by PROTEIN-TYROSINE KINASES. It is structurally related to PHOSPHOLIPASE C DELTA with the addition of SRC HOMOLOGY DOMAINS and pleckstrin homology domains located between two halves of the CATALYTIC DOMAIN.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
Glycoproteins found on the membrane or surface of cells.
A gene silencing phenomenon whereby specific dsRNAs (RNA, DOUBLE-STRANDED) trigger the degradation of homologous mRNA (RNA, MESSENGER). The specific dsRNAs are processed into SMALL INTERFERING RNA (siRNA) which serves as a guide for cleavage of the homologous mRNA in the RNA-INDUCED SILENCING COMPLEX. DNA METHYLATION may also be triggered during this process.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Paxillin is a signal transducing adaptor protein that localizes to FOCAL ADHESIONS via its four LIM domains. It undergoes PHOSPHORYLATION in response to integrin-mediated CELL ADHESION, and interacts with a variety of proteins including VINCULIN; FOCAL ADHESION KINASE; PROTO-ONCOGENE PROTEIN PP60(C-SRC); and PROTO-ONCOGENE PROTEIN C-CRK.
Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.
Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.
A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.
A large class of structurally-related proteins that contain one or more LIM zinc finger domains. Many of the proteins in this class are involved in intracellular signaling processes and mediate their effects via LIM domain protein-protein interactions. The name LIM is derived from the first three proteins in which the motif was found: LIN-11, Isl1 and Mec-3.
A family of pattern recognition receptors characterized by an extracellular leucine-rich domain and a cytoplasmic domain that share homology with the INTERLEUKIN 1 RECEPTOR and the DROSOPHILA toll protein. Following pathogen recognition, toll-like receptors recruit and activate a variety of SIGNAL TRANSDUCING ADAPTOR PROTEINS.
A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.
A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.
Graphs representing sets of measurable, non-covalent physical contacts with specific PROTEINS in living organisms or in cells.
A pattern recognition receptor that interacts with LYMPHOCYTE ANTIGEN 96 and LIPOPOLYSACCHARIDES. It mediates cellular responses to GRAM-NEGATIVE BACTERIA.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
A signal-transducing adaptor protein that associates with TNF RECEPTOR complexes. It contains a death effector domain that can interact with death effector domains found on INITIATOR CASPASES such as CASPASE 8 and CASPASE 10. Activation of CASPASES via interaction with this protein plays a role in the signaling cascade that leads to APOPTOSIS.
Molecules on the surface of T-lymphocytes that recognize and combine with antigens. The receptors are non-covalently associated with a complex of several polypeptides collectively called CD3 antigens (ANTIGENS, CD3). Recognition of foreign antigen and the major histocompatibility complex is accomplished by a single heterodimeric antigen-receptor structure, composed of either alpha-beta (RECEPTORS, ANTIGEN, T-CELL, ALPHA-BETA) or gamma-delta (RECEPTORS, ANTIGEN, T-CELL, GAMMA-DELTA) chains.
The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the PROTEASOME ENDOPEPTIDASE COMPLEX where proteolysis occurs.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.
Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell.
The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.
Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.
Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.
A family of structurally related proteins that were originally discovered for their role in cell-cycle regulation in CAENORHABDITIS ELEGANS. They play important roles in regulation of the CELL CYCLE and as components of UBIQUITIN-PROTEIN LIGASES.
A large family of signal-transducing adaptor proteins present in wide variety of eukaryotes. They are PHOSPHOSERINE and PHOSPHOTHREONINE binding proteins involved in important cellular processes including SIGNAL TRANSDUCTION; CELL CYCLE control; APOPTOSIS; and cellular stress responses. 14-3-3 proteins function by interacting with other signal-transducing proteins and effecting changes in their enzymatic activity and subcellular localization. The name 14-3-3 derives from numerical designations used in the original fractionation patterns of the proteins.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
Intracellular signaling adaptor proteins that play a role in the coupling of SYNDECANS to CYTOSKELETAL PROTEINS.
A macromolecular complex of proteins that includes DYSTROPHIN and DYSTROPHIN-ASSOCIATED PROTEINS. It plays a structural role in the linking the CYTOSKELETON to the EXTRACELLULAR MATRIX.
A protein tyrosine kinase that is required for T-CELL development and T-CELL ANTIGEN RECEPTOR function.
Membrane-associated tyrosine-specific kinases encoded by the c-src genes. They have an important role in cellular growth control. Truncation of carboxy-terminal residues in pp60(c-src) leads to PP60(V-SRC) which has the ability to transform cells. This kinase pp60 c-src should not be confused with csk, also known as c-src kinase.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Lymphocytes responsible for cell-mediated immunity. Two types have been identified - cytotoxic (T-LYMPHOCYTES, CYTOTOXIC) and helper T-lymphocytes (T-LYMPHOCYTES, HELPER-INDUCER). They are formed when lymphocytes circulate through the THYMUS GLAND and differentiate to thymocytes. When exposed to an antigen, they divide rapidly and produce large numbers of new T cells sensitized to that antigen.
The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Proteins that bind to RNA molecules. Included here are RIBONUCLEOPROTEINS and other proteins whose function is to bind specifically to RNA.
Proteins found in any species of fungus.
MONOMERIC GTP-BINDING PROTEINS that were initially recognized as allosteric activators of the MONO(ADP-RIBOSE) TRANSFERASE of the CHOLERA TOXIN catalytic subunit. They are involved in vesicle trafficking and activation of PHOSPHOLIPASE D. This enzyme was formerly listed as EC
The process by which two molecules of the same chemical composition form a condensation product or polymer.
A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
A superfamily of PROTEIN-SERINE-THREONINE KINASES that are activated by diverse stimuli via protein kinase cascades. They are the final components of the cascades, activated by phosphorylation by MITOGEN-ACTIVATED PROTEIN KINASE KINASES, which in turn are activated by mitogen-activated protein kinase kinase kinases (MAP KINASE KINASE KINASES).
Phosphotransferases that catalyzes the conversion of 1-phosphatidylinositol to 1-phosphatidylinositol 3-phosphate. Many members of this enzyme class are involved in RECEPTOR MEDIATED SIGNAL TRANSDUCTION and regulation of vesicular transport with the cell. Phosphatidylinositol 3-Kinases have been classified both according to their substrate specificity and their mode of action within the cell.
Proteins found in any species of bacterium.
Cell lines whose original growing procedure consisted being transferred (T) every 3 days and plated at 300,000 cells per plate (J Cell Biol 17:299-313, 1963). Lines have been developed using several different strains of mice. Tissues are usually fibroblasts derived from mouse embryos but other types and sources have been developed as well. The 3T3 lines are valuable in vitro host systems for oncogenic virus transformation studies, since 3T3 cells possess a high sensitivity to CONTACT INHIBITION.
A cell line derived from cultured tumor cells.
Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
Cleavage of proteins into smaller peptides or amino acids either by PROTEASES or non-enzymatically (e.g., Hydrolysis). It does not include Protein Processing, Post-Translational.
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
Protein interaction domains of about 70-90 amino acid residues, named after a common structure found in PSD-95, Discs Large, and Zona Occludens 1 proteins. PDZ domains are involved in the recruitment and interaction of proteins, and aid the formation of protein scaffolds and signaling networks. This is achieved by sequence-specific binding between a PDZ domain in one protein and a PDZ motif in another protein.
Ubiquitous, inducible, nuclear transcriptional activator that binds to enhancer elements in many different cell types and is activated by pathogenic stimuli. The NF-kappa B complex is a heterodimer composed of two DNA-binding subunits: NF-kappa B1 and relA.
A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology.
A light microscopic technique in which only a small spot is illuminated and observed at a time. An image is constructed through point-by-point scanning of the field in this manner. Light sources may be conventional or laser, and fluorescence or transmitted observations are possible.
Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
Intracellular signaling adaptor proteins that bind to the cytoplasmic death domain region found on DEATH DOMAIN RECEPTORS. Many of the proteins in this class take part in intracellular signaling from TUMOR NECROSIS FACTOR RECEPTORS.
Regulatory proteins that down-regulate phosphorylated G-protein membrane receptors, including rod and cone photoreceptors and adrenergic receptors.
Cell surface molecules on cells of the immune system that specifically bind surface molecules or messenger molecules and trigger changes in the behavior of cells. Although these receptors were first identified in the immune system, many have important functions elsewhere.
Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.
Adherence of cells to surfaces or to other cells.
A general term for single-celled rounded fungi that reproduce by budding. Brewers' and bakers' yeasts are SACCHAROMYCES CEREVISIAE; therapeutic dried yeast is YEAST, DRIED.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)
A set of protein subcomplexes involved in PROTEIN SORTING of UBIQUITINATED PROTEINS into intraluminal vesicles of MULTIVESICULAR BODIES and in membrane scission during formation of intraluminal vesicles, during the final step of CYTOKINESIS, and during the budding of enveloped viruses. The ESCRT machinery is comprised of the protein products of Class E vacuolar protein sorting genes.
Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.
A signal transducing tumor necrosis factor receptor associated factor that is involved in regulation of NF-KAPPA B signalling and activation of JNK MITOGEN-ACTIVATED PROTEIN KINASES.
IMMUNOGLOBULINS on the surface of B-LYMPHOCYTES. Their MESSENGER RNA contains an EXON with a membrane spanning sequence, producing immunoglobulins in the form of type I transmembrane proteins as opposed to secreted immunoglobulins (ANTIBODIES) which do not contain the membrane spanning segment.
The systematic study of the complete complement of proteins (PROTEOME) of organisms.
Orientation of intracellular structures especially with respect to the apical and basolateral domains of the plasma membrane. Polarized cells must direct proteins from the Golgi apparatus to the appropriate domain since tight junctions prevent proteins from diffusing between the two domains.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
A protein complex comprised of COATOMER PROTEIN and ADP RIBOSYLATION FACTOR 1. It is involved in transport of vesicles between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
The heavy chain subunits of clathrin.
One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.
A class of cellular receptors that have an intrinsic PROTEIN-TYROSINE KINASE activity.
Surface ligands that mediate cell-to-cell adhesion and function in the assembly and interconnection of the vertebrate nervous system. These molecules promote cell adhesion via a homophilic mechanism. These are not to be confused with NEURAL CELL ADHESION MOLECULES, now known to be expressed in a variety of tissues and cell types in addition to nervous tissue.
The rate dynamics in chemical or physical systems.
DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.
A pattern recognition receptor that forms heterodimers with other TOLL-LIKE RECEPTORS. It interacts with multiple ligands including PEPTIDOGLYCAN, bacterial LIPOPROTEINS, lipoarabinomannan, and a variety of PORINS.
An ATP-dependent protease found in prokaryotes, CHLOROPLASTS, and MITOCHONDRIA. It is a soluble multisubunit complex that plays a role in the degradation of many abnormal proteins.
A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus.
Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.
A negative regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins.
The capacity of a normal organism to remain unaffected by microorganisms and their toxins. It results from the presence of naturally occurring ANTI-INFECTIVE AGENTS, constitutional factors such as BODY TEMPERATURE and immediate acting immune cells such as NATURAL KILLER CELLS.
A subtype of non-receptor protein tyrosine phosphatases that contain two SRC HOMOLOGY DOMAINS. Mutations in the gene for protein tyrosine phosphatase, non-receptor type 11 are associated with NOONAN SYNDROME.
A cell surface receptor involved in regulation of cell growth and differentiation. It is specific for EPIDERMAL GROWTH FACTOR and EGF-related peptides including TRANSFORMING GROWTH FACTOR ALPHA; AMPHIREGULIN; and HEPARIN-BINDING EGF-LIKE GROWTH FACTOR. The binding of ligand to the receptor causes activation of its intrinsic tyrosine kinase activity and rapid internalization of the receptor-ligand complex into the cell.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
An intracellular signaling system involving the MAP kinase cascades (three-membered protein kinase cascades). Various upstream activators, which act in response to extracellular stimuli, trigger the cascades by activating the first member of a cascade, MAP KINASE KINASE KINASES; (MAPKKKs). Activated MAPKKKs phosphorylate MITOGEN-ACTIVATED PROTEIN KINASE KINASES which in turn phosphorylate the MITOGEN-ACTIVATED PROTEIN KINASES; (MAPKs). The MAPKs then act on various downstream targets to affect gene expression. In mammals, there are several distinct MAP kinase pathways including the ERK (extracellular signal-regulated kinase) pathway, the SAPK/JNK (stress-activated protein kinase/c-jun kinase) pathway, and the p38 kinase pathway. There is some sharing of components among the pathways depending on which stimulus originates activation of the cascade.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Src-family kinases that associate with T-CELL ANTIGEN RECEPTOR and phosphorylate a wide variety of intracellular signaling molecules.
An anchoring junction of the cell to a non-cellular substrate. It is composed of a specialized area of the plasma membrane where bundles of the ACTIN CYTOSKELETON terminate and attach to the transmembrane linkers, INTEGRINS, which in turn attach through their extracellular domains to EXTRACELLULAR MATRIX PROTEINS.
Detergent-insoluble CELL MEMBRANE components. They are enriched in SPHINGOLIPIDS and CHOLESTEROL and clustered with glycosyl-phosphatidylinositol (GPI)-anchored proteins.

