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 3.6.1.47Dimerization: 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. (1/190)

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. (2/190)

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)

Mu1B, a novel adaptor medium chain expressed in polarized epithelial cells. (3/190)

The apical and basolateral plasma membrane domains of polarized epithelial cells contain distinct sets of integral membrane proteins. Biosynthetic targeting of proteins to the basolateral plasma membrane is mediated by cytosolic tail determinants, many of which resemble signals involved in the rapid endocytosis or lysosomal targeting. Since these signals are recognized by adaptor proteins, we hypothesized that there could be epithelial-specific adaptors involved in polarized sorting. Here, we report the identification of a novel member of the adaptor medium chain family, named mu1B, which is closely related to the previously described mu1A (79% amino acid sequence identity). Northern blotting and in situ hybridization analyses reveal the specific expression of mu1B mRNA in a subset of polarized epithelial and exocrine cells. Yeast two-hybrid analyses show that mu1B is capable of interacting with generic tyrosine-based sorting signals. These observations suggest that mu1B may be involved in protein sorting events specific to polarized cells.  (+info)

Early endosomes are required for major histocompatiblity complex class II transport to peptide-loading compartments. (4/190)

Antigen presentation to CD4(+) T lymphocytes requires transport of newly synthesized major histocompatibility complex (MHC) class II molecules to the endocytic pathway, where peptide loading occurs. This step is mediated by a signal located in the cytoplasmic tail of the MHC class II-associated Ii chain, which directs the MHC class II-Ii complexes from the trans-Golgi network (TGN) to endosomes. The subcellular machinery responsible for the specific targeting of MHC class II molecules to the endocytic pathway, as well as the first compartments these molecules enter after exit from the TGN, remain unclear. We have designed an original experimental approach to selectively analyze this step of MHC class II transport. Newly synthesized MHC class II molecules were caused to accumulate in the Golgi apparatus and TGN by incubating the cells at 19 degrees C, and early endosomes were functionally inactivated by in vivo cross-linking of transferrin (Tf) receptor-containing endosomes using Tf-HRP complexes and the HRP-insoluble substrate diaminobenzidine. Inactivation of Tf-containing endosomes caused a marked delay in Ii chain degradation, peptide loading, and MHC class II transport to the cell surface. Thus, early endosomes appear to be required for delivery of MHC class II molecules to the endocytic pathway. Under cross-linking conditions, most alphabetaIi complexes accumulated in tubules and vesicles devoid of gamma-adaptin and/or mannose-6-phosphate receptor, suggesting an AP1-independent pathway for the delivery of newly synthesized MHC class II molecules from the TGN to endosomes.  (+info)

Gamma-synergin: an EH domain-containing protein that interacts with gamma-adaptin. (5/190)

The AP-1 adaptor complex is associated with the TGN, where it links selected membrane proteins to the clathrin lattice, enabling these proteins to be concentrated in clathrin-coated vesicles. To identify other proteins that participate in the clathrin-coated vesicle cycle at the TGN, we have carried out a yeast two- hybrid library screen using the gamma-adaptin subunit of the AP-1 complex as bait. Two novel, ubiquitously expressed proteins were found: p34, which interacts with both gamma-adaptin and alpha-adaptin, and gamma-synergin, an alternatively spliced protein with an apparent molecular mass of approximately 110-190 kD, which only interacts with gamma-adaptin. gamma-Synergin is associated with AP-1 both in the cytosol and on TGN membranes, and it is strongly enriched in clathrin-coated vesicles. It binds directly to the ear domain of gamma-adaptin and it contains an Eps15 homology (EH) domain, although the EH domain is not part of the gamma-adaptin binding site. In cells expressing alpha-adaptin with the gamma-adaptin ear, a construct that goes mainly to the plasma membrane, much of the gamma-synergin is also rerouted to the plasma membrane, indicating that it follows AP-1 onto membranes rather than leading it there. The presence of an EH domain suggests that gamma-synergin links the AP-1 complex to another protein or proteins.  (+info)

Duplications on human chromosome 22 reveal a novel Ret Finger Protein-like gene family with sense and endogenous antisense transcripts. (6/190)

