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.
(1/155) 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.

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)

(2/155) Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant mu2 subunit and its effects on endocytosis.

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)

(3/155) Association of AP1 adaptor complexes with GLUT4 vesicles.

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)

(4/155) The leucine-based sorting motifs in the cytoplasmic domain of the invariant chain are recognized by the clathrin adaptors AP1 and AP2 and their medium chains.

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

(5/155) Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based sorting motif.

HIV-1 Nef interacts with cellular adaptor protein (AP) complexes and their medium (mu) subunits. However, the role of the dileucine-based sorting motif within Nef in these interactions has been incompletely characterized. Here, yeast two-hybrid assays indicated that HIV-1 Nef interacted not only with the mu subunits of AP-1 and AP-2, but also with that of AP-3. The interactions with mu1 and mu3 were markedly stronger than the interaction with mu2. Leucine residues of the sorting motif were required for the interactions with mu3 and mu2 and contributed to the interaction with mu1. Confocal immunofluorescence microscopy indicated that Nef, AP-1, and AP-3 (but not AP-2) were concentrated in a juxtanuclear region near the cell center, potentially facilitating interaction between Nef and the mu1 and mu3 subunits. However, leucine residues of the sorting motif were not required for this subcellular localization of Nef. These data suggest that the dileucine motif, required for optimal viral replication, functions through interactions with a variety of AP complexes, including AP-3, potentially by recruiting adaptor complexes to subcellular locations specified by additional determinants in the Nef protein.  (+info)

(6/155) RLIP76, an effector of the GTPase Ral, interacts with the AP2 complex: involvement of the Ral pathway in receptor endocytosis.

RLIP76 is a modular protein that was identified as a putative effector of Ral, a GTPase activated during Ras signaling. To explore further the contribution of the Ral-RLIP76 pathway to Ras signaling, we have looked for partners of RLIP76. Mu2, the medium chain of the AP2 complex is shown to interact with RLIP76. We show also that in vivo endogenous AP2 and RLIP76 form a complex and that this in vivo interaction is independent of cells being stimulated by a growth factor. Furthermore, RLIP76 differentiates AP2 from AP1 in vivo as RLIP76 differentiates mu2 from mu1 in vitro and in two hybrid assays. We show that activated Ral interferes with both tranferrin receptor endocytosis and epidermal growth factor (EGF) receptor endocytosis in HeLa cells. We propose a model where the Ral-RLIP76 pathway connects signal transduction and endocytosis through interaction on one hand between the Ras-Ral pathway and RLIP, on the other hand between RLIP and proteins belonging to the endocytotic machinery.  (+info)

(7/155) Defective organellar membrane protein trafficking in Ap3b1-deficient cells.

AP-3 is a heterotetrameric protein complex involved in intracellular vesicle transport. Molecular analyses show that Ap3b1, which encodes the AP-3 (&bgr;)3A subunit, is altered in pearl mice. To provide genetic evidence that mutation of Ap3b1 is responsible for the pearl phenotype and to determine the null phenotype, the Ap3b1 gene was disrupted by homologous recombination. Mice homozygous for the resulting allele, Ap3b1(LN), or compound heterozygotes with pearl, displayed phenotypes similar to those of pearl mice, confirming that Ap3b1 is the causal gene for pearl. Moreover, pearl is likely to be a hypomorph as the Ap3b1(LN) homozygotes had a lighter coat color and accumulated fewer of the micro3 and (&dgr;)3 subunits of AP-3 than did pearl mice. Finally, immunofluorescence analysis of fibroblasts and melanocytes cultured from Ap3b1(LN) homozygotes revealed that the lysosomal membrane proteins Lamp I and Lamp II and the melanosomal membrane protein tyrosinase were mislocalized. In particular, the Lamp proteins were clustered on the cell surface. These findings strengthen the evidence for an alternate pathway via the plasma membrane for cargo normally transported to organelles by AP-3.  (+info)

(8/155) Multiple C-terminal motifs of the 46-kDa mannose 6-phosphate receptor tail contribute to efficient binding of medium chains of AP-2 and AP-3.