Phosphorylation of the medium chain subunit of the AP-2 adaptor complex does not influence its interaction with the tyrosine based internalisation motif of TGN38. (1/337)

Tyrosine based motifs conforming to the consensus YXXphi (where phi represents a bulky hydrophobic residue) have been shown to interact with the medium chain subunit of clathrin adaptor complexes. These medium chains are targets for phosphorylation by a kinase activity associated with clathrin coated vesicles. We have used the clathrin coated vesicle associated kinase activity to specifically phosphorylate a soluble recombinant fusion protein of mu2, the medium chain subunit of the plasma membrane associated adaptor protein complex AP-2. We have tested whether this phosphorylation has any effect on the interaction of mu2 with the tyrosine based motif containing protein, TGN38, that has previously been shown to interact with mu2. Phosphorylation of mu2 was shown to have no significant effect on the in vitro interaction of mu2 with the cytosolic domain of TGN38, indicating that reversible phosphorylation of mu2 does not play a role in regulating its direct interaction with tyrosine based internalisation motifs. In addition, although a casein kinase II-like activity has been shown to be associated with clathrin coated vesicles, we show that mu2 is not phosphorylated by casein kinase II implying that another kinase activity is present in clathrin coated vesicles. Furthermore the kinase activity associated with clathrin coated vesicles was shown to be capable of phosphorylating dynamin 1. Phosphorylation of dynamin 1 has previously been shown to regulate its interaction with other proteins involved in clathrin mediated endocytosis.  (+info)

Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant mu2 subunit and its effects on endocytosis. (2/337)

Although interactions between the mu2 subunit of the clathrin adaptor protein complex AP-2 and tyrosine-based internalization motifs have been implicated in the selective recruitment of cargo molecules into coated pits, the functional significance of this interaction for endocytosis of many types of membrane proteins remains unclear. To analyze the function of mu2-receptor interactions, we constructed an epitope-tagged mu2 that incorporates into AP-2 and is targeted to coated pits. Mutational analysis revealed that Asp176 and Trp421 of mu2 are involved in the interaction with internalization motifs of TGN38 and epidermal growth factor (EGF) receptor. Inducible overexpression of mutant mu2, in which these two residues were changed to alanines, resulted in metabolic replacement of endogenous mu2 in AP-2 complexes and complete abrogation of AP-2 interaction with the tyrosine-based internalization motifs. As a consequence, endocytosis of the transferrin receptor was severely impaired. In contrast, internalization of the EGF receptor was not affected. These results demonstrate the potential usefulness of the dominant-interfering approach for functional analysis of the adaptor protein family, and indicate that clathrin-mediated endocytosis may proceed in both a mu2-dependent and -independent manner.  (+info)

Splice variants of intersectin are components of the endocytic machinery in neurons and nonneuronal cells. (3/337)

We recently identified and cloned intersectin, a protein containing two Eps15 homology (EH) domains and five Src homology 3 (SH3) domains. Using a newly developed intersectin antibody, we demonstrate that endogenous COS-7 cell intersectin localizes to clathrin-coated pits, and transfection studies suggest that the EH domains may direct this localization. Through alternative splicing in a stop codon, a long form of intersectin is generated with a C-terminal extension containing Dbl homology (DH), pleckstrin homology (PH), and C2 domains. Western blots reveal that the long form of intersectin is expressed specifically in neurons, whereas the short isoform is expressed at lower levels in glia and other nonneuronal cells. Immunofluorescence analysis of cultured hippocampal neurons reveals that intersectin is found at the plasma membrane where it is co-localized with clathrin. Ibp2, a protein identified based on its interactions with the EH domains of intersectin, binds to clathrin through the N terminus of the heavy chain, suggesting a mechanism for the localization of intersectin at clathrin-coated pits. Ibp2 also binds to the clathrin adaptor AP2, and antibodies against intersectin co-immunoprecipitate clathrin, AP2, and dynamin from brain extracts. These data suggest that the long and short forms of intersectin are components of the endocytic machinery in neurons and nonneuronal cells.  (+info)

A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain. (4/337)

The alpha subunit of the endocytotic AP2 adaptor complex contains a 30 kDa "appendage" domain, which is joined to the rest of the protein via a flexible linker. The 1.9 A resolution crystal structure of this domain reveals a single binding site for its ligands, which include amphiphysin, Eps15, and epsin. This domain when overexpressed in COS7 fibroblasts is shown to inhibit transferrin uptake, whereas mutants in which interactions with its binding partners are abolished do not. DPF/W motifs present in appendage domain-binding partners are shown to play a crucial role in their interactions with the domain. A single site for binding multiple ligands would allow for temporal and spatial regulation in the recruitment of components of the endocytic machinery.  (+info)

Dynamin-dependent endocytosis of ionotropic glutamate receptors. (5/337)

Little is known about the mechanisms that regulate the number of ionotropic glutamate receptors present at excitatory synapses. Herein, we show that GluR1-containing alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors (AMPARs) are removed from the postsynaptic plasma membrane of cultured hippocampal neurons by rapid, ligand-induced endocytosis. Although endocytosis of AMPARs can be induced by high concentrations of AMPA without concomitant activation of N-methyl-D-aspartate (NMDA) receptors (NMDARs), NMDAR activation is required for detectable endocytosis induced by synaptically released glutamate. Activated AMPARs colocalize with AP2, a marker of endocytic coated pits, and endocytosis of AMPARs is blocked by biochemical inhibition of clathrin-coated pit function or overexpression of a dominant-negative mutant form of dynamin. These results establish that ionotropic receptors are regulated by dynamin-dependent endocytosis and suggest an important role of endocytic membrane trafficking in the postsynaptic modulation of neurotransmission.  (+info)

Association of AP1 adaptor complexes with GLUT4 vesicles. (6/337)

Nycodenz gradients have been used to examine the in vitro effects of GTP-(gamma)-S on adaptor complex association with GLUT4 vesicles. On addition of GTP-(gamma)-S, GLUT4 fractionates as a heavier population of vesicles, which we suggest is due to a budding or coating reaction. Under these conditions there is an increase in co-sedimentation of GLUT4 with AP1, but not with AP3. Western blotting of proteins associated with isolated GLUT4 vesicles shows the presence of high levels of AP1 and some AP3 but very little AP2 adaptor complexes. Cell free, in vitro association of the AP1 complex with GLUT4 vesicles is increased approximately 4-fold by the addition of GTP-(gamma)-S and an ATP regenerating system. Following GTP-(gamma)-S treatment in vitro, ARF is also recruited to GLUT4 vesicles, and the temperature dependence of ARF recruitment closely parallels that of AP1. The recruitment of both AP1 and ARF are partially blocked by brefeldin A. These data demonstrate that the coating of GLUT4 vesicles can be studied in isolated cell-free fractions. Furthermore, at least two distinct adaptor complexes can associate with the GLUT4 vesicles and it is likely that these adaptors are involved in mediating distinct intracellular sorting events at the level of TGN and endosomes.  (+info)

The leucine-based sorting motifs in the cytoplasmic domain of the invariant chain are recognized by the clathrin adaptors AP1 and AP2 and their medium chains. (7/337)

Recognition of sorting signals within the cytoplasmic tail of membrane proteins by adaptor protein complexes is a crucial step in membrane protein sorting. The three known adaptor complexes, AP1, AP2, and AP3, have all been shown to recognize tyrosine- and leucine-based sorting signals, which are the most common sorting signals within membrane protein cytoplasmic tails. Although tyrosine-based signals are recognized by the micro-chains of adaptor complexes, the subunit recognizing leucine-based sorting signals is less clear. In this report we show by surface plasmon resonance that the two leucine-based sorting signals within the cytoplasmic tail of the invariant chain bind independently from each other to AP1 and AP2 but not to AP3. We also show that both motifs can be recognized by the micro-chains of AP1 and AP2. Moreover, by using monomeric as well as trimeric invariant chain constructs, we show that adaptor binding does not require trimerization of the invariant chain.  (+info)

Internalization of proximal tubular type II Na-P(i) cotransporter by PTH: immunogold electron microscopy. (8/337)

Physiological/pathophysiological alterations in proximal tubular P(i) reabsorption are associated with an altered brush-border membrane (BBM) expression of type II Na-P(i) cotransporter molecules. Reduction is achieved by an internalization and lysosomal degradation and an increase in P(i) reabsorption by new synthesis and BBM insertion of type II Na-P(i) cotransporters. In the present study, we investigated by immunohistochemistry and immunogold electron microscopy the routing of internalized rat type II Na-P(i) cotransporters (NaPi-2). In kidney of rats on a chronic low-P(i) diet, NaPi-2 is mainly localized in the BBM, in cisterns of the Golgi apparatus and sparsely also in large endocytotic vacuoles and lysosomes. Fifteen minutes after the injection of the 1-34 analog of parathyroid hormone (PTH), the amount of NaPi-2 was decreased in the BBM and increased in endocytotic vesicles. NaPi-2 molecules colocalized with horseradish peroxidase injected prior to the injection of PTH. Vesicles labeled for NaPi-2 were occasionally also labeled for clathrin or the adaptor protein AP2. We conclude that NaPi-2 molecules enter the subapical compartment from where NaPi-2-containing vesicles are segregated off and directed to the lysosomes. A clathrin-mediated pathway may contribute to the PTH-induced internalization of NaPi-2.  (+info)

