Adaptor Protein Complex 3: An adaptor protein complex found primarily on perinuclear compartments.Adaptor Protein Complex 1: A clathrin adaptor protein complex primarily involved in clathrin-related transport at the TRANS-GOLGI NETWORK.Adaptor Protein Complex 2: An adaptor protein complex primarily involved in the formation of clathrin-related endocytotic vesicles (ENDOSOMES) at the CELL MEMBRANE.Adaptor Protein Complex 4: An adaptor protein complex involved in transport of molecules between the TRANS-GOLGI NETWORK and the endosomal-lysosomal system.Adaptor Protein Complex Subunits: The subunits that make up the large, medium and small chains of adaptor proteins.Adaptor Protein Complex delta Subunits: 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.Adaptor Protein Complex mu Subunits: 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.Adaptor Proteins, Vesicular Transport: 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.Adaptor Protein Complex gamma Subunits: 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.Adaptor Protein Complex beta Subunits: A family of large adaptin protein complex subunits of approximately 90-130 kDa in size.Adaptor Protein Complex alpha Subunits: 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.Adaptor Proteins, Signal Transducing: 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 enzymesClathrin: 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.Human Characteristics: The fundamental dispositions and traits of humans. (Merriam-Webster's Collegiate Dictionary, 10th ed)Monomeric Clathrin Assembly Proteins: A subclass of clathrin assembly proteins that occur as monomers.GRB2 Adaptor Protein: 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).Shc Signaling Adaptor Proteins: 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.Adaptor Protein Complex sigma Subunits: A family of small adaptin protein complex subunits of approximately 19 KDa in size.Endocytosis: Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.Coated Vesicles: 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.Protein Binding: 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.trans-Golgi Network: 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.Clathrin-Coated Vesicles: 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.Endosomes: Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.Membrane Proteins: 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.Protein Transport: 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.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Molecular Sequence Data: 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.Amino Acid Sequence: 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.Transport Vesicles: 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.PhosphoproteinsCoated Pits, Cell-Membrane: 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.GRB10 Adaptor Protein: 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.Gene Products, nef: 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 Fusion Proteins: 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.src Homology Domains: 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.Multiprotein Complexes: Macromolecular complexes formed from the association of defined protein subunits.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Brefeldin A: A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.Signal Transduction: 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.nef Gene Products, Human Immunodeficiency Virus: Proteins encoded by the NEF GENES of the HUMAN IMMUNODEFICIENCY VIRUS.Mutation: 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.HeLa Cells: 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.Proteins: 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.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Lysosomes: 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)Proto-Oncogene Proteins c-crk: 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.Protein Structure, Tertiary: 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.Transfection: 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.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Protein Interaction Mapping: Methods for determining interaction between PROTEINS.CRADD Signaling Adaptor Protein: 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.Myeloid Differentiation Factor 88: 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.Two-Hybrid System Techniques: 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.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Immunoprecipitation: 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.Tyrosine: A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.Amino Acid Motifs: 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.Intracellular Signaling Peptides and Proteins: 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.Nuclear Proteins: 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.COS Cells: 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).)Models, Biological: 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.GRB7 Adaptor Protein: 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.Precipitin Tests: 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.DNA-Binding Proteins: 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.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Mice, Knockout: 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.Nerve Tissue ProteinsCytoskeletal Proteins: 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 Interaction Domains and Motifs: 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.Saccharomyces cerevisiae Proteins: 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.Jurkat Cells: 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 Protein: 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.HEK293 Cells: A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.Oncogene Proteins: Proteins coded by oncogenes. They include proteins resulting from the fusion of an oncogene and another gene (ONCOGENE PROTEINS, FUSION).Vesicular Transport Proteins: 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 c-cbl: 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, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Cells, Cultured: 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-Tyrosine Kinases: Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.Saccharomyces cerevisiae: 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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Receptors, Interleukin-1: 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.Phosphotyrosine: 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.Macromolecular Substances: 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.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.Immunoblotting: 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.Enzyme Activation: 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.Son of Sevenless Proteins: 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.RNA, Small Interfering: 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.CARD Signaling Adaptor Proteins: 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.