The interaction of adaptor protein (AP) complexes with signal structures in the cytoplasmic domains of membrane proteins is required for intracellular sorting. Tyrosine- or dileucine-based motifs have been reported to bind to medium chain subunits (mu) of AP-1, AP-2, or AP-3. In the present study, we have examined the interaction of the entire 67-amino acid cytoplasmic domain of the 46-kDa mannose 6-phosphate receptor (MPR46-CT) containing tyrosine- as well as dileucine-based motifs with mu2 and mu3A chains using the yeast two-hybrid system. Both mu2 and mu3A bind specifically to the MPR46-CT. In contrast, mu3A fails to bind to the cytoplasmic domain of the 300-kDa mannose 6-phosphate receptor. Mutational analysis of the MPR46-CT revealed that the tyrosine-based motif and distal sequences rich in acidic amino acid residues are sufficient for effective binding to mu2. However, the dileucine motif was found to be one part of a consecutive complex C-terminal structure comprising tyrosine and dileucine motifs as well as clusters of acidic residues necessary for efficient binding of mu3A. Alanine substitution of 2 or 4 acidic amino acid residues of this cluster reduces the binding to mu3A much more than to mu2. The data suggest that the MPR46 is capable of interacting with different AP complexes using multiple partially overlapping sorting signals, which might depend on posttranslational modifications or subcellular localization of the receptor.  (+info)