The AP-complex family (Boehm and Bonifacino, 2001; Nakatsu and Ohno, 2003; Owen et al., 2004; Robinson, 2004) has six members in mammals. AP-1A, AP-2, AP-3A and AP-4 are ubiquitously expressed. The other two members, AP-5 and AP-6, are cell-type-specific isoforms of AP-1A and AP-3A: the epithelium-specific AP-1B and the neuron-restricted AP-3B.. The AP complexes consist of four subunits: one small (σ1-σ4), one medium (μ1-μ4) and two large (α, γ, δ or ϵ; and β1-β4) subunits. These assemble to form a structure in which two appendage domains are connected by flexible hinge regions to the core (Owen et al., 2004; Owen and Luzio, 2000; Robinson, 2004). The large subunits are divided into three domains: the N-terminal domain, which makes up the core with the μ and σ subunits; the hinge domain, and the C-terminal appendage. One of the large subunits (α, γ, δ or ϵ) is implicated in binding to the target membrane (Collins et al., 2002; Nakatsu and Ohno, 2003; Owen et al., 2004; Traub, ...
AP1S3_HUMAN] Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. Involved in TLR3 trafficking (PubMed:24791904).[1] [AP1G1_MOUSE] Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. [BST2_HUMAN] IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell ...
Stonins are a small family of evolutionarily conserved clathrin adaptor complex AP-2mu-related factors that may act as cargo-specific sorting adaptors in endocytosis and perhaps beyond. Whereas little is known about the localization and function of stonin 1, recent work suggests that stonin 2 serves …
The protein encoded by this gene is the medium chain of the trans-Golgi network clathrin-associated protein complex AP-1. The other components of this complex are beta-prime-adaptin, gamma-adaptin, and the small chain AP1S1. This complex is located at the…
Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
Current scientific tests which include ours, discovered a novel role of Rho3 in the Golgi/ endosomal trafficking, partly through bodily and/or purposeful conversation with the clathrin-associated adaptor protein-1 (AP-1) intricate and Cdc42 in fission yeast [9,10]. We also confirmed that the AP-1 complex mutant strains confirmed flaws in Golgi/ endosomal trafficking, secretion and vacuole fusion [eleven,twelve] and that Sip1, the AP-one accent recruits the AP-1 complicated to the Golgi/endosomes by figuring out the sip1-i4 mutant allele, which abolished the endosomal localization of the AP-1 complicated [13]. Sip1 is a homolog of Laa1 in the budding yeast [fourteen] and p200 in increased eukaryotes [fifteen], the two of which belong to the rising family members of AP-1 interacting associates. To realize the molecular operate of the AP-one accessory protein and elucidate the pathways interacting with Sip1/AP-one-mediated trafficking, we screened for the multi-duplicate suppressor of the ... is the marketplace for research antibodies. Find the right antibody for your research needs. Phosphorylation of the AP2 mu subunit by AAK1 mediates high affinity binding to membrane protein sorting signals. is the marketplace for research antibodies. Find the right antibody for your research needs. Phosphorylation of the AP2 mu subunit by AAK1 mediates high affinity binding to membrane protein sorting signals.
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TY - JOUR. T1 - Inhibition of the interaction between tyrosine-based motifs and the medium chain subunit of the AP-2 adaptor complex by specific tyrphostins. AU - Crump, CM. AU - Williams, JL. AU - Stephens, DJ. AU - Banting, G. PY - 1998. Y1 - 1998. M3 - Article (Academic Journal). VL - 273. SP - 28073. EP - 28077. JO - Journal of Biological Chemistry. JF - Journal of Biological Chemistry. SN - 0021-9258. ER - ...
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Function: Phosphorylates the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2). May play a role in regulating aspects of clathrin-mediated endocytosis (By similarity ...
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Toxoplasma gondii possesses a highly polarized secretory system, which efficiently assembles de novo micronemes and rhoptries during parasite replication. These apical secretory organelles release their contents into host cells promoting parasite invasion and survival. Using a CreLox-based inducible knock-out strategy and the ddFKBP over-expression system, we unraveled novel functions of the clathrin adaptor complex TgAP1. First, our data indicate that AP1 in T. gondii likely functions as a conserved heterotetrameric complex composed of the four subunits γ, β, μ1, σ1 and interacts with known regulators of clathrin-mediated vesicular budding such as the unique ENTH-domain containing protein, which we named Epsin-like protein (TgEpsL). Disruption of the μ1 subunit resulted in the mis-sorting of microneme proteins at the level of the Trans-Golgi-Network (TGN). Furthermore, we demonstrated that TgAP1 regulates rhoptry biogenesis by activating rhoptry protein exit from the TGN, but also ...
In the present work, we have investigated mechanisms involved in the nucleotide-dependent regulation of clathrin-coated pit nucleation at the synapse. Our results implicate ARF6 in this process and demonstrate two effects of the GTP-bound form of this small GTPase; stimulation of the recruitment of clathrin/AP-2 to presynaptic membranes and binding plus activation of PIPKIγ. They also suggest that the two effects are related and that PI(4,5)P2 production by PIPKIγ stimulation represents the major mechanism through which ARF6 enhances clathrin/AP-2 recruitment. The action of GTP-ARF6 on clathrin/AP-2 recruitment mimics the effect of GTPγs, and its effects are antagonized by experimental manipulations that prevent either ARF activation (i.e., dominant-negative ARF6) or PI(4,5)P2 production and availability (i.e., kinase inhibition, PIPKIγ depletion, and PI(4,5)P2 hydrolysis by synaptojanins inositol 5′-phosphatase domain). These results strongly indicate that enhanced clathrin coat ...
The heterotetrameric adaptor protein complex AP2 is one of the best-studied components of the endocytic machinery. The AP2 complex consists of four different subunits, α, β2, σ2, and μ2, which assemble into a core domain with two appendages (Fig. 2; Collins et al., 2002; Jackson et al., 2010). AP2 has multiple binding partners, including phosphatidylinositol 4,5-bisphosphate (PIP2), clathrin, several endocytic accessory proteins, and two signaling motifs present on some cargo receptors (see Traub, 2009 for a detailed review). The AP2 complex has classically been considered to be the master initiator of clathrin-mediated endocytosis through its role in recruiting clathrin molecules to the membrane. However, several lines of evidence question this idea.. If the AP2 complex has an essential role in initiation then its presence would be required for the formation of endocytic sites. However, in yeast the endocytosis of mating pheromone α-factor is unaffected in strains lacking functional AP2 ...
Proteins internalized at the cell surface by clathrin-mediated endocytosis contain specific sorting sequences that bind to the internalization machinery. The best characterized of these is the tyrosine-based YXXΦ motif (in which X is any residue and Φ is a bulky, hydrophobic residue). This binds to a specific region in the μ2 subunit of the AP2 clathrin adaptor protein, and structural studies have shown that the spacing between the Y and Φ residues is crucial. Ruth Murrell and co-workers now unveil a novel type of tyrosine-based endocytic motif (p. 3073). They have used site-directed mutagenesis and CD8-based chimeras to analyse endocytosis of P2X4 receptors, ATP-gated cation channels that rapidly cycle off the plasma membrane. These receptors possess consensus YXXΦ motifs, but surprisingly these are inaccessible to AP2 and not needed for endocytosis. Instead, the authors show, a downstream YXXGΦ motif is required. Determining the structure of a YXXGΦ-μ2 complex, they demonstrate that ...
The KOMP Repository is located at the University of California Davis and Childrens Hospital Oakland Research Institute. Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International +1-530-752-KOMP, or for vectors [email protected] or +1-510-450-7917 ...
To obtain insights into the mechanism by which FCHo2 couples CCP growth and lifetime in CME, we analyzed the nanoscale localization of FCHo2 at CCPs. Dual-color SD-dSTORM (spectral demixing direct stochastic optical reconstruction microscopy) analysis of the distribution of endogenous FCHo2 within CCPs followed by quantitative averaging of ,250 images revealed a marked concentration of FCHo2 in ring-like structures (about 225 nm in diameter) at the outer rim of CCPs [consistent with (27)] while being largely absent from the CCP center (Fig. 3, D and E) that eventually gives rise to the dome as CCPs invaginate. Hence, FCHo2 selectively accumulates at the rim of CCPs, consistent with its early role in coupling CCP growth and dynamics.. Different models have been proposed regarding the early endocytic function of FCHo2. According to one model, FCHo2 nucleates CCPs by acting as a plasma membrane-associated recruitment hub for early-acting endocytic proteins bound to its μ-homology domain (20). This ...
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Most difficulties in working with Micro-Manager arise from configuring the system and from problems/issues with specific devices. In both of these cases you are interacting mainly with device adapters. These device adapters have been written by several different authors, all behave slightly differently, and interact with specific hardware that has its own peculiarities. On these pages we will maintain as much information as possible about Micro-Manager device adapters. This will help you configure and understand your Micro-Manager system. We hope that the authors of the device adapters will maintain this information, but please feel free to update the information here with your own experiences. The information here will refer to the most recent Micro-Manager release. ...
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During clathrin-mediated endocytosis, it has been thought that the sensing and binding of the clathrin adaptor protein AP2 to cargo and lipids leads to the recruitment of clathrin, nucleating the formation of a clathrin-coated pit. Henne et al. have now found that this process of AP2 binding may not in fact represent either the first or the nucleation event of endocytosis. Instead, ubiquitous proteins called FCHo1/2 (F-BAR proteins) bind to the plasma membrane and define the sites of endocytosis independently of AP2. The F-BAR protein can generate very low curvatures and, at higher concentrations, generates higher curvatures like those required at the neck of budding vesicles. The C terminus of the protein has a μ-homology domain (with homology to the μ domain of the AP2 complex) that interacts with Eps15 and intersectin and via these proteins recruits AP2, which further recruits clathrin. Thus, a curvature-inducing protein can act to nucleate clathrin-coated pit assembly during ...
Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity.
2014 Project discussion}} ,br> --[[User:Z8600021,Mark Hill]] ([[User talk:Z8600021,talk]]) 16:49, 20 March 2014 (EST) --[[User:Z3399239,Z3399239]] ([[User talk:Z3399239,talk]]) 16:49, 20 March 2014 (EST) --[[User:Z3420257,Z3420257]] ([[User talk:Z3420257,talk]]) 16:49, 20 March 2014 (EST) --[[User:Z3373930,Z3373930]] ([[User talk:Z3373930,talk]]) 16:50, 20 March 2014 (EST) Hello dear colleagues. Is anyone else interested in doing into the cell from the plasma membrane (Endocytosis)? --[[User:Z3399239,Z3399239]] ([[User talk:Z3399239,talk]]) 16:52, 20 March 2014 (EST) And if not Endocytosis would anyone be interested in doing from the trans Golgi network to the cell exterior (Exocytosis) ? --[[User:Z3399239,Z3399239]] ([[User talk:Z3399239,talk]]) 12:58, 27 March 2014 (EST) So would z3373930 research: CLIC/GEEC endocytic pathway and arf6-dependent endocytosis and z3420257 research: flotillin-dependent endocytosis and macropinocytosis and z3375490 research: circular doral ruffles and ...
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říj 09 6:45:21: There are no TAP-Windows adapters on this system. You should be able to create a TAP-Windows adapter by going to Start -, All Programs -, TAP-Windows -, Utilities -, Add a new TAP-Windows virtual ethernet adapter ...
You might not know this, but life as you once knew it is over. No, were not talking about crises economic or environmental, the Red Menace, or the count down t...
"Entrez Gene: AP1S1 adaptor-related protein complex 1, sigma 1 subunit". Montpetit A, Côté S, Brustein E, Drouin CA, Lapointe L ... AP-1 complex subunit sigma-1A is a protein that in humans is encoded by the AP1S1 gene. The protein encoded by this gene is ... Boehm M, Aguilar RC, Bonifacino JS (Nov 2001). "Functional and physical interactions of the adaptor protein complex AP-4 with ... "HIV-1 Nef stabilizes the association of adaptor protein complexes with membranes". The Journal of Biological Chemistry. 278 (10 ...
The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. Two ... "Entrez Gene: AP1G1 adaptor-related protein complex 1, gamma 1 subunit". Fölsch H, Ohno H, Bonifacino JS, Mellman I (Oct 1999 ... and 3 ADP-ribosylation factors with adaptor protein complexes 1 and 3". Biochemistry. 41 (14): 4669-77. doi:10.1021/bi016064j. ... "Interactions between adaptor protein-1 of the clathrin coat and microtubules via type 1a microtubule-associated proteins". The ...
The protein encoded by this gene is a member of the X11 protein family. It is a neuronal adaptor protein that interacts with ... "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 ... "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 ... It is also regarded as a putative vesicular trafficking protein in the brain that can form a complex with the potential to ...
"Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 ... Maximov A, Südhof TC, Bezprozvanny I (1999). "Association of neuronal calcium channels with modular adaptor proteins". J. Biol ... This protein is a multidomain scaffolding protein with a role in synaptic transmembrane protein anchoring and ion channel ... "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 ...
... adaptor protein (AP) complexes, and alternative adaptors. Her working hypothesis is that for each trafficking pathway, there ... "The Fifth Adaptor Protein Complex". PLOS Biology. 9 (10): e1001170. doi:10.1371/journal.pbio.1001170. PMC 3191125. PMID ... matching up machinery and cargo proteins; investigating how clathrin and adaptors are hijacked by the HIV-1-encoded protein Nef ... Robinson and her lab managed to find another AP complex, AP-3, which interacts with lysosomal membrane proteins such as LAMP1. ...
"Entrez Gene: AP3S2 adaptor-related protein complex 3, sigma 2 subunit". CS1 maint: discouraged parameter (link) Dell'Angelica, ... Dell'Angelica EC, Ohno H, Ooi CE, Rabinovich E, Roche KW, Bonifacino JS (Apr 1997). "AP-3: an adaptor-like protein complex with ... 2003). "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1". Dev. Cell. 5 (3): 513-21. doi:10.1016/ ... 2002). "Role of adaptor complex AP-3 in targeting wild-type and mutated CD63 to lysosomes". Mol. Biol. Cell. 13 (3): 1071-82. ...
"Entrez Gene: AP3B2 adaptor-related protein complex 3, beta 2 subunit". Human AP3B2 genome location and AP3B2 gene details page ... 1997). "AP-3: an adaptor-like protein complex with ubiquitous expression". EMBO J. 16 (5): 917-28. doi:10.1093/emboj/16.5.917. ... Dell'Angelica EC, Klumperman J, Stoorvogel W, Bonifacino JS (1998). "Association of the AP-3 adaptor complex with clathrin". ... AP-3 complex subunit beta-2 is a protein that in humans is encoded by the AP3B2 gene. GRCh38: Ensembl release 89: ...
The protein encoded by this gene is one of two large chain components of the AP2 adaptor complex, which serves to link clathrin ... "Entrez Gene: AP2B1 adaptor-related protein complex 2, beta 1 subunit". Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, ... He G, Gupta S, Yi M, Michaely P, Hobbs HH, Cohen JC (Nov 2002). "ARH is a modular adaptor protein that interacts with the LDL ... He G, Gupta S, Yi M, Michaely P, Hobbs HH, Cohen JC (Nov 2002). "ARH is a modular adaptor protein that interacts with the LDL ...
"Entrez Gene: AP2M1 adaptor-related protein complex 2, mu 1 subunit". Follows ER, McPheat JC, Minshull C, Moore NC, Pauptit RA, ... which belongs to the adaptor complexes medium subunits family. The encoded protein is required for the activity of a vacuolar ... Diviani D, Lattion AL, Abuin L, Staub O, Cotecchia S (May 2003). "The adaptor complex 2 directly interacts with the alpha 1b- ... Zhang Y, Allison JP (Aug 1997). "Interaction of CTLA-4 with AP50, a clathrin-coated pit adaptor protein". Proceedings of the ...
The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. This ... "Entrez Gene: AP1G2 adaptor-related protein complex 1, gamma 2 subunit". Rost, Martina; Döring Tatjana; Prange Reinhild (Nov ... 2003). "HIV-1 Nef stabilizes the association of adaptor protein complexes with membranes". J. Biol. Chem. 278 (10): 8725-32. ... 2005). "Leucine-specific, functional interactions between human immunodeficiency virus type 1 Nef and adaptor protein complexes ...
"Entrez Gene: AP2A2 adaptor-related protein complex 2, alpha 2 subunit". Chen H, Fre S, Slepnev VI, Capua MR, Takei K, Butler MH ... the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes ... "Interaction of Shc with adaptor protein adaptins". The Journal of Biological Chemistry. 271 (9): 5265-9. doi:10.1074/jbc.271.9. ... "Interaction of Shc with adaptor protein adaptins". The Journal of Biological Chemistry. 271 (9): 5265-9. doi:10.1074/jbc.271.9. ...