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Proto-Oncogene Proteins: 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.Drosophila Proteins: 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.src-Family Kinases: 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.Protein Subunits: 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.Cytoplasm: 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)Phospholipase C gamma: 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.Blotting, Western: 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.Membrane Glycoproteins: Glycoproteins found on the membrane or surface of cells.RNA Interference: 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.Gene Expression Regulation: 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.Ubiquitin-Protein Ligases: 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.Mice, Inbred C57BLCloning, Molecular: 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.Protein-Serine-Threonine Kinases: A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.Sequence Alignment: 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: 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.Cell Cycle Proteins: 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, Fluorescence: 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.Cercopithecus aethiops: 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.LIM Domain Proteins: 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.Toll-Like Receptors: 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.Glutathione Transferase: 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.Ubiquitin: 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.Protein Interaction Maps: Graphs representing sets of measurable, non-covalent physical contacts with specific PROTEINS in living organisms or in cells.Toll-Like Receptor 4: A pattern recognition receptor that interacts with LYMPHOCYTE ANTIGEN 96 and LIPOPOLYSACCHARIDES. It mediates cellular responses to GRAM-NEGATIVE BACTERIA.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Fas-Associated Death Domain Protein: 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.Receptors, Antigen, T-Cell: 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.Ubiquitination: 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.Protein Conformation: 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).Actins: 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.Microfilament Proteins: 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.Protein Multimerization: The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.Green Fluorescent Proteins: 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.Protein Isoforms: Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.Cullin Proteins: 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.14-3-3 Proteins: 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.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Retinoblastoma-Like Protein p130: A negative regulator of the CELL CYCLE that undergoes PHOSPHORYLATION by CYCLIN-DEPENDENT KINASES. RBL2 contains a conserved pocket region that binds E2F4 TRANSCRIPTION FACTOR and E2F5 TRANSCRIPTION FACTOR. RBL2 also interacts with viral ONCOPROTEINS such as POLYOMAVIRUS TUMOR ANTIGENS; ADENOVIRUS E1A PROTEINS; and PAPILLOMAVIRUS E7 PROTEINS.Cell Nucleus: 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)Syntenins: Intracellular signaling adaptor proteins that play a role in the coupling of SYNDECANS to CYTOSKELETAL PROTEINS.Dystrophin-Associated Protein Complex: 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.ZAP-70 Protein-Tyrosine Kinase: A protein tyrosine kinase that is required for T-CELL development and T-CELL ANTIGEN RECEPTOR function.Proto-Oncogene Proteins pp60(c-src): 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, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.T-Lymphocytes: 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.Cytoskeleton: The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.RNA-Binding Proteins: Proteins that bind to RNA molecules. Included here are RIBONUCLEOPROTEINS and other proteins whose function is to bind specifically to RNA.Fungal Proteins: Proteins found in any species of fungus.ADP-Ribosylation Factors: 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 22.214.171.124Dimerization: The process by which two molecules of the same chemical composition form a condensation product or polymer.Golgi Apparatus: 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)DNA, Complementary: 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.Mitogen-Activated Protein Kinases: 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).Phosphatidylinositol 3-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.Bacterial Proteins: Proteins found in any species of bacterium.3T3 Cells: 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.Cell Line, Tumor: A cell line derived from cultured tumor cells.Calcium-Binding Proteins: Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.Protein Processing, Post-Translational: 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.Proteolysis: 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.Protein Structure, Quaternary: The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).RNA, Messenger: 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.PDZ Domains: 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.NF-kappa B: 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.Drosophila: 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.Microscopy, Confocal: 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.Receptors, Cell Surface: 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.DNA Primers: 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.Plasmids: 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.Death Domain Receptor Signaling Adaptor Proteins: 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.Arrestins: Regulatory proteins that down-regulate phosphorylated G-protein membrane receptors, including rod and cone photoreceptors and adrenergic receptors.Receptors, Immunologic: 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.Repressor Proteins: 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.Cell Adhesion: Adherence of cells to surfaces or to other cells.Yeasts: 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.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Ligands: 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)Endosomal Sorting Complexes Required for Transport: 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.Guanine Nucleotide Exchange Factors: Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.TNF Receptor-Associated Factor 6: 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.Receptors, Antigen, B-Cell: 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.Proteomics: The systematic study of the complete complement of proteins (PROTEOME) of organisms.Cell Polarity: 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.Peptides: 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.Coat Protein Complex I: 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.Fibroblasts: Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.Clathrin Heavy Chains: The heavy chain subunits of clathrin.Apoptosis: 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.Receptor Protein-Tyrosine Kinases: A class of cellular receptors that have an intrinsic PROTEIN-TYROSINE KINASE activity.Cell Adhesion Molecules, Neuronal: 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.Kinetics: The rate dynamics in chemical or physical systems.Promoter Regions, Genetic: 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.Toll-Like Receptor 2: 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.Endopeptidase Clp: 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.Gene Deletion: 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.GTPase-Activating Proteins: Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.Down-Regulation: 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.Immunity, Innate: 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.Protein Tyrosine Phosphatase, Non-Receptor Type 11: 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.Receptor, Epidermal Growth Factor: 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.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.Adenosine Triphosphatases: 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.Protein Kinases: A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.MAP Kinase Signaling System: 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.Escherichia coli: 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.Proto-Oncogene Proteins c-fyn: Src-family kinases that associate with T-CELL ANTIGEN RECEPTOR and phosphorylate a wide variety of intracellular signaling molecules.Focal Adhesions: 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.