*  CENTG2
"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 ...
*  AP3D1
"Entrez Gene: AP3D1 adaptor-related protein complex 3, delta 1 subunit". Martinez-Arca S, Rudge R, Vacca M, Raposo G, Camonis J ... "Characterization of the adaptor-related protein complex, AP-3". The Journal of Cell Biology. 137 (4): 835-45. doi:10.1083/jcb. ... "Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based sorting ... "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1". Developmental Cell. 5 (3): 513-21. doi:10.1016/ ...
*  AP3S2
"Entrez Gene: AP3S2 adaptor-related protein complex 3, sigma 2 subunit". Dell'Angelica, E C; Ooi C E; Bonifacino J S (Jun 1997 ... 2003). "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1". Dev. Cell. 5 (3): 513-21. doi:10.1016/ ... an adaptor-like protein complex with ubiquitous expression". EMBO J. 16 (5): 917-28. doi:10.1093/emboj/16.5.917. PMC 1169692 . ... 2002). "Role of adaptor complex AP-3 in targeting wild-type and mutated CD63 to lysosomes". Mol. Biol. Cell. 13 (3): 1071-82. ...
*  AP3S1
"Entrez Gene: AP3S1 adaptor-related protein complex 3, sigma 1 subunit". Human AP3S1 genome location and AP3S1 gene details page ... 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. ... an adaptor-like protein complex with ubiquitous expression". EMBO J. 16 (5): 917-28. doi:10.1093/emboj/16.5.917. PMC 1169692 . ...
*  AP3B1
"Entrez Gene: AP3B1 adaptor-related protein complex 3, beta 1 subunit". GeneReviews/NCBI/NIH/UW entry on Hermansky-Pudlak ... Simpson F, Peden AA, Christopoulou L, Robinson MS (May 1997). "Characterization of the adaptor-related protein complex, AP-3". ... a subunit of the adaptor-like complex AP-3". The Journal of Biological Chemistry. 272 (24): 15078-84. doi:10.1074/jbc.272.24. ... "Nonsense mutations in ADTB3A cause complete deficiency of the beta3A subunit of adaptor complex-3 and severe Hermansky-Pudlak ...
*  AP3B2
"Entrez Gene: AP3B2 adaptor-related protein complex 3, beta 2 subunit". Human AP3B2 genome location and AP3B2 gene details page ... an adaptor-like protein complex with ubiquitous expression". EMBO J. 16 (5): 917-28. doi:10.1093/emboj/16.5.917. PMC 1169692 . ... is a neuron-specific vesicle coat protein". Cell. 82 (5): 773-83. doi:10.1016/0092-8674(95)90474-3. PMID 7671305. Darnell RB, ... Furneaux HM, Posner JB (Jun 1991). "Antiserum from a patient with cerebellar degeneration identifies a novel protein in ...
*  AP3M1
"Entrez Gene: AP3M1 adaptor-related protein complex 3, mu 1 subunit". Human AP3M1 genome location and AP3M1 gene details page in ... 2000). "Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based ... 2005). "Leucine-specific, functional interactions between human immunodeficiency virus type 1 Nef and adaptor protein complexes ... which is an adaptor-related protein complex associated with the Golgi region as well as more peripheral intracellular ...
*  ARF5
2000). "A New Paxillin-binding Protein, PAG3/Papα/KIAA0400, Bearing an ADP-Ribosylation Factor GTPase-activating Protein ... "ADP-ribosylation factor is functionally and physically associated with the Golgi complex". Proc. Natl. Acad. Sci. U.S.A. 87 (3 ... 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. doi:10.1038 ... The gene products include 6 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF ...
*  AP1G1
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 ... "Interactions between adaptor protein-1 of the clathrin coat and microtubules via type 1a microtubule-associated proteins". The ... "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using yeast three- ...
*  CENTG1
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- ...
*  CCDC47
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 ...
*  Adaptor-related protein complex 2, alpha 1
This gene encodes the alpha 1 adaptin subunit of the adaptor protein 2 (AP2 adaptors) complex found in clathrin coated vesicles ... 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; ... AP-2 complex subunit alpha-1 is a protein that in humans is encoded by the AP2A1 gene. ...
*  Pyroptosis
The formation of the multi-protein complex inflammasome is achieved through the binding of intracellular bacterial, viral or ... Biochemical and mass spectroscopic analysis revealed that this pyroptosome is largely composed of dimers of the adaptor protein ... The interaction between NLRP3 and caspase-1 is via the adaptor protein ASC. ASC contains a caspase activation and recruitment ... Of note, Caspase-1 deficient mice develop normally, arguing that inhibition of this protein would produce beneficial rather ...