"Entrez Gene: AP3B1 adaptor-related protein complex 3, beta 1 subunit". GeneReviews/NCBI/NIH/UW entry on Hermansky-Pudlak ... The encoded protein is part of the heterotetrameric AP-3 protein complex which interacts with the scaffolding protein clathrin ... AP-3 complex subunit beta-1 is a protein that in humans is encoded by the AP3B1 gene. This gene encodes a protein that may play ... Simpson F, Peden AA, Christopoulou L, Robinson MS (May 1997). "Characterization of the adaptor-related protein complex, AP-3". ...
This gene encodes a subunit of the heterotetrameric adaptor-related protein complex 1 (AP-1), which belongs to the adaptor ... "Entrez Gene: AP1M2 adaptor-related protein complex 1, mu 2 subunit". Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot ... Fölsch H, Pypaert M, Schu P, Mellman I (Feb 2001). "Distribution and function of AP-1 clathrin adaptor complexes in polarized ... Fölsch H, Ohno H, Bonifacino JS, Mellman I (Oct 1999). "A novel clathrin adaptor complex mediates basolateral targeting in ...
Adaptor protein complex 1 is found at the cytoplasmic face of coated vesicles located at the Golgi complex, where it mediates ... "Entrez Gene: AP1S2 adaptor-related protein complex 1, sigma 2 subunit". Huo L, Teng Z, Wang H, Liu X (March 2019). "A novel ... The protein encoded by this gene serves as the small subunit of this complex and is a member of the adaptin protein family. ... March 2003). "HIV-1 Nef stabilizes the association of adaptor protein complexes with membranes". The Journal of Biological ...
"Entrez Gene: AP1M1 adaptor-related protein complex 1, mu 1 subunit". Hinners I, Wendler F, Fei H, Thomas L, Thomas G, Tooze SA ... AP-1 complex subunit mu-1 is a protein that in humans is encoded by the AP1M1 gene. The protein encoded by this gene is the ... Fölsch H, Ohno H, Bonifacino JS, Mellman I (Oct 1999). "A novel clathrin adaptor complex mediates basolateral targeting in ... Fölsch H, Ohno H, Bonifacino JS, Mellman I (Oct 1999). "A novel clathrin adaptor complex mediates basolateral targeting in ...
AP-3 complex subunit delta-1 is a protein that in humans is encoded by the AP3D1 gene. AP3D1 is a subunit of the AP3 adaptor- ... "Entrez Gene: AP3D1 adaptor-related protein complex 3, delta 1 subunit". CS1 maint: discouraged parameter (link) Martinez-Arca S ... Simpson F, Peden AA, Christopoulou L, Robinson MS (May 1997). "Characterization of the adaptor-related protein complex, AP-3". ... "Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based sorting ...
"Entrez Gene: AP3S1 adaptor-related protein complex 3, sigma 1 subunit". Human AP3S1 genome location and AP3S1 gene details page ... Dell'Angelica EC, Ohno H, Ooi CE, Rabinovich E, Roche KW, Bonifacino JS (March 1997). "AP-3: an adaptor-like protein complex ... Simpson F, Peden AA, Christopoulou L, Robinson MS (May 1997). "Characterization of the adaptor-related protein complex, AP-3". ... "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1". Developmental Cell. 5 (3): 513-21. doi:10.1016/ ...
"Entrez Gene: APPL2 adaptor protein, phosphotyrosine interaction, PH domain and leucine zipper containing 2". "Salmonella ... Akt2 and FOXO1a Interact with FSHR in a Potential Signaling Complex". Mol Cell Endocrinol. 260-262: 93-9. doi:10.1016/j.mce. ... DCC-interacting protein 13-beta is a protein that in humans is encoded by the APPL2 gene. Model organisms have been used in the ... 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. doi:10.1038 ...
2000). "Regulation of complex formation of POB1/epsin/adaptor protein complex 2 by mitotic phosphorylation". J. Biol. Chem. 275 ... EPN1 is an endocytic accessory protein that interacts with EPS15 (MIM 600051), the alpha subunit of the clathrin adaptor AP2 ( ... Timsit YE, Miller SL, Mohney RP, O'Bryan JP (2005). "The U-box ligase carboxyl-terminus of Hsc 70-interacting protein ... Epsin-1 is a protein that in humans is encoded by the EPN1 gene. ... as well as with other accessory proteins for the endocytosis of ...
Adaptor protein complex 1 is found on the cytoplasmic face of vesicles located at the Golgi complex, where it mediates both the ... "Entrez Gene: AP1S2 adaptor-related protein complex 1, sigma 2 subunit". Piccini M, Vitelli F, Bruttini M, Pober BR, Jonsson JJ ... This nucleolar protein is involved in the processing and modification of tRNA. GDI1: RabGDI alpha makes a complex with ... All AFF proteins are localized in the nucleus and have a role as transcriptional activators with a positive action on RNA ...
"Entrez Gene: AP2S1 adaptor-related protein complex 2, sigma 1 subunit". Pearse BM, Smith CJ, Owen DJ (2000). "Clathrin coat ... "A novel spliced transcript of human CLAPS2 encoding a protein alternative to clathrin adaptor protein AP17". Gene. 220 (1-2): ... One of two major clathrin-associated adaptor complexes, AP-2, is a heterotetramer which is associated with the plasma membrane ... 1991). "AP17 and AP19, the mammalian small chains of the clathrin-associated protein complexes show homology to Yap17p, their ...
... has been shown to interact with CRMP1, Adaptor-related protein complex 2, alpha 1 and NUMB. GRCh38: Ensembl release 89: ... Dihydropyrimidinase-related protein 2 is an enzyme that in humans is encoded by the DPYSL2 gene. ... 2003). "p80 ROKalpha binding protein is a novel splice variant of CRMP-1 which associates with CRMP-2 and modulates RhoA- ... Gu Y, Ihara Y (2000). "Evidence that collapsin response mediator protein-2 is involved in the dynamics of microtubules". J. ...
Journal of Immunology, 2006 PMID 17056525 HIV Nef-mediated CD4 down-regulation is adaptor protein complex 2 dependent. Jin YJ, ... protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness. ... cell age reduces effector activity but preserves proliferative capacity in a murine allogeneic major histocompatibility complex ...
Guo Y, Zanetti G, Schekman R (January 2013). "A novel GTP-binding protein-adaptor protein complex responsible for export of ... The protein encoded by the VANGL2 gene is a membrane protein involved in the regulation of planar cell polarity, especially in ... The encoded protein transmits directional signals to individual cells or groups of cells in epithelial sheets. This protein is ... "Entrez Gene: VANGL planar cell polarity protein 2". Retrieved 2018-07-05. Erdal E, Erdal C, Bulut G, Kunter I, Kir M, Atabey N ...
This gene encodes a protein which interacts with clathrin and adaptor-related protein complex 2, alpha 1 subunit. The protein ... 1998). "Intersectin, a novel adaptor protein with two Eps15 homology and five Src homology 3 domains". J. Biol. Chem. 273 (47 ... 1997). "Binding specificity and in vivo targets of the EH domain, a novel protein-protein interaction module". Genes Dev. 11 ( ... "The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module". J ...
The encoded protein belongs to the adaptor complexes medium subunits family. This AP-4 complex is involved in the recognition ... "Entrez Gene: AP4M1 adaptor-related protein complex 4, mu 1 subunit". Hirst J, Bright NA, Rous B, Robinson MS (August 1999). " ... Dell'Angelica EC, Mullins C, Bonifacino JS (Apr 1999). "AP-4, a novel protein complex related to clathrin adaptors". J Biol ... Hirst J, Bright NA, Rous B, Robinson MS (1999). "Characterization of a Fourth Adaptor-related Protein Complex". Mol. Biol. Cell ...
AP-4 complex subunit beta-1 is a protein that in humans is encoded by the AP4B1 gene. The heterotetrameric adaptor protein (AP ... "Entrez Gene: AP4B1 adaptor-related protein complex 4, beta 1 subunit". Hirst J, Bright NA, Rous B, Robinson MS (August 1999). " ... Dell'Angelica EC, Mullins C, Bonifacino JS (Apr 1999). "AP-4, a novel protein complex related to clathrin adaptors". J Biol ... 2001). "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using ...
AP-4 complex subunit sigma-1 is a protein that in humans is encoded by the AP4S1 gene. The heterotetrameric adaptor protein (AP ... "Entrez Gene: adaptor-related protein complex 4". CS1 maint: discouraged parameter (link) Abou Jamra R, Philippe O, Raas- ... Hirst J, Bright NA, Rous B, Robinson MS (1999). "Characterization of a fourth adaptor-related protein complex". Mol. Biol. Cell ... Dell'Angelica EC, Mullins C, Bonifacino JS (1999). "AP-4, a novel protein complex related to clathrin adaptors". J. Biol. Chem ...
AP-4 complex subunit epsilon-1 is a protein that in humans is encoded by the AP4E1 gene. The heterotetrameric adaptor protein ( ... "Entrez Gene: adaptor-related protein complex 4". Abou Jamra R, Philippe O, Raas-Rothschild A, Eck SH, Graf E, Buchert R, Borck ... Hirst J, Bright NA, Rous B, Robinson MS (1999). "Characterization of a fourth adaptor-related protein complex". Mol. Biol. Cell ... Boehm M, Aguilar RC, Bonifacino JS (2001). "Functional and physical interactions of the adaptor protein complex AP-4 with ADP- ...
2001). "The Shc-related adaptor protein, Sck, forms a complex with the vascular-endothelial-growth-factor receptor KDR in ... "The Shc-related adaptor protein, Sck, forms a complex with the vascular-endothelial-growth-factor receptor KDR in transfected ... SHC-transforming protein 2 is a protein that in humans is encoded by the SHC2 gene. SHC2 has been shown to interact with Kinase ... Nakamura T; Muraoka S; Sanokawa R; Mori N (Apr 1998). "N-Shc and Sck, two neuronally expressed Shc adapter homologs. Their ...
Sedimentation Velocity Analysis of Heterogeneous Protein-Protein Interactions: Lamm Equation Modeling and Sedimentation ... The ribosomes, membranes and Golgi complexes can be separated by another technique called density gradient centrifugation. ... The rotors may come with different adapters to hold various sizes of test tubes, bottles, or microtiter plates. ... By 1900, it had been generally accepted that proteins were composed of amino acids; however, whether proteins were colloids or ...
Signal transducing adaptor proteins. *EDARADD *EDARADD Hypohidrotic ectodermal dysplasia. *SH3BP2 *Cherubism. *LDB3 *Zaspopathy ... Mutations in the RPS6KA3 disturb the function of the protein, but it is unclear how a lack of this protein causes the signs and ... The RPS6KA3 gene makes a protein that is involved with signaling within cells. Researchers believe that this protein helps ... The protein RSK2 which is encoded by the RPS6KA3 gene is a kinase which phosphorylates some substrates like CREB and histone H3 ...
Calcium channel, voltage-dependent, L type, alpha 1C subunit (also known as Cav1.2) is a protein that in humans is encoded by ... L-type voltage-gated calcium channel complex. • integral component of plasma membrane. • cell junction. • dendrite. • ... Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Apr 1996). "A "double adaptor" method for improved shotgun library ... Click on genes, proteins and metabolites below to link to respective Wikipedia articles. [§ 1] ...
... cell surface expression of SAP-binding receptor CD229 is regulated via its interaction with clathrin-associated adaptor complex ... a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 ... Lee YJ، Luisiri P، Clark MR (1996). "A novel complex, p40/42, is constitutively associated with the B cell antigen receptor and ... SLAMF6‏ (SLAM family member 6) هوَ بروتين يُشَفر بواسطة جين SLAMF6 في الإنسان.[1][2] ...
Adaptor molecules are responsible for self-assembly and recruitment. Two examples of adaptor proteins are AP180[3] and epsin.[4 ... During mitosis, clathrin binds to the spindle apparatus, in complex with two other proteins: TACC3 and ch-TOG/CKAP5. Clathrin ... In a cell, a triskelion floating in the cytoplasm binds to an adaptor protein, linking one of its feet to the membrane at a ... In a cell, clathrin triskelion in the cytoplasm binds to an adaptor protein that has bound membrane, linking one of its three ...
The assembled complex of hslV (blue) and hslU (red) from E. coli. This complex of heat shock proteins is thought to resemble ... the SCF itself is regulated by the APC via ubiquitination of the adaptor protein, Skp2, which prevents SCF activity before the ... Proteasomes are protein complexes which degrade unneeded or damaged proteins by proteolysis, a chemical reaction that breaks ... These proteins are ubiquitinated by SCFTIR1, or SCF in complex with the auxin receptor TIR1. Degradation of Aux/IAA proteins ...
Bacteria and fungi may form complex biofilms, protecting from immune cells and proteins; biofilms are present in the chronic ... In parallel, when toll-like receptors in the endocytic compartments recognize a virus the activation of the adaptor protein ... This leads to antiviral protein production, such as protein kinase R, which inhibits viral protein synthesis, or the 2′,5′- ... "Resistance" (R) proteins, encoded by R genes, are widely present in plants and detect pathogens. These proteins contain domains ...
... which is also part of a protein complex. The autophagy-inducible Beclin-1 complex[40] contains the proteins p150, Atg14L and ... and enables the docking of specific cargos and adaptor proteins such as Sequestosome-1/p62.[49] The completed autophagosome ... WIPI2, a PtdIns(3)P binding protein of the WIPI (WD-repeat protein interacting with phosphoinositides) protein family, was ... substrate/chaperone complex.[32] This complex then moves to the lysosomal membrane-bound protein that will recognise and bind ...
1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107-13. doi:10.1006/abio. ... 2009). "ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery". Mol. Biol. Cell. 20 (7): 1992-2003. doi: ... Autophagy-related protein 13 also known as ATG13 is a protein that in humans is encoded by the KIAA0652 gene. ATG13 is an ... X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 5 (3): 169-76 ...
Together, these were a prerequisite for the evolution of the most complex eukaryotic cells, from which all multicellular ... by comparing sequences of DNA or proteins. The result of a successful analysis is a hierarchy of clades - groups that share a ... "On degenerate templates and the adaptor hypothesis" (PDF). Archived from the original (PDF) on October 1, 2008. Retrieved ... Retrieved September 2, 2008.. *^ a b Cowen, R. (2000). History of Life (3rd ed.). Blackwell Science. pp. 47-50. ISBN 0-632- ...
cyclin-dependent protein kinase holoenzyme complex. • nuclear membrane. • membrane. • transcription factor complex. • ... 1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107-13. doi:10.1006/abio. ... The protein encoded by this gene is a member of the Ser/Thr protein kinase family. This protein is highly similar to the gene ... protein kinase activity. • kinase activity. • protein serine/threonine kinase activity. • cyclin-dependent protein serine/ ...
positive regulation of protein complex assembly. • protein kinase B signaling. • positive regulation of cytokine production. • ... This dissociation enables the adaptor protein TRADD to bind to the death domain, serving as a platform for subsequent protein ... positive regulation of protein complex disassembly. • regulation of cell proliferation. • cellular response to amino acid ... negative regulation of protein complex disassembly. • multicellular organism development. • negative regulation of bicellular ...
"The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck". The Journal of Biological ... SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell ... protein binding. • identical protein binding. • actin binding. • protein kinase binding. • small GTPase binding. • Rac GTPase ... "Wiskott-Aldrich syndrome protein is associated with the adapter protein Grb2 and the epidermal growth factor receptor in living ...
... and SH3 domain-containing adaptor protein that has been also shown to interact with another CAS family member, p130Cas/BCAR1, ... "Dcas supports cell polarization and cell-cell adhesion complexes in development". PLOS ONE. 5 (8): e12369. Bibcode:2010PLoSO ... "Entrez Gene: Cas scaffolding protein family member 4".. *^ a b Tikhmyanova N, Little JL, Golemis EA (April 2010). "CAS proteins ... Cas scaffolding protein family member 4 is a protein that in humans is encoded by the CASS4 gene.[5] ...
... to bind to the ITAM and activated ZAP-70 phosphorylates tyrosines on the adaptor protein LAT, which then attracts PLC-γ. Other ... The TCR complex[edit]. The TCR receptor complex is an octomeric complex of variable TCR receptor α and β chains with three ... Associated molecules of the TCR complex involved in T-cell activation[edit]. The essential function of the TCR complex is to ... UMich Orientation of Proteins in Membranes protein/pdbid-2hac - Zeta-zeta dimer of T cell receptor ...
... where sequencing adapters are added prior to bisulfite fragmentation. Instead, the adapters are added after the DNA is treated ... October 2017). "Multiplexed quantification of proteins and transcripts in single cells". Nature Biotechnology. 35 (10): 936-939 ... "Cell type atlas and lineage tree of a whole complex animal by single-cell transcriptomics". Science. 360 (6391): eaaq1723. doi ... A transposase inserts sequencing adapters directly into open regions of chromatin, allowing those regions to be amplified and ...
2002). "Mixed lineage kinase LZK forms a functional signaling complex with JIP-1, a scaffold protein of the c-Jun NH(2)- ... 2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest ... protein kinase inhibitor activity. • protein binding. • kinesin binding. • protein kinase binding. • JUN kinase binding. • ... "Entrez Gene: MAPK8IP1 mitogen-activated protein kinase 8 interacting protein 1".. *^ a b c d e f Yasuda, J; Whitmarsh A J; ...