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). [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.
antibody-antibodies.com 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.
antibody-antibodies.com 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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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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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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... 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. Robinson, Margaret S.; ... 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: 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 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 ...
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 ...
This leads to association with a Shc adaptor protein. Then Shc interacts with GRB2/SoS complex which results in activation of ... and GM-CSF alpha and beta receptor messenger ribonucleic acid and protein in human ovarian tissue". Biology of Reproduction. 53 ... which encodes a truncated protein". American Journal of Hematology. 58 (2): 145-7. doi:10.1002/(SICI)1096-8652(199806)58:2. 3.0 ... "Molecular assembly of the ternary granulocyte-macrophage colony-stimulating factor receptor complex". Blood. 101 (4): 1308-15. ...
"Entrez Gene: AP3S2 adaptor-related protein complex 3, sigma 2 subunit". Dell'Angelica, E C; Ooi C E; Bonifacino J S (Jun 1997 ... 2003). "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1". Dev. Cell. 5 (3): 513-21. doi:10.1016/ ... an adaptor-like protein complex with ubiquitous expression". EMBO J. 16 (5): 917-28. doi:10.1093/emboj/16.5.917. PMC 1169692 . ... 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". ...
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". Human AP1S2 genome location and AP1S2 gene details page ... The protein encoded by this gene serves as the small subunit of this complex and is a member of the adaptin protein family. ... "HIV-1 Nef stabilizes the association of adaptor protein complexes with membranes". The Journal of Biological Chemistry. 278 (10 ...
"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". Martinez-Arca S, Rudge R, Vacca M, Raposo G, Camonis J ... "Characterization of the adaptor-related protein complex, AP-3". The Journal of Cell Biology. 137 (4): 835-45. doi:10.1083/jcb. ... "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: 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 ...
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 ...
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 ...
2001). "Characterization of the CIN85 adaptor protein and identification of components involved in CIN85 complexes". Biochem. ... The B-cell linker protein is encoded by the BLNK gene and is an adaptor protein also known as SLP-65, BASH, and BCA. BLNK is ... Linker or adaptor proteins provide mechanisms by which receptors can amplify and regulate downstream effector proteins. The B- ... "Characterization of the CIN85 Adaptor Protein and Identification of Components Involved in CIN85 Complexes". Biochemical and ...
"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 ...
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 ...
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 ...
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 ...
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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:// ...
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 ...
... 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 ...
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 ...
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 ...
AP1S2 encodes an adaptin protein that constitutes part of the adaptor protein complex found at the cytoplasmic face of coated ... Aberrant endocytic processing through disruption of adaptor protein complexes is likely to result from the AP1S2 mutations ... AP1S2 is the first reported XLMR gene that encodes a protein directly involved in the assembly of endocytic vesicles. ... The complex mediates the recruitment of clathrin to the vesicle membrane. ...
doi: 10.1186/s12872-018-0905-2. Research Support, Non-U.S. Govt ... Adaptor Protein Complex alpha Subunits. *adaptor protein ... Adaptor-related protein complex 2 alpha 2 subunit (AP2A2) gene encodes a protein-a subunit of the AP-2 adaptor protein complex ... A genetic variant near adaptor-related protein complex 2 alpha 2 subunit gene is associated with coronary artery disease in a ... Evidence has revealed that benzodiazepine receptor-associated protein 1 (BZRAP1) is abundant in the hippocampus with potential ...