*  List of A1 genes, proteins or receptors
... alpha 1 Adaptor-related protein complex 2, alpha 1 Aldehyde dehydrogenase 3 family, member A1 Aldehyde dehydrogenase 4 family, ... alpha 1 RNA binding motif protein, Y-linked, family 1, member A1 Replication protein A1 S100 calcium binding protein A1 Sec61 ... mitochondrial F1 complex, alpha 1 BCL2-related protein A1 Butyrophilin, subfamily 1, member A1 Butyrophilin, subfamily 3, ... DP alpha 1 Major histocompatibility complex, class II, DQ alpha 1 Myosin light chain A1, an actin-binding protein NADH ...
*  Vesicular transport adaptor protein
Most of the adaptor proteins are heterotetramers. In the AP complexes, there are two large proteins (∼100 kD) and two smaller ... Vesicular transport adaptor proteins are proteins involved in forming complexes that function in the trafficking of molecules ... but not closely related to the AP/TSET complexes. The individual proteins of the COPII complex are called SEC proteins, because ... Epsin and AP180 in the ANTH domain are other adaptor proteins that have been reviewed. An important transport complex, COPII, ...
*  COP9 signalosome complex subunit 3
2003). "Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome". EMBO J. 22 (6): 1302-12. doi:10.1093 ... a novel tetratrico peptide repeat-containing adaptor molecule". J. Cell Sci. 116 (Pt 3): 453-61. doi:10.1242/jcs.00243. PMID ... 1998). "The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex". Curr ... Yuryev A, Wennogle LP (2003). "Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis ...
*  Fanconi anemia, complementation group C
Gordon SM, Buchwald M (Jul 2003). "Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid ... "The Fanconi anemia gene product FANCF is a flexible adaptor protein". The Journal of Biological Chemistry. 279 (38): 39421-30. ... Fanconi anemia group C protein is a protein that in humans is encoded by the FANCC gene. The protein encoded by this gene ... A nuclear complex containing FANCC protein (as well as FANCA, FANCF and FANCG) is essential for the activation of the FANCD2 ...
*  CRKL
... "p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene". ... Shi CS, Tuscano J, Kehrl JH (February 2000). "Adaptor proteins CRK and CRKL associate with the serine/threonine protein kinase ... "p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene". ... "B cell antigen receptor signaling induces the formation of complexes containing the Crk adapter proteins". The Journal of ...
*  PIK3R4
... an adaptor protein for the human phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by phosphatidylinositol ... Ligon LA, Shelly SS, Tokito M, Holzbaur EL (2003). "The Microtubule Plus-End Proteins EB1 and Dynactin Have Differential ... 2009). "Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages". Nat. Cell Biol ... transfer protein to the p150.Ptdins 3-kinase complex". J. Biol. Chem. 272 (4): 2477-85. doi:10.1074/jbc.272.4.2477. PMID ...
*  MTMR12
The protein encoded by this gene functions as an adaptor subunit in a complex with an active PtdIns(3)P 3-phosphatase. ... Myotubularin related protein 12 is a protein that in humans is encoded by the MTMR12 gene. Phosphatidylinositide 3-kinase- ... Myotubularin related protein 12". Retrieved 2017-05-19. Nandurkar HH, Layton M, Laporte J, Selan C, Corcoran L, Caldwell KK, ... 3-PAP". Proc. Natl. Acad. Sci. U.S.A. 100 (15): 8660-5. doi:10.1073/pnas.1033097100. PMC 166368 . PMID 12847286. Rose JE, Behm ...
*  AP1M1
"Entrez Gene: AP1M1 adaptor-related protein complex 1, mu 1 subunit". Hinners I, Wendler F, Fei H, Thomas L, Thomas G, Tooze SA ... AP-1 complex subunit mu-1 is a protein that in humans is encoded by the AP1M1 gene. The protein encoded by this gene is the ... Fölsch H, Ohno H, Bonifacino JS, Mellman I (Oct 1999). "A novel clathrin adaptor complex mediates basolateral targeting in ... Fölsch H, Ohno H, Bonifacino JS, Mellman I (Oct 1999). "A novel clathrin adaptor complex mediates basolateral targeting in ...
*  CD28
Ellis JH, Ashman C, Burden MN, Kilpatrick KE, Morse MA, Hamblin PA (June 2000). "GRID: a novel Grb-2-related adapter protein ... Okkenhaug K, Rottapel R (August 1998). "Grb2 forms an inducible protein complex with CD28 through a Src homology 3 domain- ... Association of the TCR of a naive T cell with MHC:antigen complex without CD28:B7 interaction results in a T cell that is ... Schneider H, Cai YC, Prasad KV, Shoelson SE, Rudd CE (Apr 1995). "T cell antigen CD28 binds to the GRB-2/SOS complex, ...
*  PACS1