... essential adapter proteins in TLR signaling), they were still able to induce inflammatory responses, increase T cell activation ... clippings as antigen on their cell surface by coupling them to a special receptor known as a major histocompatibility complex ( ... Medzhitov R, Preston-Hurlburt P, Janeway CA (July 1997). "A human homologue of the Drosophila Toll protein signals activation ... 154 (2): 804-13. PMID 7814884.. *^ Kashiwakura J, Yokoi H, Saito H, Okayama Y (October 2004). "T cell proliferation by direct ...
Signal transducing adaptor protein. *I-kappa B protein. *Mucin-4. *Olfactory marker protein ... GTP-binding protein regulators regulate G proteins in several different ways. Small GTPases act as molecular switches in ... and thus requires another class of regulatory proteins to accelerate this activity, the GTPase activating proteins (GAPs). ... GTP-Binding+Protein+Regulators at the US National Library of Medicine Medical Subject Headings (MeSH) ...
The adaptor molecules were eventually shown to be tRNAs and the catalytic "ribonucleic-protein complexes" became known as ... ribonucleic-protein complexes that catalyse the assembly of amino acids into proteins according to the messenger RNA ... Many molecular biologists were puzzled by the problem of the origin of a protein replicating system that is as complex as that ... DNA → RNA → Protein. Some critics thought that by using the word "dogma", Crick was implying that this was a rule that could ...
Signal transducing adaptor proteins. *EDARADD *EDARADD Hypohidrotic ectodermal dysplasia. *SH3BP2 *Cherubism. *LDB3 *Zaspopathy ... Carney complex. *PRKAG2 *Wolff-Parkinson-White syndrome. *PRKCSH *PRKCSH Polycystic liver disease ... It is often associated with Cowden syndrome.[1] It was described by Jacques Jean Lhermitte and P. Duclos in 1920.[2] ... MICROSCOPY(lhermitte-duclos disease) 1,Enlarged circumscribed cerebellar folia 2,internal granular layer is focally indistinct ...
Proteins of the major histocompatibility complex class I are endogenous negative regulators of NMDAR-mediated currents in the ... adaptor, and scaffolding proteins. ... Two specific proteins have been identified as a major pathway ... The receptor is a heteromeric complex that interacts with multiple intracellular proteins by three different subunits: GluN1, ... which contain residues that can be directly modified by a series of protein kinases and protein phosphatases, as well as ...
Protein nanopore sequencing utilizes membrane protein complexes such as α-hemolysin, MspA (Mycobacterium smegmatis Porin A) or ... MPSS was a bead-based method that used a complex approach of adapter ligation followed by adapter decoding, reading the ... a small protein secreted by the pancreas. This provided the first conclusive evidence that proteins were chemical entities with ... Sanger is one of the few scientists who was awarded two Nobel prizes, one for the sequencing of proteins, and the other for the ...
受體蛋白(英语:Template:Signal transducing adaptor proteins). *GTP-binding(英语:Template:GTP-binding protein regulators) ... López-Rodríguez ML, Murcia M, Benhamú B, Olivella M, Campillo M, Pardo L. Computational model of the complex between GR113808 ... 卷曲受体 (1(英语:FZD1), 2(英语:FZD2), 3(英语:FZD3), 4(英语:FZD4), 5(英语:FZD5), 6(英语:FZD6), 7(英语:FZD7), 8(英语:FZD8), 9(英语:FZD9), 10(英语:FZD10)) ... TAS1R(甜味) (1(英语:TAS1R1), 2(英语:TAS1R2), 3(英语:TAS1R3)) · TAS2R(苦味) (1(英语:TAS2R1), 3(英语:TAS2R3), 4(英语
"p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene". ... protein tyrosine kinase activity. • protein phosphatase binding. 細胞の構成要素. • 細胞質. • 細胞質基質. • 膜. • 焦点接着. • extrinsic component of ... positive regulation of protein phosphorylation. • regulation of cell adhesion mediated by integrin. • 胎座. • 脈管形成. • protein ... "Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions
Ensuing binding of ephrin-B3 to the cytoplasmic adaptor protein, Grb4, leads to the recruitment and binding of Dock180 and p21 ... the need to understand more complex structures becomes much more pertinent, and simpler associations formed at childhood are ... Reverse signaling between ephrin-B proteins and their Eph receptor tyrosine kinases have been found to initiate the retraction ... This suggests that pruning is triggered once the ligand reaches threshold protein levels within a few days after detectable ...
... which is facilitated by binding to adaptor proteins via protein-protein interaction motifs that are collectively referred to as ... These proteins allow caspase-1 activation by forming a multiprotein activating complex called Inflammasomes. For example, a NOD ... The adaptor protein FADD will recruit (by a Death domain-Death domain interaction) pro-Caspase 8 via the DED domain. This FasR ... Multiprotein complexes often form during caspase activation.[12] Some activating multiprotein complexes includes: *The death- ...
"EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains". Neuron. 22 (3): 511-24. doi:10.1016/ ... Stegmüller J, Werner H, Nave KA, Trotter J (2003). "The proteoglycan NG2 is complexed with alpha-amino-3-hydroxy-5-methyl-4- ... "Interaction of the ERC family of RIM-binding proteins with the liprin-alpha family of multidomain proteins". J. Biol. Chem. 278 ... GRIP2‏ (Glutamate receptor interacting protein 2) هوَ بروتين يُشَفر بواسطة جين GRIP2 في الإنسان.[1] ...
Some of the proteins that associate with HATs in these complexes function by targeting the HAT complex to nucleosomes at ... transcriptional adaptor), TFIID (transcription factor II D), TFTC (TBP-free TAF-containing complex), and NuA3/NuA4 (nucleosomal ... and it is the last protein to bind in the complex.. Histones tend to be positively charged proteins with N-terminal tails that ... structural proteins, polyamines, and proteins involved in nuclear import.[3] Acetylation of these proteins can alter their ...
... control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb". Curr. Biol. 13 (15): 1259-68. doi:10.1016 ... on growth factor receptors or adaptor proteins via the pY-X-X-M motif.[13][14] ... October 2004). "A rapid method for determining protein kinase phosphorylation specificity". Nat. Methods. 1 (1): 27-9. doi: ... Use of Oriented Peptide Libraries to determine phosphopeptide binding specificity and protein kinase substrate specificity[edit ...
Adaptor-related protein complex 2, alpha 1 has been shown to interact with DPYSL2 and NUMB. GRCh38: Ensembl release 89: ... "Entrez Gene: AP2A1 adaptor-related protein complex 2, alpha 1 subunit". Nishimura, Takashi; Fukata Yuko; Kato Katsuhiro; ... This gene encodes the alpha 1 adaptin subunit of the adaptor protein 2 (AP2 adaptors) complex found in clathrin coated vesicles ... 1996). "Interaction of Shc with adaptor protein adaptins". J. Biol. Chem. 271 (9): 5265-9. doi:10.1074/jbc.271.9.5265. PMID ...
... a virally encoded peripheral membrane protein. Nef binds to the adaptor protein (AP) complexes of coated vesicles, inducing an ... adaptor related protein complex 2 subunit beta 1provided by HGNC. Primary source. HGNC:HGNC:563 See related. Ensembl: ... AP2B1 adaptor related protein complex 2 subunit beta 1 [ Homo sapiens (human) ] Gene ID: 163, updated on 6-Jan-2019 ... adapter-related protein complex 2 subunit beta. adaptin, beta 2 (beta). adaptor protein complex AP-2 subunit beta. adaptor ...
Clat_adaptor_s; Clathrin adaptor complex small chain. cl10970. Location:154 → 423. AP_MHD_Cterm; C-terminal domain of adaptor ... Clat_adaptor_s; Clathrin adaptor complex small chain. cl10970. Location:154 → 421. AP_MHD_Cterm; C-terminal domain of adaptor ... clathrin-associated adaptor medium chain mu2. golgi adaptor AP-1 47 kDa protein. golgi adaptor HA1/AP1 adaptin mu-2 subunit. mu ... a virally encoded peripheral membrane protein. Nef binds to the adaptor protein (AP) complexes of coated vesicles, inducing an ...
Compare adaptor related protein complex 2 subunit sigma 1 ELISA Kits from leading suppliers on Biocompare. View specifications ... adaptor related protein complex 2 subunit sigma 1 ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a well- ... Your search returned 34 adaptor related protein complex 2 subunit sigma 1 ELISA ELISA Kit across 3 suppliers. ... Watch Webinar: How To Get Speed and Depth in your Host Cell Protein (HCP) Analysis ...
The term AP complex, or adaptor, generally denotes one of four heterotetrameric protein complexes (AP-1, AP-2, AP-3, and AP-4 ... HIV Nef-Mediated CD4 Down-Regulation Is Adaptor Protein Complex 2 Dependent. Yong-Jiu Jin, Catherine Yi Cai, Xiaoping Zhang, ... Interactions of HIV-1 nef with the μ subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based sorting ... To elucidate the mechanism related to the switching, we examined the adaptor protein complex required for Nef-mediated and PMA- ...
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Adaptor-Related Protein Complex 1, beta 1 Subunit ELISA Kits * Adaptor-Related Protein Complex 1 Associated Regulatory Protein ... clathrin adaptor complex AP2, mu subunit , clathrin coat adaptor protein AP50 , clathrin-associated/assembly/adaptor protein, ... Adaptor Related Protein Complex 1 sigma 1 ELISA Kits * Adaptor Protein, phosphotyrosine Interaction, PH Domain and Leucine ... clathrin coat assembly protein AP50 (CpipJ_CPIJ003697) Elisa Kit * adaptor-related protein complex 2, mu 1 subunit (Ap2m1) ...
What is Adaptor protein complex AP-2 subunit mu? Meaning of Adaptor protein complex AP-2 subunit mu medical term. What does ... Adaptor protein complex AP-2 subunit mu explanation free. ... Looking for online definition of Adaptor protein complex AP-2 ... redirected from Adaptor protein complex AP-2 subunit mu) AP2M1. A gene on chromosome 3q28 that encodes a subunit of the ... Adaptor protein complex AP-2 subunit mu , definition of Adaptor protein complex AP-2 subunit mu by Medical dictionary https:// ...
Protein (His tag). Spezies: Maus. Quelle: Escherichia coli (E. coli). Jetzt Produkt ABIN3129522 bestellen. ... Recombinant Adaptor-Related Protein Complex 1, sigma 2 Subunit (AP1S2) ... Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi ... Adaptor-Related Protein Complex 1, sigma 2 Subunit (AP1S2) (AA 1-160) protein (His tag) Protein AP1S2 Spezies: Maus Quelle: ...
adaptor-related protein complex 2, sigma 1 subunit. Gene nomenclature, locus information, and GO, OMIM, and PMID associations ... OMIM: HYPOCALCIURIC HYPERCALCEMIA, FAMILIAL, TYPE III; HHC3, ADAPTOR-RELATED PROTEIN COMPLEX 2, SIGMA-1 SUBUNIT; AP2S1*Gene ...
OMIM: ADAPTOR-RELATED PROTEIN COMPLEX 2, ALPHA-2 SUBUNIT; AP2A2*Gene Ontology: Ap2a2 *Mouse Phenome DB: Ap2a2 *UCSC: Chr.7: ... adaptor-related protein complex 2, alpha 2 subunit. Synonyms: 2410074K14Rik, Adtab, alpha-adaptin C, alpha-C adaptin, L25. Gene ...
Creative Biomart offer ap3s2 proteins for life sciences research. All the products are rigorously tested to meet the most ... adaptor complex sigma3B;AP-3 complex subunit sigma-3B;clathrin-associated/assembly/adaptor protein, small 4, 22-kD;AP3S3; ... AP3S2;adaptor-related protein complex 3, sigma 2 subunit;AP-3 complex subunit sigma-2;sigma3b;sigma-3B-adaptin;sigma-adaptin 3b ... Protein Function. AP3S2 has several biochemical functions, for example, protein transporter activity. Some of the functions are ...
Clathrin:AP2 complex [clathrin-coated endocytic vesicle membrane] (Homo sapiens) * Adaptor protein 2 complex [endolysosome ... Clathrin:AP2 complex [clathrin-coated endocytic vesicle membrane] (Homo sapiens) * Adaptor protein 2 complex [endolysosome ... Clathrin:AP2 complex [clathrin-coated endocytic vesicle membrane] (Homo sapiens) * Adaptor protein 2 complex [endolysosome ... Clathrin:AP2 complex [clathrin-coated endocytic vesicle membrane] (Homo sapiens) * Adaptor protein 2 complex [endolysosome ...
GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex. J Cell ... STAM Adaptor Proteins Interact with COPII Complexes and Function in ER-to-Golgi Trafficking. ... Rismanchi, N., Puertollano, R. and Blackstone, C. (2009), STAM Adaptor Proteins Interact with COPII Complexes and Function in ... The Vps27p Hse1p complex binds ubiquitin and mediates endosomal protein sorting. Nat Cell Biol 2002;4:534-539. *PubMed, ...
... in complex with a sorting peptide from the amyloid precursor protein (APP) ... Crystal structure of adaptor protein complex 4 (AP-4) mu4 subunit C-terminal domain, ... Crystal structure of adaptor protein complex 4 (AP-4) mu4 subunit C-terminal domain, in complex with a sorting peptide from the ... Sorting of the Alzheimers disease amyloid precursor protein mediated by the AP-4 complex.. Burgos, P.V., Mardones, G.A., Rojas ...
... and they form complexes with a number of endocytic proteins, including Hrs and Eps15. In this study, we demonstrate that STAM ... Signal-transducing adaptor molecules (STAMs) are involved in growth factor and cytokine signaling as well as receptor ... STAM adaptor proteins interact with COPII complexes and function in ER-to-Golgi trafficking Traffic. 2009 Feb;10(2):201-17. doi ... Furthermore, STAM proteins interact with coat protein II (COPII) proteins, probably at endoplasmic reticulum (ER) exit sites, ...
... is brought into the complex by the substrate adaptor protein, while the Rbx1 protein recruits a ubiquitin-charged E2 protein. ... Keap1 functions as a substrate adaptor protein for a Cul3/Rbx1 E3 ubiquitin ligase complex.Cullin proteins function as ... Keap1 Is a Redox-Regulated Substrate Adaptor Protein for a Cul3-Dependent Ubiquitin Ligase Complex. Donna D. Zhang, Shih-Ching ... The ability of Keap1 to function as a redox-sensitive substrate adaptor protein for an E3 ubiquitin ligase complex constitutes ...
E3 ubiquitin-protein ligase complex involved in regulation of cytoskeleton structure. The BCR(TNFAIP1) E3 ubiquitin ligase ... complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin ... Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) ... with other proteins or protein complexes.,p>,a href=/help/ ... This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.. View all proteins of ...
Soluble N-ethylmaleimide-sensitive-factor Attachment protein Receptors (SNAREs) participate in the specificity of membrane ... Protein Transport / physiology. Protozoan Proteins / metabolism. R-SNARE Proteins / metabolism*. Recombinant Fusion Proteins / ... Adaptor Protein Complex 2 / metabolism. Adaptor Proteins, Vesicular Transport / metabolism*. Animals. Cell Membrane / ... 0/Adaptor Proteins, Vesicular Transport; 0/Macromolecular Substances; 0/Protozoan Proteins; 0/R-SNARE Proteins; 0/Recombinant ...
We have demonstrated that the 3BP2 adapter protein is a component of the CD19 costimulatory complex and is essential for ... CD19 as a membrane-anchored adaptor protein of B lymphocytes: costimulation of lipid and protein kinases by recruitment of Vav ... The 3BP2 Adapter Protein Is Required for Optimal B-Cell Activation and Thymus-Independent Type 2 Humoral Response. Grace Chen, ... 3BP2 forms complexes with a number of signaling proteins, such as Zap-70, LAT, phospholipase C γ1 (PLC-γ1), Grb2, Cbl, and Fyn ...
Adaptor protein complex-4 (AP-4) deficiency causes a novel autosomal recessive cerebral palsy syndrome with microcephaly and ... Adaptor protein complex-4 (AP-4) deficiency causes a novel autosomal recessive cerebral palsy syndrome with microcephaly and ... one of the four subunits of the adaptor protein complex-4 (AP-4), identified by chromosomal microarray analysis. ... Conclusion These findings, along with previous reports of human and mouse mutations in other members of the complex, indicate ...
Forms a complex with RAB11FIP2 that is recruited to the phagosomes to promote the activation of the actin-regulatory GTPases ... Involved in IL-18 signaling and is proposed to function as a sorting adapter for MYD88 in IL-18 signaling during adaptive ... Functions as sorting adapter in different signaling pathways to facilitate downstream signaling leading to type I interferon ... section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes ...
Lymphocytes with a complex: adapter proteins in antigen receptor signaling. Immunol. Today 21:584-591. ... Adapters are scaffolding proteins lacking enzymatic domains. However, they contain protein-protein interaction modules such as ... protein kinase C; PLCγ, phospholipase C-γ; SH, Src homology; SLAP, Src-like adapter protein; TRE, tetracycline responsive ... SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling. Proc. Natl. Acad. Sci. USA. 96:9775-9780 ...
... and protein kinase C (PKC). InaD organizes these proteins into a signaling complex that allows efficient activation of the TRP ... kinase binding proteins such as 14-3-3 proteins serve as adaptor proteins for signaling networks, whereas proteins such as ... The covalent association of these recognition modules-as found in adaptors, anchoring proteins, and docking proteins-allows a ... In this review, we compare and contrast the protein modules, adaptor molecules, targeting subunits, and anchoring proteins that ...
Mechanisms of synaptic plasticity mediated by Clathrin Adaptor-protein complexes 1 and 2 in mice - eDiss In this collection. ... Clathrin adaptor protein complexes 1 and 2 (AP1 and AP2) have essential functions in synaptic vesicle (SV) recycling. In all ... Mechanisms of synaptic plasticity mediated by Clathrin Adaptor-protein complexes 1 and 2 in mice. Ratnakar Mishra ... Neurons express the ubiquitous AP1/σ1A complex and in addition, the tissue-specific AP1/σ1B complex. In our lab, we have ...
Here we describe the identification of the adaptor protein, Shc-like protein (Sck), as a binding partner for KDR. We ... We have also shown that the SH2 domain of Sck, but not that of Src-homology collagen protein (Shc), can precipitate ... and that an N-terminally truncated Sck protein can associate with KDR, in a phosphorylation-dependent fashion, when co- ... demonstrate that this interaction requires phosphorylation of KDR, and identify the binding site for the Src-homology 2 (SH2) ...