InteractionsDomain-containTransmembrane proteinsMembrane proteinsInteractionRelated protein complex 1 subunitPlasma membrane adaptorEndocytic adaptor complexMoleculesEndosomesMutationMolecularLipidsCoatCargoBelongsSigmaInteractELISA KitsUbiquitin ligaseAppendage domainMutationsLarge subunitMedium subunitsSequenceTrans-Golgi nReceptorsInternalizationEps15AntibodiesAdaptinAP2M1Cytoplasmic tailsSignalingEndoplasmic reticulumSynaptic
- 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. (antikoerper-online.de)
- V1H can function as an adaptor for interactions between Nef and AP-2 (zeige GTF3A ELISA Kits ). (antikoerper-online.de)
- AP3S2 has direct interactions with proteins and molecules. (creativebiomart.net)
- 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. (rcsb.org)
- 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 ). (sciencemag.org)
- 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 ). (pnas.org)
- 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. (biomedcentral.com)
- 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. (biomedcentral.com)
- In this paper we present a new approach for the detection of putative protein interactions based on expression data. (biomedcentral.com)
- 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. (biomedcentral.com)
- Firstly, protein-protein interactions are more easily identified if the interacting protein pair belongs to a multi-protein complex. (biomedcentral.com)
- Therefore, we focused on tracking interactions within protein complexes, even though our algorithm can, in principle, identify any type of protein-protein interaction. (biomedcentral.com)
- Preventing premature interactions between microtubules and protein-based structures called kinetochores ensures that chromosomes are segregated by meiosis rather than mitosis in reproductive cells. (elifesciences.org)
- 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. (elifesciences.org)
- 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 ). (pubmedcentralcanada.ca)
- To fully appreciate the function and regulation of these neurotransmitter receptors, we must understand their interactions with other proteins. (jneurosci.org)
- The pathway maps illustrate protein interactions and regulation to provide a comprehensive picture of signaling and disease processes. (bio-rad.com)
- 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 ). (jimmunol.org)
- Integrin cell adhesion receptors participate in cell-cell and cell-ECM interactions [ 2 ]. (hindawi.com)
- As a scaffolding protein, CASK participates in multiple interactions. (jneurosci.org)
- Preliminary HDX results for CheA also set a stage for future analysis of the domain interactions of CheA in the functional complexes, and the differences that correlate with kinase activity. (umass.edu)
- This cooperativity explains how Nef is able to efficiently downregulate CD4 despite weak binary interactions between components of the tripartite complex. (genes2cognition.org)
- Interactions of viral protein U (Vpu) with cellular factors. (indigo.ca)
- Imaging of HIV/host protein interactions. (indigo.ca)
- Vpr and its interactions with cellular proteins. (indigo.ca)
- 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. (asm.org)
- 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 ). (asm.org)
- 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. (antibodies-online.com)
- AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. (abcam.com)
- Chemoreceptors are transmembrane proteins that sense chemicals in the environment and use this information to control a phosphorylation cascade that enables the cell to swim towards favorable environments. (umass.edu)
- 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. (pnas.org)
- 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. (pnas.org)
- Robinson and her lab managed to find another AP complex, AP-3, which interacts with lysosomal membrane proteins such as LAMP1. (wikipedia.org)
- The production of mature SGs requires concentrating newly synthesized soluble content proteins in granules whose membranes contain the appropriate integral membrane proteins. (frontiersin.org)
- The mechanisms underlying the sorting of soluble and integral membrane proteins destined for SGs from other proteins are not yet well understood. (frontiersin.org)
- The trafficking of granule membrane proteins can be controlled by both luminal and cytosolic factors. (frontiersin.org)
- Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, l. (xenbase.org)
- Basolateral sorting of human poliovirus receptor alpha involves an interaction with the mu1B subunit of the clathrin adaptor complex in polarized epithelial cells. (nih.gov)
- 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 ). (jimmunol.org)