"HIV-1 Nef protein binds to the cellular protein PACS-1 to downregulate class I major histocompatibility complexes". Nature Cell ... "PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic". The EMBO Journal. 20 (9): 2191-201. ... The PACS-1 protein has a putative role in the localization of trans-Golgi network (TGN) membrane proteins. Mouse and rat ... Phosphofurin acidic cluster sorting protein 1 also known as PACS-1 is a protein that in humans is encoded by the PACS1 gene. ...
*  NCK1
The Nck (non-catalytic region of tyrosine kinase adaptor protein 1) belongs to the adaptor family of proteins. The nck gene was ... Ku GM, Yablonski D, Manser E, Lim L, Weiss A (February 2001). "A PAK1-PIX-PKL complex is activated by the T-cell receptor ... "Induced direct binding of the adapter protein Nck to the GTPase-activating protein-associated protein p62 by epidermal growth ... "The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck". J. Biol. Chem. 273 (33): ...
*  Nucleotide exchange factor
"Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos ... and are often specific to a single protein or class of proteins with which they interact. Nucleoside-diphosphate kinase Guanine ... of nucleoside diphosphates for nucleoside triphosphates bound to other proteins. Many cellular proteins cleave (hydrolyze) ... These changes in turn affect the structural, enzymatic, or signalling properties of the protein. Nucleotide exchange factors ...
*  Interferon
... both type I and type II IFNs activate a member of the CRK family of adaptor proteins called CRKL, a nuclear adaptor for STAT5 ... the phosphorylated eIF-2 forms an inactive complex with another protein, called eIF2B, to reduce protein synthesis within the ... Some viruses can encode proteins that bind to double-stranded RNA (dsRNA) to prevent the activity of RNA-dependent protein ... protein, and vaccinia virus employs using the gene product of its E3L gene, p25. The ability of interferon to induce protein ...
WikiGenes - AP1S3 - adaptor-related protein complex 1, sigma 3...  WikiGenes - AP1S3 - adaptor-related protein complex 1, sigma 3...
Adaptor protein complex AP-1 subunit sigma-1C, Adaptor-related protein complex 1 subunit sigma-1C, Clathrin assembly protein ... complex 1 sigma-1C small chain, Golgi adaptor HA1/AP1 adaptin sigma-1C subunit, ... ... 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 ...
more infohttps://www.wikigenes.org/e/gene/e/130340.html
Adaptor protein complex-4 (AP-4) deficiency causes a novel autosomal recessive cerebral palsy syndrome with microcephaly and...  Adaptor protein complex-4 (AP-4) deficiency causes a novel autosomal recessive cerebral palsy syndrome with microcephaly and...
Adaptor protein complex-4 (AP-4) deficiency causes a novel autosomal recessive cerebral palsy syndrome with microcephaly and ... Adaptor protein complex-4 (AP-4) deficiency causes a novel autosomal recessive cerebral palsy syndrome with microcephaly and ... one of the four subunits of the adaptor protein complex-4 (AP-4), identified by chromosomal microarray analysis. ... Conclusion These findings, along with previous reports of human and mouse mutations in other members of the complex, indicate ...
more infohttp://jmg.bmj.com/content/early/2010/10/23/jmg.2010.082263
ap3s2 Protein, adaptor-related protein complex 3, sigma 2 subunit - Creative BioMart  ap3s2 Protein, adaptor-related protein complex 3, sigma 2 subunit - Creative BioMart
Creative Biomart offer ap3s2 proteins for life sciences research. All the products are rigorously tested to meet the most ... AP3S2;adaptor-related protein complex 3, sigma 2 subunit;AP-3 complex subunit sigma-2;sigma3b;sigma-3B-adaptin;sigma-adaptin 3b ... Protein Function. AP3S2 has several biochemical functions, for example, protein transporter activity. Some of the functions are ... Interacting Protein. AP3S2 has direct interactions with proteins and molecules. Those interactions were detected by several ...
more infohttps://www.creativebiomart.net/symbolsearch_AP3S2.htm
Adapter-related protein complex 3 subunit beta-1 | definition of Adapter-related protein complex 3 subunit beta-1 by Medical...  Adapter-related protein complex 3 subunit beta-1 | definition of Adapter-related protein complex 3 subunit beta-1 by Medical...
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 ...
more infohttps://medical-dictionary.thefreedictionary.com/Adapter-related+protein+complex+3+subunit+beta-1
Ap3b2 - AP-3 complex subunit beta-2 - Mus musculus (Mouse) - Ap3b2 gene & protein  Ap3b2 - AP-3 complex subunit beta-2 - Mus musculus (Mouse) - Ap3b2 gene & protein