Analysis of 600 kb of sequence encompassing the beta-prime adaptin (BAM22) gene on human chromosome 22 revealed intrachromosomal duplications within 22q12-13 resulting in three active RFPL genes, two RFPL pseudogenes, and two pseudogenes of BAM22. The genomic sequence of BAM22vartheta1 shows a remarkable similarity to that of BAM22. The cDNA sequence comparison of RFPL1, RFPL2, and RFPL3 showed 95%-96% identity between the genes, which were most similar to the Ret Finger Protein gene from human chromosome 6. The sense RFPL transcripts encode proteins with the tripartite structure, composed of RING finger, coiled-coil, and B30-2 domains, which are characteristic of the RING-B30 family. Each of these domains are thought to mediate protein-protein interactions by promoting homo- or heterodimerization. The MID1 gene on Xp22 is also a member of the RING-B30 family and is mutated in Opitz syndrome (OS). The autosomal dominant form of OS shows linkage to 22q11-q12. We detected a polymorphic protein-truncating allele of RFPL1 in 8% of the population, which was not associated with the OS phenotype. We identified 6-kb and 1.2-kb noncoding antisense mRNAs of RFPL1S and RFPL3S antisense genes, respectively. The RFPL1S and RFPL3S genes cover substantial portions of their sense counterparts, which suggests that the function of RFPL1S and RFPL3S is a post-transcriptional regulation of the sense RFPL genes. We illustrate the role of intrachromosomal duplications in the generation of RFPL genes, which were created by a series of duplications and share an ancestor with the RING-B30 domain containing genes from the major histocompatibility complex region on human chromosome 6.  (+info)

A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells. (7/190)

Although polarized epithelial cells are well known to maintain distinct apical and basolateral plasma membrane domains, the mechanisms responsible for targeting membrane proteins to the apical or basolateral surfaces have remained elusive. We have identified a novel form of the AP-1 clathrin adaptor complex that contains as one of its subunits mu1B, an epithelial cell-specific homolog of the ubiquitously expressed mu1A. LLC-PK1 kidney epithelial cells do not express mu1B and missort many basolateral proteins to the apical surface. Stable expression of mu1B selectively restored basolateral targeting, improved the overall organization of LLC-PK1 monolayers, and had no effect on apical targeting. We conclude that basolateral sorting is mediated by an epithelial cell-specific version of the AP-1 complex containing mu1B.  (+info)

Association of AP1 adaptor complexes with GLUT4 vesicles. (8/190)

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)