- 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. (rcsb.org)
- 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. (rcsb.org)
- We recently initiated an effort to systematically identify interaction partners of established presynaptic proteins using an automated yeast two-hybrid (Y2H) screen. (pnas.org)
- For soluble proteins, luminal pH and divalent metals can affect aggregation and interaction with surrounding membranes. (frontiersin.org)
- S-nitrosylation of FLICE inhibitory protein determines its interaction with RIP1 and activation of NF-kappa B. (cdc.gov)
- The N-terminal region of PIDD contains seven leucine-rich repeats (LRRs), a protein interaction motif found in various proteins with diverse functions, followed by two ZU-5 domains and a C-terminal DD. (abcam.com)
- Increased PIDD expression results in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli, via interaction with caspase-2 and CRADD/RAIDD. (abcam.com)
- In this study, we show that the interaction of GPCR-bound arrestin with Adaptor Protein 2 (AP-2) is a critical anti-apoptotic event. (pubmedcentralcanada.ca)
- We demonstrate that this interaction is mediated by the AP-2 mu subunit (Apm4) YXXΦ binding domain. (asm.org)
- Exchange is rapid throughout the CF except in the protein interaction region where CF binds CheA and CheW. (umass.edu)
- The authors have recently described an interaction between Gag and the delta subunit of the AP-3 adaptor protein complex (1). (indigo.ca)
- We selected proteins and molecules interacted with AP3S2 here. (creativebiomart.net)
- The adaptin family of proteins is composed of four classes of molecules named alpha, beta-, beta prime- and gamma- adaptins. (genecards.org)
- 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 ). (asm.org)
- In this review, we compare and contrast the protein modules, adaptor molecules, targeting subunits, and anchoring proteins that coordinate signaling networks. (sciencemag.org)
- Experiments in vitro revealed that, in addition to having direct mitogenic effects, these molecules enhance intercellular PDGF-B signaling in a cell-type specific manner: VEGF-A enhances endothelial PDGF-B expression, whereas FGF-2 enhances mural PDGF receptor β (PDGFR β ) expression. (biologists.org)
- Complex formation between phosphorylated GPCRs, arrestins and an ever-increasing number of effector molecules is known to regulate cellular function. (pubmedcentralcanada.ca)
- 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. (asm.org)
- Integrins act as bidirectional signaling molecules [ 2 ]. (hindawi.com)
- The use of such hybrid regions allows for an efficient protein expression when used in conjunction with circular or linear expression DNA molecules. (freepatentsonline.com)
- 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. (antikoerper-online.de)
- May function in protein sorting in late endosomes or multivesucular bodies (MVBs). (genecards.org)
- 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. (abcam.com)
- In addition, AP-2 associates with the receptor-arrestin complex in perinuclear endosomes and is required for proper post-endocytic GPCR trafficking. (pubmedcentralcanada.ca)
- 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. (biomedsearch.com)
- Mutation of the putative myristoylation site of SLAP-2 compromised its inhibitory activity and impaired its localization to the membrane compartment. (rupress.org)
- The mutation of these residues specifically inhibits the ability of Nef to bind AP-2 and downregulate CD4. (genes2cognition.org)
- In 2003 she was appointed Professor of Molecular Cell Biology at the Cambridge Institute for Medical Research and is conducting research on coated vesicle proteins. (wikipedia.org)
- These units are delivered to the nascent synapse via molecular motor proteins of the kinesin superfamily (reviewed in Ref. 1). (pnas.org)
- However, the molecular mechanism that regulates FLIP within this complex is unknown. (cdc.gov)
- 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. (jneurosci.org)
- 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. (jneurosci.org)
- The apparent molecular mass of both proteins is 142 kD, and they consist of three structural domains. (rupress.org)
- The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. (genecards.org)
- Knowledge of the specific proteins, lipids, and mechanisms required for trafficking and killing by these toxins remains incomplete. (nih.gov)
- GPCRs are activated by a myriad of ligands including amino acids and their derivatives, peptides, proteins, ions, lipids and photons. (pubmedcentralcanada.ca)
- The complex binds polyphosphoinositide-containing lipids. (xenbase.org)
- The complex is part of the protein coat on the cytoplasmic face of coated vesicles which links clathrin to receptors in vesicles. (wikipedia.org)
- Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. (genecards.org)
- 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. (nih.gov)
- She eventually succeeded in purifying components of the coat that were not clathrin and are now known as adaptor proteins. (wikipedia.org)
- 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. (frontiersin.org)
- Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. (abcam.com)
- Affinity chromatography experiments demonstrated that Caskin 1 coassembles with CASK on the immobilized cytoplasmic tail of neurexin 1, suggesting that CASK and Caskin 1 coat the cytoplasmic tails of neurexins and other cell-surface proteins. (jneurosci.org)
- A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex. (nih.gov)
- 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. (antikoerper-online.de)
- Her achievements include the discovery of adaptins, which are specific proteins that manage cell-trafficking to ensure the correct cell cargo is transported to the right location. (wikipedia.org)
- Once on the membrane, the various adaptors would work together to package different types of cargo into the newly forming vesicle. (wikipedia.org)
- 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. (frontiersin.org)
- 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. (asm.org)
- In this Topical Review, we present their main protein components and discuss current models for cargo sorting. (deepdyve.com)
- The AP-2 complex is a heterotetramer consisting of two large adaptins (alpha or beta), a medium adaptin (mu), and a small adaptin (sigma). (wikipedia.org)
- Your search returned 34 adaptor related protein complex 2 subunit sigma 1 ELISA ELISA Kit across 3 suppliers. (biocompare.com)
- The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). (genecards.org)
- 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 ). (rcsb.org)
- GST-fused proteins were purified with the Cell Lytic B protocol (Sigma #B7435). (springer.com)
- 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. (nih.gov)
- Adaptor-related protein complex 2, alpha 1 has been shown to interact with DPYSL2 and NUMB. (wikipedia.org)
- Most of the proteins interact with multiple RNA elements, often from different domains. (ebi.ac.uk)
- Search, Find and Buy Antibodies, ELISA Kits and Proteins. (antibodies-online.com)
- Auf www.antikoerper-online.de finden Sie aktuell 17 Adaptor-Related Protein Complex 2, mu 1 Subunit (AP2M1) ELISA Kits von 5 unterschiedlichen Herstellern. (antikoerper-online.de)
- BMCC1 (zeige PRUNE2 ELISA Kits ) is an AP-2 (zeige GTF3A ELISA Kits ) associated endosomal protein in prostate cancer cells. (antikoerper-online.de)
- Arkadia (zeige RNF111 ELISA Kits ) complexes with clathrin adaptor AP2 (zeige GTF3A ELISA Kits ) mu2 subunit and regulates EGF (zeige EGF ELISA Kits ) signalling. (antikoerper-online.de)
- 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. (antikoerper-online.de)
- 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. (antikoerper-online.de)
- In this report, we demonstrate that Keap1 functions as a substrate adaptor protein for a Cul3-dependent E3 ubiquitin ligase complex. (asm.org)
- 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. (asm.org)
- 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. (asm.org)
- In antigen receptor-stimulated cells, SLAP-2 associated with several tyrosine phosphorylated proteins, including the ubiquitin ligase Cbl. (rupress.org)
- The structure and function of the beta 2-adaptin appendage domain. (nih.gov)
- The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. (genecards.org)
- Indeed, an appendage domain of alpha-adaptin was identified as a protein interacting with the cytoplasmic tail of HM1.24. (genes2cognition.org)
- 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. (ox.ac.uk)
- Huizing M, Scher CD, Strovel E, Fitzpatrick DL, Hartnell LM, Anikster Y, Gahl WA , Nonsense mutations in ADTB3A cause complete deficiency of the beta3A subunit of adaptor complex-3 and severe Hermansky-Pudlak syndrome type 2. (coriell.org)
- 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. (ebi.ac.uk)
- 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. (ebi.ac.uk)
- 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. (biomedsearch.com)
- 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. (biomedsearch.com)
- Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed. (uniprot.org)
- 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. (rupress.org)
- 2, Last sequence update) DT 00-JAN-0000 (Rel. (univ-lyon1.fr)
- 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. (freepatentsonline.com)
- 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. (freepatentsonline.com)