... that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate ... In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into ... AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related ... Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two large adaptins (delta-type subunit AP3D1 and beta-type ...
more infohttp://www.uniprot.org/uniprot/Q9JME5
AP3B1 - AP-3 complex subunit beta-1 - Canis lupus familiaris (Dog) - AP3B1 gene & protein  AP3B1 - AP-3 complex subunit beta-1 - Canis lupus familiaris (Dog) - AP3B1 gene & protein
... that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate ... In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into ... AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related ... Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two large adaptins (delta-type subunit AP3D1 and beta-type ...
more infohttp://www.uniprot.org/uniprot/Q7YRF1
Produktübersicht anti-AP3B2 Antikörper  Produktübersicht anti-AP3B2 Antikörper
anti-Adaptor-Related Protein Complex 1 Associated Regulatory Protein Antikörper * anti-Adaptor Related Protein Complex 4 sigma ... anti-Adaptor-Related Protein Complex 2, sigma 1 Subunit Antikörper * anti-Adaptor-Related Protein Complex 2, mu 1 Subunit ... anti-Adaptor-Related Protein Complex 2, beta 1 Subunit Antikörper * anti-Adaptor-Related Protein Complex 2, alpha 2 Subunit ... anti-Adaptor-Related Protein Complex 2, alpha 1 Subunit Antikörper * anti-Adaptor-Related Protein Complex 1, sigma 3 Subunit ...
more infohttps://www.antikoerper-online.de/abstract/Adaptor-Related+Protein+Complex+3%2C+beta+2+Subunit+
AP3M1 Gene - GeneCards | AP3M1 Protein | AP3M1 Antibody  AP3M1 Gene - GeneCards | AP3M1 Protein | AP3M1 Antibody
Protein Coding), Adaptor Related Protein Complex 3 Mu 1 Subunit, including: function, proteins, disorders, pathways, orthologs ... AP3M1 Gene(Protein Coding) Adaptor Related Protein Complex 3 Mu 1 Subunit. ... Protein attributes for AP3M1 Gene. Size:. 418 amino acids. Molecular mass:. 46939 Da. Quaternary structure:. *Adaptor protein ... AP3M1 (Adaptor Related Protein Complex 3 Mu 1 Subunit) is a Protein Coding gene. Among its related pathways are Chaperonin- ...
more infohttp://www.genecards.org/cgi-bin/carddisp.pl?gene=AP3M1
Neutrophil Functional Disorders  Neutrophil Functional Disorders
The complex of these cytosolic proteins then translocates to the membrane, where they attach to the flavocytochrome and ... Badolato R and Parolini S (2007) Novel insights from adaptor protein 3 complex deficiency. Journal of Allergy and Clinical ... These cytosolic proteins are p40phox, p47phox and p67phox and the small GTP‐binding proteins, rac1 or rac2. Activation involves ... The flavocytochrome consists of two proteins, gp91phox (the beta subunit) and p22phox (the alpha subunit), and is inactive ...
more infohttp://www.els.net/WileyCDA/ElsArticle/refId-a0002182.html
Chang Q[au] - PubMed - NCBI  Chang Q[au] - PubMed - NCBI
Adaptor protein-3 complex is required for Vangl2 trafficking and planar cell polarity of the inner ear. ... 1,2-Bis[(3-Methoxyphenyl)Methyl]Ethane-1,2-Dicarboxylic Acid Reduces UVB-Induced Photodamage In Vitro and In Vivo. ... 2019 Oct 3:300060519876753. doi: 10.1177/0300060519876753. [Epub ahead of print] No abstract available. ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed?cmd=search&term=Chang+Q%5Bau%5D&dispmax=50
Produktübersicht anti-AP1S3 Antikörper  Produktübersicht anti-AP1S3 Antikörper
anti-Adaptor-Related Protein Complex 1 Associated Regulatory Protein Antikörper * anti-Adaptor Related Protein Complex 4 sigma ... adapter-related protein complex 1 sigma-1C subunit , adaptor protein complex AP-1 sigma-1C subunit , clathrin assembly protein ... anti-Adaptor-Related Protein Complex 1, sigma 2 Subunit Antikörper * anti-Adaptor-Related Protein Complex 1, mu 2 Subunit ... anti-Adaptor-Related Protein Complex 1, mu 1 Subunit Antikörper * anti-Adaptor-Related Protein Complex 1, gamma 1 Subunit ...
more infohttp://www.antikoerper-online.de/abstract/AdaptorRelated+Protein+Complex+1%2C+sigma+3+Subunit+
EpsinR is an adaptor for the SNARE protein Vti1b  EpsinR is an adaptor for the SNARE protein Vti1b
BLOC-1 complex deficiency alters the targeting of adaptor protein complex-3 cargoes.. Salazar G, Craige B, Styers ML, Newell- ... Sorting of the v-SNARE VAMP7 in Dictyostelium discoideum: a role for more than one Adaptor Protein (AP) complex.. Bennett N, ... EpsinR is an adaptor for the SNARE protein Vti1b. Hirst J, Miller SE, Taylor MJ, Fischer von Mollard G, Robinson MS (2004) ... EpsinR is an adaptor for the SNARE protein Vti1b. MOLECULAR BIOLOGY OF THE CELL, 15(12), p 5593-5602. ...