AP1S3_HUMAN] Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. Involved in TLR3 trafficking (PubMed:24791904).[1] [AP1G1_MOUSE] Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. [BST2_HUMAN] IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell ...
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, ...
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 …
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.
The endocytic pathway is essential for cell homeostasis and numerous small GTPase Rab have been involved in its control. The endocytic trafficking step controlled by Rab4b has not been elucidated although recent data suggested it could be important for glucose homeostasis, synaptic homeostasis, or adaptative immunity. Here we show that Rab4b is required for early endosome sorting of transferrin receptors (TfR) to the recycling endosomes and we identified the AP1γ subunit of the clathrin adaptor AP-1 as a Rab4b effector and key component of the machinery of early endosomes sorting. We show that internalized transferrin (Tf) does not reach Vamp3/Rab11 recycling endosomes in absence of Rab4b while it is rapidly recycled back to the plasma membrane. On the contrary, Rab4b overexpression leads to the accumulation of internalized Tf within AP-1 and clathrin-coated vesicles. These vesicles are poor in early and recycling endocytic markers except TfR and require AP1γ for their formation. Furthermore, ...
beta-Adaptin antibody [N3C1], Internal (adaptor-related protein complex 1, beta 1 subunit) for WB. Anti-beta-Adaptin pAb (GTX101753) is tested in Human, Mouse samples. 100% Ab-Assurance.
EpsinR is a clathrin-coated vesicle (CCV) enriched 70-kD protein that binds to phosphatidylinositol-4-phosphate, clathrin, and the gamma appendage domain of the adaptor protein complex 1 (AP1). In cells, its distribution overlaps with the perinuclear pool of clathrin and AP1 adaptors. Overexpression disrupts the CCV-dependent trafficking of cathepsin D from the trans-Golgi network to lysosomes and the incorporation of mannose-6-phosphate receptors into CCVs. These biochemical and cell biological data point to a role for epsinR in AP1/clathrin budding events in the cell, just as epsin1 is involved in the budding of AP2 CCVs. Furthermore, we show that two gamma appendage domains can simultaneously bind to epsinR with affinities of 0.7 and 45 microM, respectively. Thus, potentially, two AP1 complexes can bind to one epsinR. This high affinity binding allowed us to identify a consensus binding motif of the form DFxDF, which we also find in gamma-synergin and use to predict that an uncharacterized EF-hand
Journal de Physique II, Journal de Physique Archives représente une mine dinformations facile à consulter sur la manière dont la physique a été publiée depuis 1872.
Katya Heldwein, PhD, Principal Investigator. Katya received her PhD from Oregon Health Sciences University in Portland, OR where she studied ligand recognition by bacterial transcription regulators using x-ray crystallography in the laboratory of Richard Brennan. She then did her postdoctoral work at Harvard Medical School in the laboratory of Stephen Harrison where she initially worked on clathrin adaptor complexes and later delved into herpesvirus cell entry. She opened her own laboratory at Tufts University School of Medicine in the Fall of 2006.. ...
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This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth.
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 ...
Previous work showed that UNC 101 and DPY 23 are adaptins orthologous to the mu1 and mu2 subunits of adaptor protein complex 1 and 2, and that they both can act as negative modulators of LET 23 Regorafenib chemical structure signalling. Similarly, SLI 1 is orthologous to CBL, an E3 ubiquitin ligase targeting LET 23 for degradation and SEM 5 is GRB2, an adaptor molecule that physically interact with EGFR. To address whether these genes could interact with cdt 2, we used loss of function alleles of dpy 23 AP2, unc 101 AP1, sli 1 CBL, and sem 5 GRB2 and performed cdt 2. We found that cdt 2 genetically interacts with dpy 23lf and unc 101lf, as cdt 2 RNAi induces a Muv phenotype in these back grounds. In contrast, no interaction was seen with sli 1lf or sem 5lf.. Since an absence of genetic interaction can sometimes suggest a physical interaction, we tested whether CDT 2 could physically interact with either SLI 1 or SEM 5. We produced in vitro labelled CDT 2 and puri fied SLI 1 and SEM 5 from ...
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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…
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 ...
Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways (PubMed:10066790, PubMed:10436028). AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system. It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons. AP-4 is involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos, but may also recognize other types of sorting signal (Probable). ...
K01602 ribulose-bisphosphate carboxylase small chain [EC:4.1.1.39] , (RefSeq) ribulose bisphosphate carboxylase small chain, ...
K01602 ribulose-bisphosphate carboxylase small chain [EC:4.1.1.39] , (RefSeq) ribulose bisphosphate carboxylase small chain A, chloroplastic- ...
npu:Npun_F4197 K01602 ribulose-bisphosphate carboxylase small chain [EC:4.1.1.39] , (GenBank) ribulose bisphosphate carboxylase, small chain RbcS (A) MQTLPKERRYETLSYLPPLSDAQIAKQIQYILNQGYIPAIEFNETSEPTELYWTMWKLPL FGAKSTQEVLSEVQGCRSQFNGSYIRVVGFDNIKQCQVLSFLVHKPNRY ...
One of the goals of this workout is to avoid "dumping the chain" into the hardest gear for a sprint. Sprinting starts out with a hard jump. As you "wind" out each gear, you shift down one. Just like driving a stick-shift car, you work down the gears when the rpms reach the correct range. After warming up, begin six sprints in the small chain ring with no gear changes, riding 50 meters and winding the gears out. Rest 2-3 minutes between sprints. Then do three sprints in the big chain ring, shifting once. Rest 2-3 minutes after each sprint. Next do three big chainring sprints two gear changes. Finish with one big-ring sprint with three gear changes. Cool down.. ...
The journal focuses on neuroimmunology and neuroinflammation, and the coverage extends to other basic and clinical studies related to neuroscience including molecular biology, psychology, pathology, physiology, endocrinology, pharmacology, oncology, etc.
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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 ...
The heterotetrameric adaptor protein (AP) complexes sort integral membrane proteins at various stages of the endocytic and ... "Entrez Gene: AP4B1 adaptor-related protein complex 4, beta 1 subunit". Hirst J, Bright NA, Rous B, Robinson MS (August 1999). " ... Hirst J, Bright NA, Rous B, Robinson MS (1999). "Characterization of a fourth adaptor-related protein complex". Mol. Biol. Cell ... 2001). "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using ...
"Entrez Gene: AP1S1 adaptor-related protein complex 1, sigma 1 subunit". Montpetit A, Côté S, Brustein E, Drouin CA, Lapointe L ... Boehm M, Aguilar RC, Bonifacino JS (Nov 2001). "Functional and physical interactions of the adaptor protein complex AP-4 with ... The protein encoded by this gene is part of the clathrin coat assembly complex which links clathrin to receptors in coated ... Fölsch H, Ohno H, Bonifacino JS, Mellman I (Oct 1999). "A novel clathrin adaptor complex mediates basolateral targeting in ...
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. ... "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using yeast three- ...
"Entrez Gene: AP1M1 adaptor-related protein complex 1, mu 1 subunit". Hinners I, Wendler F, Fei H, Thomas L, Thomas G, Tooze SA ... The protein encoded by this gene is the medium chain of the trans-Golgi network clathrin-associated protein complex AP-1. 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 ...
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, ... Kim YM, Benovic JL (Aug 2002). "Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein- ... 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, ... This gene encodes a subunit of the heterotetrameric coat assembly protein complex 2 (AP2), which belongs to the adaptor ... "Study of the interaction of the medium chain mu 2 subunit of the clathrin-associated adapter protein complex 2 with cytotoxic T ... "Study of the interaction of the medium chain mu 2 subunit of the clathrin-associated adapter protein complex 2 with cytotoxic T ...
Adaptor protein complex 1 is found at the cytoplasmic face of coated vesicles located at the Golgi complex, where it mediates ... "Entrez Gene: AP1B1 adaptor-related protein complex 1, beta 1 subunit". Nakagawa, T; Setou M; Seog D; Ogasawara K; Dohmae N; ... The protein encoded by this gene serves as one of the large subunits of this complex and is a member of the adaptin protein ... 2001). "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using ...
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 ... Adaptins, together with medium and small subunits, form a heterotetrameric complex called an adaptor, whose role is to promote ... protein along with the complex is thought to function at some trafficking step in the complex pathways between the trans-Golgi ...