Protein Coding), Adaptor Related Protein Complex 2 Alpha 2 Subunit, including: function, proteins, disorders, pathways, ... Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor ... Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor ... AP2A2 Gene(Protein Coding) Adaptor Related Protein Complex 2 Alpha 2 Subunit. ...
Protein Coding), Adaptor Related Protein Complex 1 Subunit Gamma 2, including: function, proteins, disorders, pathways, ... The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. This ... AP1G2 Gene(Protein Coding) Adaptor Related Protein Complex 1 Subunit Gamma 2. ... AP1G2 (Adaptor Related Protein Complex 1 Subunit Gamma 2) is a Protein Coding gene. Diseases associated with AP1G2 include Long ...
Ub, ubiquitin; AP, adaptor protein; ESCRT, endosomal sorting complex required for transport; ALIX, ALG-2 interacting protein X. ... Ubiquitinated proteins are endocytosed and sorted in the endosomal pathway by a process dependent on adaptor proteins that ... The identified proteins include members of the ESCRT-I protein complex (involved in recognition of ubiquitinated cargo by MVBs ... there were 10 cytoskeletal and motor proteins. There were 48 integral membrane proteins (putative cargo proteins), including ...
  • The encoded protein is found on the cytoplasmic face of coated vesicles in the plasma membrane. (
  • A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex. (
  • Cytosolic and membrane-associated proteins involved in the recruitment of AP-1 adaptors onto the trans-Golgi network. (
  • An integral membrane protein, CD4 is expressed primarily on the surface of Th cells and cells of the monocyte/macrophage lineage. (
  • The prevailing view is that AP-2 mediates endocytosis from the plasma membrane, whereas AP-1, AP-3, and AP-4 participate in the protein sorting from the trans-Golgi network and/or endosomes to lysosomes. (
  • Results indicate that AP-2 is not essential for clathrin -coated vesicle formation at the plasma membrane, but that it is one of several endocytic adaptors required for the uptake of certain cargo proteins. (
  • Under both scenarios, vesicular stomatitis virus G protein-green fluorescent protein trafficking to the plasma membrane is markedly inhibited, and recovery of Golgi morphology after Brefeldin A treatment is substantially impaired in STAM-depleted cells. (
  • Soluble N-ethylmaleimide-sensitive-factor Attachment protein Receptors (SNAREs) participate in the specificity of membrane fusions in the cell. (
  • Mutation of a potential dileucine motif dramatically increases the proportion of cells with GFP-VAMP7 in their plasma membrane, strongly supporting the participation of an AP complex in VAMP7 sorting to the endocytic pathway. (
  • The protein encoded by this gene is a subunit of the AP-2 adaptor protein complex, which is involved in linking lipid and protein membrane components with the clathrin lattice. (
  • Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. (
  • AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. (
  • The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. (
  • Adaptins are important components of clathrin-coated vesicles transporting ligand-receptor complexes from the plasma membrane or from the trans-Golgi network to lysosomes. (
  • The complex mediates the recruitment of clathrin to the vesicle membrane. (
  • However, it remains a mystery how aquaporin-2 (an integral membrane protein) and other apical transporters are delivered to the urine. (
  • AQP2 is an integral membrane protein, and investigators thus far have been puzzled with regard to the mechanism of its secretion into the urine. (
  • Immunoblotting of urinary membrane fractions has revealed that, in addition to AQP2, the kidneys excrete membranes containing apical plasma-membrane transporter proteins from each renal tubule segment ( 5 ), suggesting that analysis of urinary membrane fractions could provide noninvasive information about the pathophysiological state of the entire renal tubule. (
  • We hypothesize that AQP2 and other apical plasma-membrane proteins are excreted through the process of exosome formation, i.e., delivery of the internal vesicles of multivesicular bodies (MVBs) to the urinary space by fusion of the outer membrane of MVBs with the apical plasma membrane of renal tubule epithelial cells. (
  • Here we use immunoelectron microscopy and nanospray liquid chromatography-tandem MS (LC-MS/MS) analysis of urinary membrane proteins to show that AQP2 and other apical plasma-membrane proteins are excreted through the process of exosome formation in agreement with the predictions above. (
  • Mutation of the putative myristoylation site of SLAP-2 compromised its inhibitory activity and impaired its localization to the membrane compartment. (
  • Here, we report a transport complex linking syntaxin 1a (Stx) and Munc18, two proteins functioning in synaptic vesicle exocytosis at the presynaptic plasma membrane, to the motor protein Kinesin-1 via the kinesin adaptor FEZ1. (
  • Transport of syntaxin 1a (Stx), an essential component of the exocytotic release apparatus residing in the presynaptic plasma membrane, is clearly distinct from synaptic vesicle precursors and appears to involve a complex between Kinesin-1 and the Stx-binding protein syntabulin ( 6 , 7 ). (
  • The production of mature SGs requires concentrating newly synthesized soluble content proteins in granules whose membranes contain the appropriate integral membrane proteins. (
  • The mechanisms underlying the sorting of soluble and integral membrane proteins destined for SGs from other proteins are not yet well understood. (
  • The trafficking of granule membrane proteins can be controlled by both luminal and cytosolic factors. (
  • Cytosolic adaptor proteins (APs), which recognize the cytosolic domains of proteins that span the SG membrane, have been shown to play essential roles in the assembly of functional SGs. (
  • AP-2α binds to phosphatidylinositol (4,5)-bisphosphate [PtdIns(4,5) P 2 ] and/or phosphatidylinositol (3,4,5)-trisphosphate [PtdIns(3,4,5) P 3 ] lipids enriched in the plasma membrane. (
  • The C-terminal domain also has a PtdIns(4,5) P 2 -binding site that probably approaches the plasma membrane when this conformational change occurs, and the interaction of the μ2 C-terminal domain with PtdIns(4,5) P 2 in the plasma membrane may keep the Yxxϕ-binding site open. (
  • 3 4 5 6 7 Retinoschisin is almost entirely composed of a highly conserved discoidin domain frequently found in a wide range of membrane and extracellular proteins and most likely mediating cell adhesion and cellular signaling processes. (
  • The enzyme is recruited to the plasma membrane via the interaction of its carboxyl-terminal pleckstrin-homology (PH) domain with the beta and gamma subunits of heterotrimeric G proteins (Gbetagamma). (
  • Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro. (
  • The ability of epithelial cells to distinguish between domains on opposing cell surfaces within a tissue, a property known as planar cell polarity, relies on proteins and protein complexes directing the traffic of signaling proteins to specific locations on the cell surface membrane. (
  • Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, l. (
  • AP50 is a subunit of the plasma membrane adaptor. (
  • Proteins required for nutrient uptake or cell wall biosynthesis in the new environment are incorporated into the plasma membrane via the secretory pathway. (
  • By cleaving critical proteins, caspases lead to the changes that characterize apoptosis both morphologically and biochemically, such as chromatin condensation, loss of cell adhesion, cell shrinkage, membrane blebbing, DNA fragmentation, and finally formation of apoptotic bodies, which stimulate their own engulfment by phagocytes. (
  • The Adaptor Protein 3 complex (AP-3) sorts transmembrane proteins to lysosomes and deficiency in AP-3 results in missorting of proteins from the lysosomal to plasma membrane. (
  • Shaping Giant Membrane Vesicles in 3D-Printed Protein Hydrogel Cages. (
  • This protein along with the complex is thought to function at some trafficking step in the complex pathways between the trans-Golgi network and the cell surface. (
  • Many signaling pathways do so by altering the phosphorylation state of tyrosine, serine, or threonine residues of target proteins. (
  • The assembly of signaling proteins into biochemical pathways or networks is typified by the association of autophosphorylated receptor tyrosine kinases with cytoplasmic proteins that contain specialized protein modules that mediate formation of signaling complexes (Fig. 2 ) ( 1 ). (
  • Hypersensitive mutants revealed cytoprotective pathways, including stress-activated signaling and protein degradation. (
  • Several mechanistically distinct pathways exist for vesicular uptake of surface receptors ( Fig. 1 ), but the best studied and quantitatively most significant is CME ( Fig. 2 ). (
  • This binding elicits the internalization and intracellular sorting of receptor-ligand complexes and activates growth-modulating signaling pathways. (
  • We propose a model in which the abnormal accumulation of internalized GPCR-arrestin complexes in recycling endosomes, resulting from defective arrestin-AP-2 interactions, leads to the specific initiation of aberrant signaling pathways and apoptosis. (
  • The evolutionary origin of the Krebs citric acid cycle has been for a long time a model case in the understanding of the origin and evolution of metabolic pathways: How can the emergence of such a complex pathway be explained? (
  • Inside-out signaling refers to intracellular signaling pathways that regulate protein interactions at the cytoplasmic tails, which control integrin conformation and thereby affinity. (
  • Receptor-ligand systems of this group are critically involved in various cellular signalling pathways such as inflammation, lymphocyte homeostasis, apoptosis and tissue development [ 2 , 3 ]. (
  • It may also play a role in regulating the intracellular trafficking and function of CTLA-4 protein. (
  • Antigen receptors on T and B cells recognize pathogens and foreign antigens and initiate a series of intracellular biochemical signaling events that result in complex biological responses ( 1 , 2 ). (
  • Members of this Type 1 transmembrane protein family share structural characteristics including an extracellular domain consisting of multiple epidermal growth factor-like (EGF) repeats, and an intracellular domain consisting of multiple, different domain types. (
  • Activated receptors are subsequently phosphorylated in complex patterns on intracellular domains by serine/threonine G protein-coupled receptor kinases (GRKs), which reduce receptor affinity for G proteins and increase receptor affinity for arrestins ( 7 - 10 ). (
  • at least 215 X-linked MR (XLMR) conditions have been described, and mutations have been identified in 83 different genes, encoding proteins with a variety of function, such as chromatin remodeling, synaptic function, and intracellular trafficking. (
  • HPS-2 disease results from mutations in the b3A subunit of a coat protein, adaptor complex-3, responsible for intracellular vesicle formation. (
  • The highly-conserved Notch signaling pathway is unique, as both the Notch receptor and most of its respective ligands (canonically the DSL or Delta/Serrate/lag-2 family members) are transmembrane proteins attached to the cell surface. (
  • The remaining C-terminal two-thirds dictate cargo selection by directly recognizing the Yxxϕ motif, one of the most common sorting signals present in the cytosolic domains of transmembrane proteins. (
  • AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. (
  • These results suggest that AP-2 (zeige GTF3A ELISA Kits ) is essential for endocytic clathrin coated- pit (zeige IRF6 ELISA Kits ) and coated-vesicle formation. (
  • Signal-transducing adaptor molecules (STAMs) are involved in growth factor and cytokine signaling as well as receptor degradation, and they form complexes with a number of endocytic proteins, including Hrs and Eps15. (
  • AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. (
  • The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. (
  • Aberrant endocytic processing through disruption of adaptor protein complexes is likely to result from the AP1S2 mutations identified in the three XLMR-affected families, and such defects may plausibly cause abnormal synaptic development and function. (
  • AP1S2 is the first reported XLMR gene that encodes a protein directly involved in the assembly of endocytic vesicles. (
  • Strikingly, the AP2 complex, which in metazoans links endocytic cargo to the clathrin coat, but had no assigned function in yeast, was critical for K28 toxicity. (
  • In addition, AP-2 associates with the receptor-arrestin complex in perinuclear endosomes and is required for proper post-endocytic GPCR trafficking. (
  • In this study, we show that the AP-2 endocytic adaptor complex is required for the internalization of the major cell wall biosynthesis enzyme Chs3. (
  • The study also highlights key distinctions between endocytic requirements of growth at yeast buds compared to that at hyphal tips and different requirements of AP-2 in maintaining the polarity of mannosylated proteins and ergosterol at hyphal tips. (
  • Together, our findings highlight the importance of correct cell wall deposition in cell shape maintenance and polarized growth and the key regulatory role of endocytic recycling via the AP-2 complex. (
  • A functional endocytic pathway is known to be required for the morphological switch from yeast to filamentous hyphal growth and in the maintenance of polarized growth in hyphae ( 2 - 4 ). (
  • Adaptor protein 4 (AP-4) is the most recently discovered and least well-characterized member of the family of heterotetrameric adaptor protein (AP) complexes that mediate sorting of transmembrane cargo in post-Golgi compartments. (
  • The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. (
  • GABA B receptors are G-protein-coupled receptors that mediate inhibitory synaptic actions through a series of downstream target proteins. (
  • It is increasingly appreciated that the GABA B receptor forms part of larger signaling complexes, which enable the receptor to mediate multiple different effects within neurons. (
  • Complex signaling networks between the chloroplast and the nucleus mediate the emergence of the seedling into the light and the establishment of photosynthesis. (
  • 3BP2 is a pleckstrin homology domain- and Src homology 2 (SH2) domain-containing adapter protein that is mutated in the rare human bone disorder cherubism and which has also been implicated in immunoreceptor signaling. (
  • 3BP2 is a pleckstrin homology (PH) domain- and Src homology 2 (SH2) domain-containing adapter protein of unknown function that was originally cloned in a screen to identify c-Abl SH3 binding proteins ( 4 , 33 ). (
  • AP-2 complex subunit alpha-1 is a protein that in humans is encoded by the AP2A1 gene. (
  • This gene encodes the alpha 1 adaptin subunit of the adaptor protein 2 (AP2 adaptors) complex found in clathrin coated vesicles. (
  • The protein encoded by this gene is one of two large chain components of the assembly protein complex 2, which serves to link clathrin to receptors in coated vesicles. (
  • This gene encodes a subunit of the heterotetrameric adaptor-related protein comlex 1 (AP-1), which belongs to the adaptor complexes medium subunits family. (
  • AP2A2 (Adaptor Related Protein Complex 2 Alpha 2 Subunit) is a Protein Coding gene. (
  • The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. (
  • Gene Ontology (GO) annotations related to this gene include binding and protein transporter activity . (
  • Mutations in the gene encoding the Sigma 2 subunit of the adaptor protein 1 complex, AP1S2, cause X-linked mental retardation. (
  • A genetic variant near adaptor-related protein complex 2 alpha 2 subunit gene is associated with coronary artery disease in a Chinese population. (
  • Adaptor-related protein complex 2 alpha 2 subunit (AP2A2) gene encodes a protein-a subunit of the AP-2 adaptor protein complex. (
  • The protein encoded by this gene belongs to the subtilisin-like proprotein convertase family. (
  • This gene encodes and ADAM family member that cleaves many proteins including TNF-alpha and E-cadherin. (
  • This gene encodes a protein which is similar to the Drosophila crumbs protein and localizes to the inner segment of mammalian photoreceptors. (
  • Several miRNAs have been shown to regulate gene expression or biological processes relevant to blood pressure regulation or the development of hypertension 2 - 6 and it is conceivable that many more miRNAs may be involved. (
  • Complex formation initiates a signaling cascade that leads to changes in gene expression and cell division. (
  • We propose a new approach to identify interacting proteins based on gene expression data. (
  • HPS-2 is caused by a mutation in the gene encoding the beta-3A subunit of the heterotetrameric AP3 complex ( ADTB3A ), which resides on chromosome 5. (
  • AFG3 ATPase family gene 3-like 2 (S. c. (
  • An important gene associated with Dandy-Walker Malformation with Intellectual Disability, Basal Ganglia Disease and Seizures is AP1S2 (Adaptor Related Protein Complex 1 Subunit Sigma 2). (
  • This thesis describes two new patients with HPS2, both with homozygous mutations in the AP3B1 gene, which codes for the β3A subunit of the AP-3 complex. (
  • AP3S2 has direct interactions with proteins and molecules. (
  • We selected proteins and molecules interacted with AP3S2 here. (