more infohttps://pub.uni-bielefeld.de/publication/2374294
CENTG2 - Wikipedia  CENTG2 - Wikipedia
"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 ...
more infohttps://en.wikipedia.org/wiki/CENTG2
AP3D1 - Wikipedia  AP3D1 - Wikipedia
"Entrez Gene: AP3D1 adaptor-related protein complex 3, delta 1 subunit". Martinez-Arca S, Rudge R, Vacca M, Raposo G, Camonis J ... "Characterization of the adaptor-related protein complex, AP-3". The Journal of Cell Biology. 137 (4): 835-45. doi:10.1083/jcb. ... "Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based sorting ... "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1". Developmental Cell. 5 (3): 513-21. doi:10.1016/ ...
more infohttps://en.wikipedia.org/wiki/AP3D1
Index by author - May 01, 2018, 177 (1) | Plant Physiology  Index by author - May 01, 2018, 177 (1) | Plant Physiology
The ADAPTOR PROTEIN-3 Complex Mediates Pollen Tube Growth by Coordinating Vacuolar Targeting and Organization Qiang-Nan Feng, ... A chromatin regulatory complex displays two modes of action in regulating the gene expression of a subclade of a transcription ... The ADAPTOR PROTEIN-3 Complex Mediates Pollen Tube Growth by Coordinating Vacuolar Targeting and Organization Qiang-Nan Feng, ... The ADAPTOR PROTEIN-3 Complex Mediates Pollen Tube Growth by Coordinating Vacuolar Targeting and Organization Qiang-Nan Feng, ...
more infohttp://www.plantphysiol.org/content/177/1.index-by-author
Exam 3: Ch 14 Secretory Pathway & Vesicle Budding Flashcards by Molly Gallagher | Brainscape  Exam 3: Ch 14 Secretory Pathway & Vesicle Budding Flashcards by Molly Gallagher | Brainscape
Study Exam 3: Ch 14 Secretory Pathway & Vesicle Budding flashcards from Molly Gallagher ... combination of soluble protein complexes onto the membrane to form a protein vesicle coat ... assembly of vesicle coat proteins (ex. ARF protein, Sar1). Sar1-ATP helps coat proteins bind, hydrolysis to GDP causes release ... when protein coat disassembles, VAMP exposed, binds to syntaxin after Rab-GTP tethering to memb.. forms SNARE complex ...
more infohttps://www.brainscape.com/flashcards/exam-3-ch-14-secretory-pathway-amp-vesicl-3631175/packs/5106499
SMART: AP3B1 C domain annotation  SMART: AP3B1 C domain annotation
This domain lies at the C-terminus of the clathrin-adaptor protein complex-3 beta-1 subunit. The AP-3 complex is associated ... This domain lies at the C terminus of the clathrin-adaptor protein complex-3 beta-1 subunit. The AP-3 complex is associated ... We have recently shown that two proteins related to two of the adaptor subunitsof clathrincoated vesicles, p47 (mu3) and beta- ... Antibodies raisedagainst recombinant delta and sigma3 show that they are the other two subunits ofthe adaptor-like complex. We ...
more infohttp://smart.embl.de/smart/do_annotation.pl?DOMAIN=AP3B1_C&START=822&END=969&E_VALUE=1.58e-78&TYPE=SMART&BLAST=PPSKDVFLLDLDDFNPVSTPVALPTPALSPSLIADLEGLNLSTSSSVINVSTPVFVPTKTHELLHRMHGKGLAAHYCFPRQPCIFSDKMVSVQITLTNTSDRKIENIHIGGKGLPVGMQMHAFHPIDSLEPKGSVTVSVGIDFCDSTQ
SMART: BLVR domain annotation  SMART: BLVR domain annotation
Evaluation of the delta subunit of bovine adaptor protein complex 3 as a receptorfor bovine leukaemia virus. ... to a gene family of the delta subunit of the adaptor protein (AP)complex 3, AP-3. Therefore, bovine cDNAs (boAP3delta) that are ... Click on the protein counts, or double click on taxonomic names to display all proteins containing BLVR domain in the selected ... A boAP3delta protein taggedwith green fluorescent protein was localized in the cytoplasm and incorporatedinto AP-3 in bovine ...
more infohttp://smart.embl.de/smart/do_annotation.pl?DOMAIN=BLVR&BLAST=DUMMY
AGAP3 and Arf6 Regulate Trafficking of AMPA Receptors and Synaptic Plasticity | Journal of Neuroscience  AGAP3 and Arf6 Regulate Trafficking of AMPA Receptors and Synaptic Plasticity | Journal of Neuroscience
2003) Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1. Dev Cell 5:513-521, doi:10.1016/S1534-5807( ... 2005) The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3. J Cell Sci 118:3555-3566, ... 2012) GTP-binding protein-like domain of AGAP1 is protein binding site that allosterically regulates ArfGAP protein catalytic ... SynGAP coimmunoprecipitated with AGAP3, suggesting that they do exist in the same protein complex in the brain (Fig. 1D). ...
more infohttp://www.jneurosci.org/content/33/31/12586.full
Defective AP-3-dependent VAMP8 trafficking impairs Weibel-Palade body exocytosis in Hermansky-Pudlak Syndrome type 2 blood...  Defective AP-3-dependent VAMP8 trafficking impairs Weibel-Palade body exocytosis in Hermansky-Pudlak Syndrome type 2 blood...