"Entrez Gene: AP3S1 adaptor-related protein complex 3, sigma 1 subunit". Human AP3S1 genome location and AP3S1 gene details page ... Dell'Angelica EC, Ohno H, Ooi CE, Rabinovich E, Roche KW, Bonifacino JS (Apr 1997). "AP-3: an adaptor-like protein complex with ... 2003). "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1". Dev. Cell. 5 (3): 513-21. doi:10.1016/ ... Simpson F, Peden AA, Christopoulou L, Robinson MS (1997). "Characterization of the adaptor-related protein complex, AP-3". J. ...
"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 ... Simpson F, Peden AA, Christopoulou L, Robinson MS (May 1997). "Characterization of the adaptor-related protein complex, AP-3". ... Dell'Angelica EC, Klumperman J, Stoorvogel W, Bonifacino JS (Apr 1998). "Association of the AP-3 adaptor complex with clathrin ...
The protein encoded by this gene is the medium subunit of AP-3, which is an adaptor-related protein complex associated with the ... "Entrez Gene: AP3M1 adaptor-related protein complex 3, mu 1 subunit". Human AP3M1 genome location and AP3M1 gene details page in ... AP-3 is a heterotetrameric protein complex composed of two large subunits (delta and beta3), a medium subunit (mu3), and a ... Drake MT, Zhu Y, Kornfeld S (2001). "The assembly of AP-3 adaptor complex-containing clathrin-coated vesicles on synthetic ...
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. ... the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes ...
The family routinely lies on the clathrin adaptor complex 3 beta-1 subunit proteins. The exact function of DUF 1682 is unclear ... The final protein is thought to be translated from the endoplasmic reticulum into the cytoplasm of the cell. The protein is ... "Protein One". Transcription Factors. Retrieved 29 March 2014. "Protein Spotlight, The PAR b ZIP Family". Retrieved March 28, ... The portion of the protein which extends into the cytosol is predicted to be highly phosphorylated as the protein's ...
"Entrez Gene: AP1S2 adaptor-related protein complex 1, sigma 2 subunit". Piccini M, Vitelli F, Bruttini M, Pober BR, Jonsson JJ ... Adaptor protein complex 1 is found on the cytoplasmic face of vesicles located at the Golgi complex, where it mediates both the ... This nucleolar protein is involved in the processing and modification of tRNA. GDI1: RabGDI alpha makes a complex with ... "Mutations in the Gene Encoding the Sigma 2 Subunit of the Adaptor Protein 1 Complex, AP1S2, Cause X-Linked Mental Retardation ...
"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. ... "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1". Developmental Cell. 5 (3): 513-21. doi:10.1016/ ... and 3 ADP-ribosylation factors with adaptor protein complexes 1 and 3". Biochemistry. 41 (14): 4669-77. doi:10.1021/bi016064j. ...
"The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3". Journal of Cell Science. 118 (Pt ... "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1". Developmental Cell. 5 (3): 513-21. doi:10.1016/ ... Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1 is an enzyme that in humans is encoded by the AGAP1 gene. ... The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 6 (3): 197-205 ...
... 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. ...
Nie Z, Fei J, Premont RT, Randazzo PA (2005). "The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes ... Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2 is a protein that in humans is encoded by the AGAP2 gene. ... Werden SJ, Barrett JW, Wang G, Stanford MM, McFadden G (2007). "M-T5, the ankyrin repeat, host range protein of myxoma virus, ... A nuclear gtpase that enhances PI3kinase activity and is regulated by protein 4.1N". Cell. 103 (6): 919-30. doi:10.1016/S0092- ...
AP complexes mediate trafficking linking clathrin or other coat proteins to receptors in coated vesicles, selectively sorting ... which codes for the smallest subunit of the AP1 adaptor complex. The AP-1 complex is one of five Adaptor Protein complexes that ... Rychik, J.; Spray, T.L. (2002). "Strategies to treat protein-losing enteropathy". Semin Thorac Cardiovasc Surg Pediatr Card ... The AP-1 complex is found in the trans-Golgi network and is responsible for controlling AP-1-coated vesicles and the ...
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 ...
In parallel, when toll-like receptors in the endocytic compartments recognize a virus the activation of the adaptor protein ... Bacteria and fungi may form complex biofilms, protecting from immune cells and proteins; biofilms are present in the chronic ... This leads to antiviral protein production, such as protein kinase R, which inhibits viral protein synthesis, or the 2′,5′- ... "Resistance" (R) proteins, encoded by R genes, are widely present in plants and detect pathogens. These proteins contain domains ...
"Entrez Gene: AP1M2 adaptor-related protein complex 1, mu 2 subunit". Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot ... This gene encodes a subunit of the heterotetrameric adaptor-related protein complex 1 (AP-1), which belongs to the adaptor ... Fölsch H, Ohno H, Bonifacino JS, Mellman I (Oct 1999). "A novel clathrin adaptor complex mediates basolateral targeting in ... the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes ...