  • Eukaryote cells are exposed to both intrinsic and extrinsic sources of reactive oxygen species and other chemically reactive molecules that can damage biological macromolecules, including DNA, proteins, and lipids ( 22 ). (
  • The adaptin family of proteins is composed of four classes of molecules named alpha, beta-, beta prime- and gamma- adaptins. (
  • In this review, we compare and contrast the protein modules, adaptor molecules, targeting subunits, and anchoring proteins that coordinate signaling networks. (
  • Complex formation between phosphorylated GPCRs, arrestins and an ever-increasing number of effector molecules is known to regulate cellular function. (
  • While studies have identified changes in transcription leading to the synthesis and secretion of new proteins to facilitate hyphal growth, effective maintenance of hyphae also requires concomitant removal or relocalization of other cell surface molecules. (
  • Integrins act as bidirectional signaling molecules [ 2 ]. (
  • The use of such hybrid regions allows for an efficient protein expression when used in conjunction with circular or linear expression DNA molecules. (
  • Title: The AP-2 adaptor beta2 appendage scaffolds alternate cargo endocytosis. (
  • Caco-2 intestinal epithelial cells absorb soybean ferritin by mu2 (AP2)-dependent endocytosis. (
  • The mechanism of iron absorption from mineralized Soybean ferritin using Caco-2 cells via a mu2-dependent endocytosis mechanism is reported. (
  • The results demonstrate that, like the tyrosine sorting motif-dependent endocytosis (for which the transferrin receptor and the epidermal growth factor receptor are the two prototypes), dileucine sorting motif-dependent endocytosis of Nef and CD4 are also AP-2 dependent. (
  • We identify dynamin and the EAP -binding alpha-adaptin appendage domain of the AP2 adaptor as switches in a regulated, multistep maturation process and provide direct evidence for a molecular checkpoint in clathrin mediated endocytosis. (
  • multiple interactions between PIPKI gamma- p90 and AP-2 lead to spatiotemporally controlled PI(4,5)P(2) synthesis during clathrin -mediated synaptic vesicle endocytosis. (
  • Thus, in addition to their roles in signaling and endocytosis, STAMs function prominently in ER-to-Golgi trafficking, most likely through direct interactions with the COPII complex. (
  • In all cell types and tissues, AP1 mediates TGN/endosome protein sorting via clathrin-coated-vesicles (CCV), whereas AP2 transports proteins by clathrin-mediated endocytosis (CME). (
  • AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. (
  • EGFR has become a model protein for understanding the biology and endocytosis of related growth-factor receptors, and the mechanisms involved in its endocytosis and degradation have been scrutinized for several decades. (
  • Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2). (
  • The complex is part of the protein coat on the cytoplasmic face of coated vesicles which links clathrin to receptors in vesicles. (
  • In these cells, PMA can induce serine phosphorylation in the cytoplasmic tail of CD4 that triggers the down-regulation of CD4 from the cell surface ( 1 , 2 ). (
  • We demonstrate that the endogenous 3BP2 protein binds to the cytoplasmic tail of the B-cell costimulatory molecule CD19 and that 3BP2 deficiency leads to defects in Syk phosphorylation and calcium flux. (
  • We have previously shown that two separate domains in the HIV-2 envelope protein are required for this activity: a glycine-tyrosine-x-x-hydrophobic (GYxxθ) motif in the cytoplasmic tail and an unmapped region in the ectodomain of the protein. (
  • Interestingly, we found that the cytoplasmic tail of the murine leukemia virus (MLV) Env could functionally substitute for the HIV-2 Env tail, but it did so in a manner that did not require a Yxxθ motif or AP-2. (
  • AP1S2 encodes an adaptin protein that constitutes part of the adaptor protein complex found at the cytoplasmic face of coated vesicles located at the Golgi complex. (
  • An extracellular signal input drives autophosphorylation of the receptor and leads to the recruitment of cytoplasmic proteins that contain various protein modules. (
  • Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. (
  • RSU-1 is an evolutionary conserved cytoplasmic protein that contains multiple leucine-rich repeats (LRRs) and interacts with integrin-dependent adhesion complexes. (
  • The cytoplasmic region of TLRs shares a stretch of protein module called the Toll/IL-1R (TIR) domain, which mediates homo- and heterophilic interactions between TLRs and TIR-containing adaptors ( 2 ). (
  • This involves connections at the very short integrin cytoplasmic tails with a complex of cytoskeletal adapter proteins. (
  • V1H can function as an adaptor for interactions between Nef and AP-2 (zeige GTF3A ELISA Kits ). (
  • Biochemical and X-ray crystallographic analyses reveal that the properties of the APP sequence and the location of the binding site on mu4 are distinct from those of other signal-adaptor interactions. (
  • This permits simultaneous association of a single protein containing both SH2 and SH3 domains with two or more binding partners, and hence, the assembly of complexes of signaling proteins around an activated cell-surface receptor (Fig. 1 A). Similarly, subcellular organization of serine-threonine kinases and phosphatases occurs through interactions with the targeting subunits or anchoring proteins that localize these enzymes ( 3 ). (
  • Indeed, phosphorylation-regulated interactions between cargo, adaptors, and kinesins have also been observed for other transport complexes such as the kinesin light chain/JIP1 (c-Jun N-terminal kinase-interacting protein 1) complex ( 4 ). (
  • Arrestin binding sterically blocks receptor-G protein interactions, thereby terminating G protein signaling, while simultaneously providing a scaffold to coordinate the recruitment of internalization machinery, leading to receptor sequestration ( 11 - 13 ). (
  • For human cells, published experimental results are collected in databases like MINT (Molecular Interactions database) and HPRD (Human Protein Reference Database) [ 8 , 9 ], but the amount of information is still largely limited. (
  • Moreover, data have been obtained from different cellular models and using different techniques, thus rendering it difficult to build a global network of interactions or to extrapolate information about the composition of multi-protein complexes. (
  • In this paper we present a new approach for the detection of putative protein interactions based on expression data. (
  • Besides the identification of permanent complexes, it is also capable (at least for well synchronized samples) of reliably identifying interactions among proteins belonging to transient complexes. (
  • Firstly, protein-protein interactions are more easily identified if the interacting protein pair belongs to a multi-protein complex. (
  • Therefore, we focused on tracking interactions within protein complexes, even though our algorithm can, in principle, identify any type of protein-protein interaction. (
  • Preventing premature interactions between microtubules and protein-based structures called kinetochores ensures that chromosomes are segregated by meiosis rather than mitosis in reproductive cells. (
  • A combination of molecular dynamics simulations and X-ray diffraction data has been used to construct more realistic models of proteins and to provide new insights into their interactions with other proteins and biomolecules. (
  • To fully appreciate the function and regulation of these neurotransmitter receptors, we must understand their interactions with other proteins. (
  • The pathway maps illustrate protein interactions and regulation to provide a comprehensive picture of signaling and disease processes. (
  • Integrin cell adhesion receptors participate in cell-cell and cell-ECM interactions [ 2 ]. (
  • These findings demonstrate that APP and AP-4 engage in a distinct type of signal-adaptor interaction that mediates transport of APP from the trans-Golgi network (TGN) to endosomes, thereby reducing amyloidogenic processing of the protein. (
  • The BCR(TNFAIP1) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. (
  • Your search returned 12 adaptor related protein complex 1 subunit gamma 2 ELISA ELISA Kit across 1 supplier. (
  • The mutation of this motif or the depletion of AP-2 by RNA interference abrogated EVR activity and changed the cellular distribution of the Env from a predominantly punctate pattern to a more diffuse distribution. (
  • The encoded protein is required for the activity of a vacuolar ATPase, which is responsible for proton pumping occurring in the acidification of endosomes and lysosomes. (
  • The ubiquitous AP1/σ1A complex binds to these endosomes and stimulates their maturation into late, multi-vesicular-body endosomes, up regulating endolysosomal protein transport. (
  • May function in protein sorting in late endosomes or multivesucular bodies (MVBs). (
  • Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. (
  • Furthermore, STAM proteins interact with coat protein II (COPII) proteins, probably at endoplasmic reticulum (ER) exit sites, and Sar1 activity is required to maintain the localization of STAMs at discrete sites. (
  • Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. (
  • Adaptor protein 1A (AP-1A) is known to interact with specific motifs in its cargo proteins and with the clathrin heavy chain, contributing to the formation of a clathrin coat. (
  • 2 It encodes a 24-kDa protein, termed retinoschisin, which is mainly secreted from photoreceptors as a homo-oligomeric complex. (
  • 7. The expression vector according to claim 5, wherein the recombinant nucleic acid according to claim 1 further comprises a protein coding sequence that encodes a reporter protein or a therapeutic protein. (
  • Concurrently, DEDD interacts with Rb family proteins and promotes their proteasome-mediated degradation. (
  • ClpS is an adaptor protein that influences protein degradation through its binding to the N-terminal domain of the chaperone ClpA in the ClpAP chaperone-protease pair. (
  • The degradation of ClpAP substrates, both SsrA-tagged proteins and ClpA itself, is specifically inhibited by ClpS. (
  • ClpS modifies ClpA substrate specificity, potentially redirecting degradation by ClpAP toward aggregated proteins [ PMID: 11931773 ]. (
  • A green fluorescent protein (GFP)-fusion cDNA library was generated for monitoring degradation kinetics. (
  • In vitro assay of degradation is simpler than in vivo analysis, but an in vitro assay system may not fully mimic the degradation of proteins in the cells. (
  • These studies demonstrate that introducing GFP as a fusion within the context of a rapidly degraded protein does not alter the degradation properties of the parent molecule, and that the GFP moiety of the fusion protein is degraded along with the rest of the protein. (
  • 3BP2 has been implicated as a positive regulatory adapter molecule coupled to immunoreceptors on T cells ( 6 ), B cells ( 12 ), NK cells ( 17 ), and basophils ( 35 ) in overexpression studies. (
  • We previously reported a new Toll/IL-1R (TIR)-containing molecule, named TIR domain-containing adaptor inducing IFN-β (TRIF). (
  • Adaptor-related protein complex 2, alpha 1 has been shown to interact with DPYSL2 and NUMB. (
  • Title: Single nucleotide polymorphisms of matrix metalloproteinase 9 (MMP9) and tumor protein 73 (TP73) interact with Epstein-Barr virus in chronic lymphocytic leukemia: results from the European case-control study EpiLymph. (
  • Most of the proteins interact with multiple RNA elements, often from different domains. (
  • Defects in formation of the complex or in its ability to interact directly with cargo inhibit enzyme uptake and lead to defective cell walls and aberrant hyphal morphology. (
  • Available data indicate that Nef connects CD4 to an AP complex in the absence of CD4 phosphorylation ( 4 ) and that the Nef-AP interaction requires the dileucine sorting motif located in the C-terminal portion of the Nef protein ( 13 , 14 , 15 ). (
  • We show that 3BP2 binds via its SH2 domain to the CD19 signaling complex and is required for optimum Syk phosphorylation and calcium flux. (
  • Transport of the synaptic vesicle protein synaptotagmin by the UNC-76/Kinesin-1 complex requires phosphorylation of UNC-76 by the UNC-51/ATG1 kinase, a prerequisite for UNC-76 to bind synaptotagmin ( 3 ). (
  • This suggests that phosphorylation is a common mechanism for the regulation of kinesin-based transport complexes ( 5 ). (
  • Therefore, it has been proposed that the phosphorylation of another protein, an as yet unknown EGF receptor substrate, is required for the efficient recruitment of EGF receptors into coated pits ( Lamaze and Schmid, 1995 ). (
  • EGF receptor activation leads to the phosphorylation of various proteins. (
  • TRPV1 internalization depended on binding to the clathrin adaptor protein complex 2 subunit μ2 (AP2μ2) and was antagonized by phosphorylation of AP2μ2 by cyclin-dependent kinase 5 (CDK5). (
  • G protein beta gamma subunits stimulate phosphorylation of Shc adapter protein. (
  • The encoded protein catalyzes phosphorylation of phosphatidylinositol 4-phosphate, producing phosphatidylinositol 4,5-bisphosphate. (
  • These AP complexes are essential components of the clathrin-coated vesicles. (
  • Adaptins, together with medium and small subunits, form a heterotetrameric complex called an adaptor, whose role is to promote the formation of clathrin-coated pits and vesicles. (
  • Proteomic analysis of urinary vesicles through nanospray liquid chromatography-tandem mass spectrometry identified numerous protein components of MVBs and of the endosomal pathway in general. (
  • Third, the urinary vesicles should contain proteins typical of MVBs and of exosomes formed by other cell types ( 7 ). (
  • In Drosophila, deletion of UNC-76/fasciculation and elongation protein zeta 1 (FEZ1), a specific adaptor for Kinesin-1, left synaptic vesicles stranded in the axon ( 2 , 3 ), showing that Kinesin-1 is needed at least during later phases of axonal transport. (
  • Neither AP-2 nor clathrin are required for the binding of Eps15 to coated pits or coated vesicles, since in membranes lacking AP-2 and clathrin, Eps15 still shows the same staining pattern. (
  • Component of the adaptor complexes which link clathrin to receptors in coated vesicles. (
  • The impaired function of specific organelles indicates that the causative genes encode proteins operative in the formation of lysosomes and vesicles. (
  • Also, other proteins which involved in the same pathway with AP3S2 were listed below. (
  • section describes the metabolic pathway(s) associated with a protein. (
  • This protein is involved in the pathway protein ubiquitination, which is part of Protein modification. (
  • View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification . (
  • Taken together, these data suggest that the essential GYxxθ motif in the HIV-2 Env tail recruits AP-2 in order to direct Env to a cellular pathway or location that is necessary for its ability to enhance virus release but that an alternate mechanism provided by the MLV Env tail can functionally substitute. (
  • A cargo/PACS-1/AP-1A complex is necessary to drive the appropriate transport of several cargo proteins within the regulated secretory pathway. (
  • We review the functions of AP-1A, PACS-1, and GGAs in facilitating the retrieval of proteins from immature SGs and review examples of cargo proteins whose trafficking within the regulated secretory pathway is governed by APs. (
  • Collectively, our study reveals a novel pathway for FLIP regulation of NF-kappa B through protein S-nitrosylation, which is a key posttranslational mechanism controlling DR-mediated cell death and survival. (
  • Finally, the role of Egr1 in the pathogenesis of Rs1h -deficiency was investigated, and the results indicated that activation of the MAPK Erk1/2 pathway occurs as early as P7. (
  • Furthermore, the data point to a role of Erk1/2-Egr1 pathway activation in RS pathogenesis. (
  • Knockdown of Rbp1 caused a similar microcephaly phenotype as the depletion of Nosip and synergy experiments indicated that both proteins act in the same signalling pathway. (
  • This protein, as well as beta-prime-adaptin, gamma-adaptin, and the medium (mu) chain AP47, form the AP-1 assembly protein complex located at the Golgi vesicle. (
  • These cytoprotective genes, which include classical phase 2 genes, such as the glutathione S -transferases, NAD(P)H oxidoreductase (NQO1), and γ-glutamyl cysteine synthase, are regulated at the transcriptional level by cis -acting DNA sequences termed antioxidant response elements (AREs) or electrophilic response elements ( 14 , 41 , 54 ). (
  • Full liquid chromatography-tandem MS analysis revealed 295 proteins, including multiple protein products of genes already known to be responsible for renal and systemic diseases, including autosomal dominant polycystic kidney disease, Gitelman syndrome, Bartter syndrome, autosomal recessive syndrome of osteopetrosis with renal tubular acidosis, and familial renal hypomagnesemia. (
  • Through knockdown of endogenous miRNAs that were (1) highly expressed in human vascular endothelial cells, and (2) predicted to target mRNA sequences of hypertension-related genes, we have identified 35 miRNA-target pairs in which the endothelial miRNAs tonically reduce the abundance of the target mRNAs that are relevant to blood pressure regulation or hypertension. (
  • Simultaneous assessment of the expression of thousands of genes in a single experiment could allow better understanding of the complex and heterogeneous molecular properties of breast cancer. (