Mutations in the AP3B1 gene, which encodes the adaptor protein complex 3 β1 subunit, result in Hermansky-Pudlak syndrome 2, a ... Whole proteome analysis revealed that apart from adaptor protein complex 3 β1 also the micron1 subunit and the v-SNARE VAMP8 ... In this study we have investigated the role of adaptor protein complex 3-dependent mechanisms in trafficking of proteins during ... Our data show that defects in adaptor protein complex 3 dependent maturation of Weibel-Palade bodies impairs exocytosis by ...
more infohttp://www.haematologica.org/content/early/2019/01/07/haematol.2018.207787
  • The AP-3 complex may be directly involved in trafficking to lysosomes or alternatively it may be involved in another pathway, but that mis-sorting in that pathway may indirectly lead to defects in pigment granules (PMID:10024875). (embl.de)
  • This family consists of several bovine specific leukaemia virus receptors which are thought to function as transmembrane proteins, although their exact function is unknown (PMID:12692298). (embl.de)
  • There are 1193 AP3B1_C domains in 1191 proteins in SMART's nrdb database. (embl.de)
  • Taxonomic distribution of proteins containing AP3B1_C domain. (embl.de)
  • The complete taxonomic breakdown of all proteins with AP3B1_C domain is also avaliable . (embl.de)
  • Click on the protein counts, or double click on taxonomic names to display all proteins containing AP3B1_C domain in the selected taxonomic class. (embl.de)
  • Our data show that defects in adaptor protein complex 3 dependent maturation of Weibel-Palade bodies impairs exocytosis by affecting the recruitment of VAMP8. (haematologica.org)
  • It begins with the recruitment of Atg proteins, such as ATG14L and WD‐repeat proteins interacting with phosphoinositides (WIPIs), to the PAS-a step requiring the activity of the class 3, PI3K complex, as well as phosphatidylinositol 3‐phosphate. (embopress.org)
  • Biochemical and mass spectroscopic analysis revealed that this pyroptosome is largely composed of dimers of the adaptor protein ASC (apoptosis-associated speck protein containing a CARD or Caspase activation and recruitment domain). (wikipedia.org)
  • The YMNM motif beginning at tyrosine 170 in particular is critical for the recruitment of SH2-domain containing proteins, especially PI3K, Grb2 and Gads. (wikipedia.org)
  • Does not affect TGF-beta-induced SMAD2 or SMAD3 phosphorylation, nor SMAD2/SMAD4 complex formation. (uniprot.org)
  • Activation involves phosphorylation of the phox proteins and the exchange of GDP bound to the rac for GTP. (els.net)
  • Ras family small G-proteins play major roles in these signaling cascades by activating phosphorylation events that amplify the signal within the cell. (jneurosci.org)
  • The portion of the protein which extends into the cytosol is predicted to be highly phosphorylated as the protein's phosphorylation sites are conserved into the bony fish orthologs. (wikipedia.org)
  • It acts as a docking site for complex-mediated phosphorylation. (wikipedia.org)
  • This renewed glucose tolerance and insulin signaling is caused by the inhibition of the unfolded protein response pathway, particularly the protein IRE1alpha, and its subsequent phosphorylation of IRS-1 that causes insulin signaling to be blocked. (wikipedia.org)
  • CENTG2 belongs to an ADP-ribosylation factor GTPase-activating (ARF-GAP) protein family involved in membrane traffic and actin cytoskeleton dynamics (Nie et al. (wikipedia.org)
  • GTPase switch proteins control. (brainscape.com)
  • To regulate small G-protein-mediated signaling cascades, GTPase activating proteins (GAPs) and GTP exchange factors (GEFs) are necessary to inactivate and activate these signaling cascades, respectively. (jneurosci.org)
  • A nuclear gtpase that enhances PI3kinase activity and is regulated by protein 4.1N". Cell. (wikipedia.org)
  • A boAP3delta protein taggedwith green fluorescent protein was localized in the cytoplasm and incorporatedinto AP-3 in bovine cells. (embl.de)
  • Also, other proteins which involved in the same pathway with AP3S2 were listed below. (creativebiomart.net)
  • This stress causes expression of the unfolded protein response pathway, which leads to a decrease in glucose tolerance and inactivation of insulin signaling in certain cell types. (wikipedia.org)
  • This acceleration of bone loss leads researchers to believe that the pathway for bone metabolism is highly regulated by several proteins that have yet to be discovered or incorporated into a schema. (wikipedia.org)