... "p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene". J ... Ren R, Ye ZS, Baltimore D (April 1994). "Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding ... Bai RY, Jahn T, Schrem S, Munzert G, Weidner KM, Wang JY, Duyster J (August 1998). "The SH2-containing adapter protein GRB10 ... Welch PJ, Wang JY (November 1993). "A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl ...
AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... The two major types of clathrin adaptor complexes are the heterotetrameric adaptor protein (AP) complexes, and the monomeric ... and adaptor complexes that link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to ... Touz MC, Kulakova L, Nash TE (July 2004). "Adaptor protein complex 1 mediates the transport of lysosomal proteins from a Golgi- ...
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; ... AP2 adaptors) complex found in clathrin coated vesicles. The AP-2 complex is a heterotetramer consisting of two large adaptins ... 1996). "Interaction of Shc with adaptor protein adaptins". J. Biol. Chem. 271 (9): 5265-9. doi:10.1074/jbc.271.9.5265. PMID ...
adapter-related protein complex 5 mu subunit. adapter-related protein complex 5 subunit mu-1. adaptor related protein complex 5 ... adaptor related protein complex 5 subunit mu 1provided by HGNC. Primary source. HGNC:HGNC:20192 See related. Ensembl: ... The fifth adaptor protein complex. Hirst J, et al. PLoS Biol, 2011 Oct. PMID 22022230, Free PMC Article ... AP5M1 adaptor related protein complex 5 subunit mu 1 [ Homo sapiens (human) ] Gene ID: 55745, updated on 13-Mar-2020 ...
AP-2 complex subunit beta. Names. adapter-related protein complex 2 beta subunit. adapter-related protein complex 2 subunit ... adaptor protein complex AP-2 subunit beta. adaptor related protein complex 2 beta 1 subunit. adaptor-related protein complex 2 ... clathrin assembly protein complex 2 beta large chain. clathrin-associated/assembly/adaptor protein, large, beta 1. plasma ... a virally encoded peripheral membrane protein. Nef binds to the adaptor protein (AP) complexes of coated vesicles, inducing an ...
Compare adaptor related protein complex 3 subunit mu 1 ELISA Kits from leading suppliers on Biocompare. View specifications, ... adaptor related protein complex 3 subunit mu 1 ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a widely used ... Your search returned 14 adaptor related protein complex 3 subunit mu 1 ELISA ELISA Kit across 2 suppliers. ... Watch Webinar: How To Get Speed and Depth in your Host Cell Protein (HCP) Analysis ...
Adaptor-related protein complex 1 subunit sigma-1C, Clathrin assembly protein complex 1 sigma-1C small chain, Golgi adaptor HA1 ... Adaptor protein complex AP-1 subunit sigma-1C, ... AP1S3 - adaptor-related protein complex 1, sigma 3.... Homo ... wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary ... knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound ...
... adaptor related protein complex 4 sigma 1 subunit), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol. ... transporter activity clathrin-coated pit protein transporter activity protein transport endosome lumen trans-Golgi network ... transporter activity clathrin-coated pit protein transporter activity protein transport endosome lumen trans-Golgi network ... Protein : pattern, domain, 3D structure. UniProt/SwissProt. Q9Y587 [function] [subcellular_location] [family_and_domains] [ ...
... plasma membrane adaptor AP-2 50kDA protein , adaptor protein complex AP-2, mu1 , adaptor-related protein complex AP-2, mu1 , ... adapter-related protein complex 2 mu subunit , adaptin-mu2 , adaptor protein complex AP-2 subunit mu , clathrin adaptor complex ... anti-Adaptor-Related Protein Complex 2, alpha 2 Subunit Antibodies * anti-Adaptor-Related Protein Complex 2, alpha 1 Subunit ... anti-Adaptor-Related Protein Complex 3, beta 2 Subunit Antibodies * anti-Adaptor-Related Protein Complex 3, delta 1 Subunit ...
... adapter-related protein complex 2 mu subunit , adaptin-mu2 , adaptor protein complex AP-2 subunit mu , clathrin adaptor complex ... adaptor protein complex AP-2, mu1 , clathrin assembly protein complex 2 medium chain A , clathrin coat assembly protein AP50-A ... plasma membrane adaptor AP-2 50 kDa protein , adaptor-related protein complex 2, mu 1 subunit , AP-2 complex subunit mu-like , ... adaptor-related protein complex AP-2, mu1 , clathrin-associated AP-2 , coat assembly protein complex 50 kD , HA2 50 kDa subunit ...
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 ... 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. ...