- Recombinant funsion protein containing a sequence corresponding to amino acids 164-423 of human AP1M2 (NP_005489.2). (genetex.com)
- CASK, an adaptor protein of the plasma membrane, is composed of an N-terminal calcium/calmodulin-dependent protein (CaM) kinase domain, central PSD-95, Dlg, and ZO-1/2 domain (PDZ) and Src homology 3 (SH3) domains, and a C-terminal guanylate kinase sequence. (jneurosci.org)
- Caskin 1 and a closely related isoform, Caskin 2, are multidomain proteins containing six N-terminal ankyrin repeats, a single SH3 domain, and two sterile α motif domains followed by a long proline-rich sequence and a short conserved C-terminal domain. (jneurosci.org)
- Cytosolic and membrane-associated proteins involved in the recruitment of AP-1 adaptors onto the trans-Golgi network. (nih.gov)
- Adaptins are important components of clathrin-coated vesicles transporting ligand-receptor complexes from the plasma membrane or from the trans-Golgi network to lysosomes. (genecards.org)
- Soluble N-ethylmaleimide-sensitive-factor Attachment protein Receptors (SNAREs) participate in the specificity of membrane fusions in the cell. (biomedsearch.com)
- 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 ). (sciencemag.org)
- G protein-coupled receptors (GPCR) are involved in virtually every aspect of human physiology including cardiovascular ( 1 ), immune ( 2 ) and neuronal systems ( 3 ). (pubmedcentralcanada.ca)
- 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. (pubmedcentralcanada.ca)
- 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. (jneurosci.org)
- Component of the adaptor complexes which link clathrin to receptors in coated vesicles. (xenbase.org)
- This overproduction was mediated by immune complexes and involved synergistic signaling between the B cell receptor and Toll-like receptors and T cell help. (jci.org)
- This recognition is mediated by a set of germline-encoded receptors called Toll-like receptors (TLRs) 3 ( 1 , 2 , 3 ). (jimmunol.org)
- This large family of heterodimeric transmembrane receptors recognizes a plethora of extracellular ligands, including transmembrane receptors on other cells and ECM proteins. (hindawi.com)
- The receptors form a ternary complex with a histidine kinase, CheA, and an adaptor protein, CheW. (umass.edu)
- 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. (jimmunol.org)
- Immunofluorescence studies show that Eps15 colocalizes with adaptor protein-2 (AP-2) and partially with clathrin. (rupress.org)
- 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. (rupress.org)
- 171 Adaptor-Related Protein Complex 2, mu 1 Subunit (AP2M1) Antibodies from 23 manufacturers are available on www.antibodies-online.com. (antibodies-online.com)
- provides proteins, antibodies and immunological kits as well as services used in scientific research, including proteomics, biotechnology and pharmaceutical development. (biosci.com.au)
- A basic patch on alpha-adaptin is required for binding of human immunodeficiency virus type 1 Nef and cooperative assembly of a CD4-Nef-AP-2 complex. (genes2cognition.org)
- We also present evidence that the diacidic motif on Nef and the basic patch on alpha-adaptin are both required for the cooperative assembly of a CD4-Nef-AP-2 complex. (genes2cognition.org)
- 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 ). (asm.org)
- 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. (rupress.org)
- Signaling induced by phorbol myristate acetate (PMA) and ionomycin was not significantly reduced, suggesting SLAP-2 functions proximally in the antigen receptor signaling cascade. (rupress.org)
- 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. (sciencemag.org)
- B ) A localized signaling complex of three anchored signaling enzymes. (sciencemag.org)
- Protein modules for the assembly of signaling complexes. (sciencemag.org)
- Thus, we demonstrated that the directional enhancement of endogenous PDGF-B-PDGFRβ signaling is indispensable for the synergistic effect of VEGF-A and FGF-2 on neoangiogenesis in adults. (biologists.org)
- 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. (elifesciences.org)
- 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 ). (jimmunol.org)
- NRL proteins coordinate different aspects of phototropin signaling through signaling processes that are conserved in land plants and algae. (plantphysiol.org)
- After integrating with its ligand TRAIL and recruiting adapter proteins, DR5 forms the death-inducing signaling complex and eventually activates caspase cascades 11 . (nature.com)
- AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. (genecards.org)
- 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. (pnas.org)
- 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. (pnas.org)
- 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 ). (pnas.org)