  • Four such genes, HPS1, ADTB3A, HPS3, and HPS4, are associated with the 4 known subtypes of Hermansky-Pudlak syndrome: Hermansky-Pudlak syndrome type 1 (HPS-1), Hermansky-Pudlak syndrome type 2 (HPS-2), Hermansky-Pudlak syndrome type 3 (HPS-3), and Hermansky-Pudlak syndrome type 4 (HPS-4). (
  • There exist 8 different genes known to cause HPS, but only HPS-2 has a basic defect that is known. (
  • Briefly, Significance Analysis Microarrays (SAM) thresholding identified 31 up-regulated and 18 down-regulated genes with fold changes of ≥2 or≤0.5 and q-value ≤5 % in expression. (
  • The levels of C - reactive protein were higher in hypertensive patients than normotensives and inflammation-related genes were increased as well. (
  • Essential hypertension has been recognized as a complex, multifactorial, polygenic trait which involves multiple modulating genes and environmental factors. (
  • Knowledge of the specific proteins, lipids, and mechanisms required for trafficking and killing by these toxins remains incomplete. (
  • GPCRs are activated by a myriad of ligands including amino acids and their derivatives, peptides, proteins, ions, lipids and photons. (
  • The complex binds polyphosphoinositide-containing lipids. (
  • Our identification of the negative regulator SLAP-2 demonstrates that a retroviral-based screening strategy may be an efficient way to identify and characterize the function of key components of many signal transduction systems. (
  • The role of scaffold, anchoring, and adaptor proteins that contribute to the specificity of signal transduction events by recruiting active enzymes into signaling networks or by placing enzymes close to their substrates is discussed. (
  • Basolateral sorting of human poliovirus receptor alpha involves an interaction with the mu1B subunit of the clathrin adaptor complex in polarized epithelial cells. (
  • Herein, we report the interaction of an YKFFE sequence from the cytosolic tail of the Alzheimer's disease amyloid precursor protein (APP) with the mu4 subunit of AP-4. (
  • We recently initiated an effort to systematically identify interaction partners of established presynaptic proteins using an automated yeast two-hybrid (Y2H) screen. (
  • For soluble proteins, luminal pH and divalent metals can affect aggregation and interaction with surrounding membranes. (
  • In this study, we show that the interaction of GPCR-bound arrestin with Adaptor Protein 2 (AP-2) is a critical anti-apoptotic event. (
  • S-nitrosylation of FLICE inhibitory protein determines its interaction with RIP1 and activation of NF-kappa B. (
  • We demonstrate that this interaction is mediated by the AP-2 mu subunit (Apm4) YXXΦ binding domain. (
  • For example, src homology 2 (SH2) domains bind specific phosphotyrosyl residues on activated receptors (Fig. 2 A), and src homology 3 (SH3) domains bind to polyproline motifs on a separate set of target proteins (Fig. 2 D) ( 2 ). (
  • Cell surface signaling receptors, such as receptor tyrosine kinases (RTKs), G protein-coupled receptors (GPCRs), and cytokine receptors, are activated by binding to their ligands (e.g., growth hormones, peptide agonists, and cytokines). (
  • Most G protein-coupled receptors (GPCRs) are reversibly activated upon ligand binding. (
  • However, activation of protease-activated G protein-coupled receptors (PARs) occurs through an irreversible proteolytic event that results in the generation of a tethered ligand that cannot diffuse away. (
  • G protein-coupled receptors (GPCRs) are integral to cellular function in nearly all physiologic and many pathologic processes. (
  • Finally, we observed that depletion of endogenous AP-2 results in the initiation of apoptosis upon stimulation of multiple GPCRs including P2Y purinergic receptors and CXCR2 but not CXCR4. (
  • G protein-coupled receptors (GPCR) are involved in virtually every aspect of human physiology including cardiovascular ( 1 ), immune ( 2 ) and neuronal systems ( 3 ). (
  • In this model, based primarily on studies of the β2-adrenergic receptor (β2-AR), adaptor protein (AP)-2 and clathrin bind the carboxy terminus of arrestin ( 14 ), translocating receptors to clathrin-coated pits for internalization. (
  • These results indicate that the diffuse state of extrasynaptic receptors is not a default state that is simply explained by the lack of synaptic cues but necessitates additional proteins to prevent spontaneous clustering, a concept that is relevant for developmental and pathological situations. (
  • G protein-coupled receptor kinase 2 (GRK2) phosphorylates activated G protein-coupled receptors (GPCRs), which ultimately leads to their desensitization and/or downregulation. (
  • This recognition is mediated by a set of germline-encoded receptors called Toll-like receptors (TLRs) 3 ( 1 , 2 , 3 ). (
  • Here we report that GABA B receptors can physically associate with the potassium-chloride cotransporter protein, KCC2, which sets the driving force for the chloride-permeable ionotropic GABA A receptor in mature neurons. (
  • Using biochemical, molecular, and functional studies in rodent hippocampus, we show that activation of GABA B receptors results in a decrease in KCC2 function, which is associated with a reduction in the protein at the cell surface. (
  • This overproduction was mediated by immune complexes and involved synergistic signaling between the B cell receptor and Toll-like receptors and T cell help. (
  • This large family of heterodimeric transmembrane receptors recognizes a plethora of extracellular ligands, including transmembrane receptors on other cells and ECM proteins. (
  • abstract = "The envelope (Env) protein of human immunodeficiency virus type 2 (HIV-2) and the HIV-1 Vpu protein stimulate the release of retroviral particles from human cells that restrict virus production, an activity that we call the enhancement of virus release (EVR). (
  • The libraries were thus deemed to be useful for screening short-lived proteins in mammalian cells. (
  • In cases in which it is highly likely that the recombinant protein with the default tag will be insoluble our protein lab may suggest a higher molecular weight tag (e.g. (
  • These units are delivered to the nascent synapse via molecular motor proteins of the kinesin superfamily (reviewed in Ref. 1). (
  • The apparent molecular mass of both proteins is 142 kD, and they consist of three structural domains. (
  • However, the molecular mechanism that regulates FLIP within this complex is unknown. (
  • It is becoming increasingly clear that to understand the function and regulation of GABA B Rs requires a more complete understanding of the molecular associations that underlie GABA B R complexes in the brain. (
  • Thus, two CME routes characterized by specific lifetimes and specific cargo proteins contribute to synaptic plasticity. (
  • We conclude that FEZ1 operates as a kinesin adaptor for the transport of Stx, with cargo loading and unloading being regulated by protein kinases. (
  • AP-1A recruitment to membranes can be modulated by Phosphofurin Acidic Cluster Sorting protein 1 (PACS-1), a cytosolic protein which interacts with both AP-1A and cargo that has been phosphorylated by casein kinase II. (
  • Mouse Ap1s2 Protein (raised in E. Coli) purified by multi-step, protein-specific process to ensure crystallization grade. (
  • DOK2 may modulate the cellular proliferation induced by IL-4, as well as IL-2 and IL-3. (
  • Search, Find and Buy Antibodies, ELISA Kits and Proteins. (
  • Auf finden Sie aktuell 17 Adaptor-Related Protein Complex 2, mu 1 Subunit (AP2M1) ELISA Kits von 5 unterschiedlichen Herstellern. (
  • BMCC1 (zeige PRUNE2 ELISA Kits ) is an AP-2 (zeige GTF3A ELISA Kits ) associated endosomal protein in prostate cancer cells. (
  • Arkadia (zeige RNF111 ELISA Kits ) complexes with clathrin adaptor AP2 (zeige GTF3A ELISA Kits ) mu2 subunit and regulates EGF (zeige EGF ELISA Kits ) signalling. (
  • Binding of AP-2 (zeige TFAP2A ELISA Kits ) to otoferlin (zeige OTOF ELISA Kits ) facilitates replenishment of release sites, for example, via speeding AZ clearance of exocytosed material, in addition to a role of AP-2 (zeige TFAP2A ELISA Kits ) in synaptic vesicle reformation. (
  • Your search returned 34 adaptor related protein complex 2 subunit sigma 1 ELISA ELISA Kit across 3 suppliers. (
  • In this report, we demonstrate that Keap1 functions as a substrate adaptor protein for a Cul3-dependent E3 ubiquitin ligase complex. (
  • Keap1 assembles into a functional E3 ubiquitin ligase complex with Cul3 and Rbx1 that targets multiple lysine residues located in the N-terminal Neh2 domain of Nrf2 for ubiquitin conjugation both in vivo and in vitro. (
  • Our results suggest that the ability of Keap1 to assemble into a functional E3 ubiquitin ligase complex is the critical determinant that controls steady-state levels of Nrf2 in response to cancer-preventive compounds and oxidative stress. (
  • In antigen receptor-stimulated cells, SLAP-2 associated with several tyrosine phosphorylated proteins, including the ubiquitin ligase Cbl. (
  • 3BP2 forms complexes with a number of signaling proteins, such as Zap-70, LAT, phospholipase C γ1 (PLC-γ1), Grb2, Cbl, and Fyn in Jurkat cells ( 6 ) and Vav1, Vav2, PLC-γ, and Syk in Daudi B cells ( 12 ). (
  • Overexpression of SLAP-2 in B and T cell lines specifically impaired antigen receptor-mediated signaling events, including CD69 surface marker upregulation, nuclear factor of activated T cells (NFAT) promoter activation and calcium influx. (
  • Signaling induced by phorbol myristate acetate (PMA) and ionomycin was not significantly reduced, suggesting SLAP-2 functions proximally in the antigen receptor signaling cascade. (
  • B ) A localized signaling complex of three anchored signaling enzymes. (
  • In addition, kinase binding proteins such as 14-3-3 proteins serve as adaptor proteins for signaling networks, whereas proteins such as Sterile 5 (Ste 5) and AKAP79 maintain signaling scaffolds of several kinases or phosphatases (Fig. 1 B) ( 4 ). (
  • Protein modules for the assembly of signaling complexes. (
  • They provide a docking platform for the assembly of multimolecular signaling complexes. (
  • These variations in cellular fate are determined by adaptor proteins that are recruited to the DR signaling complex. (
  • This signaling eventually culminates in the production of proinflammatory cytokines to engage host defense responses and bridge acquired immunity governed by T and B lymphocytes ( 2 ). (
  • NRL proteins coordinate different aspects of phototropin signaling through signaling processes that are conserved in land plants and algae. (
  • Clathrin adaptor AP2 regulates thrombin receptor constitutive internalization and endothelial cell resensitization. (
  • Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor. (
  • The concentration of our recombinant proteins is measured using the absorbance at 280nm. (
  • Recombinant protein fragment corresponding to amino acids 97-383 of human AP2M1 (NP_001020376) produced in E.coli. (
  • The expression of recombinant GST-proteins was induced in Escherichia coli BL21 cells at 37 °C for 2 h by the addition of 1 mM IPTG. (
  • The present invention provides a recombinant DNA that is composed of a promoter, a protein coding region, and the hybrid 3′UTR in a continuous and directional orientation. (
  • 2. The recombinant nucleic acid of claim 1, wherein said first region and said second region are in proximity to each other or are adjacent to each other or overlap with each other or one encompasses the other. (
  • 3. The recombinant nucleic acid of claim 2, wherein the 3′ end of the first region is adjacent to the 5′ end of the second region or the 3′ end of the second region is adjacent to the 5′ end of the first region or the first region is located within the second region. (
  • Recombinant funsion protein containing a sequence corresponding to amino acids 164-423 of human AP1M2 (NP_005489.2). (
  • Belongs to the adaptor complexes large subunit family. (
  • Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. (
  • In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. (
  • A partial increase occurs in knockout cells for the medium subunits of AP-2 and AP-3 complexes, indicating a role for both AP-2 and AP-3. (
  • VAMP7, as well as its t-SNAREs partners syntaxin 8 and Vti1, are co-immunoprecipitated with each of the medium subunits of the AP-1, AP-2, AP-3 and AP-4 complexes. (
  • In this report we used two AP-2 complex-specific inhibitors: a dominant negative mutant of Eps15 (Eps15DIII) that binds to the α subunit of AP-2 complex and a small interference RNA that is specific for the μ2 subunit of AP-2 complex. (
  • Immunofluorescence studies show that Eps15 colocalizes with adaptor protein-2 (AP-2) and partially with clathrin. (
  • The SLAP-2 protein contains an NH 2 -terminal myristoylation consensus sequence and SH3 and SH2 Src homology domains, but lacks a tyrosine kinase domain. (
  • The kinase activity of AAK1, an α-appendage-binding protein, is activated by clathrin. (
  • Purification, crystallization and preliminary X-ray diffraction studies of a complex between G protein-coupled receptor kinase 2 and Gbeta1gamma2. (
  • The IL-1R-associated kinase (IRAK) family, a series of death domain-containing serine/threonine kinases, is also recruited to the receptor complex, and then activated. (
  • calmodulin 2 (phosphorylase kinase, de. (
  • However, yeast two- or three-hybrid studies show that the dileucine motif in HIV Nef interacts mainly with AP-1 and AP-3 and only weakly with AP-2 ( 18 , 19 ). (
  • This result supports the conclusion that VAMP7 directly interacts with both AP-2 and AP-3. (
  • Since the L domain of equine infectious anemia virus (EIAV) contains a Yxxθ motif that interacts with AP-2, we used both wild-type and L domain-defective particles of HIV-1 and EIAV to examine whether the HIV-2 Env EVR function was analogous to L domain activity. (
  • Title: Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration. (
  • Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed. (
  • The N-terminal domain of the μ subunits shows a certain degree of sequence similarity with the σ subunits ( Boehm and Bonifacino, 2001 ), consistent with the notion that it also stabilizes the complex. (
  • 2, Last sequence update) DT 00-JAN-0000 (Rel. (
  • 8. An isolated host cell comprising the expression vector of claim 5 wherein the expression vector of claim 5 comprises a protein coding sequence, and the host cell transiently or encoded in the expression vector of claim 5. (
  • 9. An isolated host cell which is obtained by in vivo injection of the expression vector of claim 5 into a cell, wherein the expression vector of claim 5 comprises a protein coding sequence, and the host cell comprises the expression vector of claim 5 and transiently or encoded in the expression vector of claim 5. (
  • 171 Adaptor-Related Protein Complex 2, mu 1 Subunit (AP2M1) Antibodies from 23 manufacturers are available on (
  • provides proteins, antibodies and immunological kits as well as services used in scientific research, including proteomics, biotechnology and pharmaceutical development. (
  • Ligand-bound GPCRs activate heterotrimeric G proteins, resulting in adenylyl cyclase and phospholipase activation, among other effector systems. (
  • The AP-2 complex is a heterotetramer consisting of two large adaptins (alpha or beta), a medium adaptin (mu), and a small adaptin (sigma). (
  • The structure and function of the beta 2-adaptin appendage domain. (
  • Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1 ), a medium adaptin (mu-type subunit AP2M1 ) and a small adaptin (sigma-type subunit AP2S1 ). (
  • Methods and results This report describes an autosomal recessive form of spastic tetraplegic cerebral palsy with profound intellectual disability, microcephaly, epilepsy and white matter loss in a consanguineous family resulting from a homozygous deletion involving AP4E1 , one of the four subunits of the adaptor protein complex-4 (AP-4), identified by chromosomal microarray analysis. (
  • However, a function for this protein has yet to be established. (
  • Deletion of the COOH terminus of SLAP-2 blocked function and abrogated its association with Cbl. (
  • Understanding the mechanisms involved in growth-factor-receptor downregulation is medically important, as several drugs that interfere with the function and trafficking of ErbB proteins are currently being developed or are already in clinical trials. (
  • In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [ PMID: 11290319 , PMID: 11114498 ]. (
  • HPS5 (ruby-eye 2) function has been recently defined. (
  • This superfamily represents a domain found at the C terminus of ribosomal proteins L7 and L12, and also in the adaptor protein ClpS, forming an alpha/beta sandwich [ PMID: 12235156 ]. (
  • Oxidative damage to biological macromolecules can have profound effects on cellular functions and has been implicated in cancer, inflammation, cardiovascular and neurodegenerative diseases, and aging ( 2 , 3 , 9 , 21 , 39 , 45 ). (
  • We here report that the cellular partner of the GYxxθ motif is the adaptor protein complex AP-2. (
  • The cellular distribution of the chimeric HIV-2/MLV Env was significantly less punctate than the wild-type Env, although confocal analysis revealed an overlap in the steady-state locations of the two proteins. (
  • Cellular proteins differ widely in their lability, ranging from those that are completely stable to those with half-lives measured in minutes. (
  • Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. (
  • Previous work by ourselves and others have shown that SKAP1 can directly bind to other adaptors such as ADAP and RapL. (