OMIM: ADAPTOR-RELATED PROTEIN COMPLEX 4, EPSILON-1 SUBUNIT; AP4E1, 613744*Gene Ontology: Ap4e1 *Mouse Phenome DB: Ap4e1 *UCSC: ... adaptor-related protein complex AP-4, epsilon 1. Synonyms: 2310033A20Rik. Gene nomenclature, locus information, and GO, OMIM, ... Vega: OTTMUSG16016 (Ap4e1, "adaptor-related protein complex AP-4, epsilon 1")*CCDS: 17696.1, 38231* ... Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International + ...
What is Adapter-related protein complex 3 subunit beta-1? Meaning of Adapter-related protein complex 3 subunit beta-1 medical ... What does Adapter-related protein complex 3 subunit beta-1 mean? ... Looking for online definition of Adapter-related protein ... Adapter-related protein complex 3 subunit beta-1 explanation free. ... redirected from Adapter-related protein complex 3 subunit beta-1) AP3B1. A gene on chromosome 5q14.1 that encodes a subunit of ...
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What is Adaptor protein complex AP-1 subunit beta-1? Meaning of Adaptor protein complex AP-1 subunit beta-1 medical term. What ... Adaptor protein complex AP-1 subunit beta-1 explanation free. ... does Adaptor protein complex AP-1 subunit beta-1 mean? ... Looking for online definition of Adaptor protein complex AP-1 subunit beta-1 in the Medical Dictionary? ... redirected from Adaptor protein complex AP-1 subunit beta-1) AP1B1. A gene on chromosome 22q12.2 that encodes a large subunit ...
... and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon ... The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, ... White boxes represent UTRs (untranslated regions). Orange: protein coding regions. The black lines connecting boxes represent ...
Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in ... adaptor related protein complex 4 subunit beta 1. Enable Javascript to view the expand/collapse boxes.. Open All Close All ... This gene encodes a subunit of a heterotetrameric adapter-like complex 4 that is involved in targeting proteins from the trans- ... It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization ...
adaptor related protein complex 5 subunit zeta 1. Enable Javascript to view the expand/collapse boxes.. Open All Close All ... As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. According to PubMed: ... The encoded protein was found in a complex with other proteins that have a role in HR-DSBR. Knockdown of this gene reduced ...
Protein Coding), Adaptor Related Protein Complex 4 Mu 1 Subunit, including: function, proteins, disorders, pathways, orthologs ... Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in ... Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in ... The encoded protein belongs to the adaptor complexes medium subunits family. This AP-4 complex is involved in the recognition ...
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 ...
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. ...
The yeast clathrin adaptor protein complex 1 is required for the efficient retention of a subset of late Golgi membrane ... The yeast clathrin adaptor protein complex 1 is required for the efficient retention of a subset of late Golgi membrane ... Disruption of the clathrin adaptor protein complex 1 (AP-1) restores Chs3p transport to the plasma membrane. Similarly, in AP-1 ... In yeast, certain resident trans-Golgi network (TGN) proteins achieve steady-state localization by cycling through late ...
603401 ADAPTOR-RELATED PROTEIN COMPLEX 3, BETA-1 SUBUNIT; AP3B1. 608233 HERMANSKY-PUDLAK SYNDROME 2; HPS2. ... Nonsense mutations in ADTB3A cause complete deficiency of the beta3A subunit of adaptor complex-3 and severe Hermansky-Pudlak ...
Adaptor protein 1A (AP-1A) is known to interact with specific motifs in its cargo proteins and with the clathrin heavy chain, ... Adaptor protein 1A (AP-1A) is known to interact with specific motifs in its cargo proteins and with the clathrin heavy chain, ... Cytosolic adaptor proteins, which recognize the cytosolic domains of proteins that span the SG membrane, have been shown to ... Cytosolic adaptor proteins, which recognize the cytosolic domains of proteins that span the SG membrane, have been shown to ...
The complex is part of the protein coat on the cytoplasmic face of coated vesicles which links clathrin to receptors in ... FBXW7 Proteins NEDD4 (Neural Precursor Cell Expressed, Developmentally Down-Regulated 4, E3 Ubiquitin Protein Ligase): NEDD4 ... DLL3 (delta Like Protein 3): DLL3 antibodies DLL3 ELISA Kits DLL3 Proteins ... The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded ...
The complex is part of the protein coat on the cytoplasmic face of coated vesicles which links clathrin to receptors in ... The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded ... This encoded protein is a calcium-dependent serine endoprotease that can efficiently cleave precursor proteins at their paired ... This gene encodes a protein which is similar to the Drosophila crumbs protein and localizes to the inner segment of mammalian ...
Adaptor Protein Complex 4. An adaptor protein complex involved in transport of molecules between the TRANS-GOLGI NETWORK and ... Adaptor Protein Complex 1. A clathrin adaptor protein complex primarily involved in clathrin-related transport at the TRANS- ... A network of membrane compartments, located at the cytoplasmic side of the GOLGI APPARATUS, where proteins and lipids are ... alone and in conjunction with 1) a theory-driven, empirically-informed social network... ...
  • The production of mature SGs requires concentrating newly synthesized soluble content proteins in granules whose membranes contain the appropriate integral membrane proteins. (frontiersin.org)
  • Both D1 and D2 are organized as rings that stack coaxially, with the NTD located at the periphery of the D1 ring ( DeLaBarre and Brunger, 2003 ) ( Figure 1B,C ). p97 converts the energy obtained via ATP hydrolysis to remove substrates from complexes or membranes and to structurally remodel or unfold them ( Barthelme and Sauer, 2016 ). (elifesciences.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)
  • The SCF complex is composed of Skp1, Cullin 1 (Cul1), an F-box protein that serves as a substrate specific adaptor protein, and the ring finger protein Rbx1/Roc1/Hrt1 ( 7 ). (asm.org)
  • We also show that binding of FEZ1 to Kinesin-1 and Munc18 is regulated by phosphorylation, with a conserved site (serine 58) being essential for binding. (pnas.org)
  • This suggests that phosphorylation is a common mechanism for the regulation of kinesin-based transport complexes ( 5 ). (pnas.org)
  • Like other growth factors, insulin uses phosphorylation and the resultant protein-protein interactions as essential tools to transmit and compartmentalize its signal. (jci.org)
  • S381DHE motif of TNFR1-death domain as well as S215LKD and S296LAE motifs of TRADD-death domain) are phosphorylated, and this is required for stable TNFR1-TRADD complex formation and subsequent activation of NF-κB. (jimmunol.org)
  • Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed. (uniprot.org)
  • The N-terminal domain of the μ subunits shows a certain degree of sequence similarity with the σ subunits ( Boehm and Bonifacino, 2001 ), consistent with the notion that it also stabilizes the complex. (biologists.org)
  • Recombinant protein encompassing a sequence within the center region of human AP4M1. (genetex.com)
  • Lu & Werner in "The complete cDNA sequence of mouse elongation factor 1 alpha (EF 1 alpha) mRNA" (NAR, 1989, vol. 17, p. 442). (freepatentsonline.com)
  • 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)
  • 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)
  • Truncation of HDC1 to the ancestral core sequence narrowed the spectrum of interactions and of phenotypic outputs but maintained binding to a H3-binding protein and to H1. (plantphysiol.org)
  • "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. (tcdb.org)
  • TORC1 positively controls protein biosynthesis by regulation of mRNA stability, translation initiation factor activity, and high-affinity amino acid permeases that serve to provide amino acids for use by the translation machinery. (uniprot.org)
  • Osteogenic differentiation was assessed by alkaline phosphatase (ALP) activity, matrix mineralization, mRNA expression of osteogenic factors, runt-related transcription factor 2, osterix, and osteocalcin, and protein levels of collagen type IA (COLIA) and osteopontin (OPN). (chemweb.com)
  • In G 1 , cells become enlarged, mRNA and new proteins are synthesized, and these are then used during the subsequent synthesis of DNA. (news-medical.net)
  • The R402Q mutation of the Tyrosinase Gene: Lack of Association with oculocutaneous albinism type 1 (OCA1). (ingentaconnect.com)
  • Notably, overexpression of spo20 + , encoding a phosphatidylcholine/phosphatidylinositol transfer protein, rescued gdi1-i11 mutation, but not ypt3-i5 or ryh1-i6 . (genetics.org)
  • These professional secretory cells devote as much as half of their total protein synthesis to the production of a single hormone ( 2 ). (frontiersin.org)
  • Depletion of either PAAF1 or Spt6 reduced histone occupancy at the HIV-1 promoter, and induced the synthesis of aberrant transcripts. (cnrs.fr)
  • Interestingly, several groups have recently demonstrated that preparations of HMGB1, which do not induce cytokine synthesis, may form complexes with exogenous or endogenous proinflammatory molecules to strongly enhance their cytokine-inducing ability. (springer.com)
  • Inhibition of mTOR blocks protein synthesis, cell cycle progression, and cell migration. (mdpi.com)
  • DNA and protein synthesis continue throughout G 2 phase. (news-medical.net)