GTP-Binding Proteins: Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.Guanosine Triphosphate: Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.GTP Phosphohydrolases: Enzymes that hydrolyze GTP to GDP. EC 3.6.1.-.rac GTP-Binding Proteins: A sub-family of RHO GTP-BINDING PROTEINS that is involved in regulating the organization of cytoskeletal filaments. This enzyme was formerly listed as EC 3.6.1.47.rho GTP-Binding Proteins: A large family of MONOMERIC GTP-BINDING PROTEINS that are involved in regulation of actin organization, gene expression and cell cycle progression. This enzyme was formerly listed as EC 3.6.1.47.Guanosine Diphosphate: A guanine nucleotide containing two phosphate groups esterified to the sugar moiety.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 3.6.1.47rab GTP-Binding Proteins: A large family of MONOMERIC GTP-BINDING PROTEINS that play a key role in cellular secretory and endocytic pathways. EC 3.6.1.-.Monomeric GTP-Binding Proteins: A class of monomeric, low molecular weight (20-25 kDa) GTP-binding proteins that regulate a variety of intracellular processes. The GTP bound form of the protein is active and limited by its inherent GTPase activity, which is controlled by an array of GTPase activators, GDP dissociation inhibitors, and guanine nucleotide exchange factors. This enzyme was formerly listed as EC 3.6.1.47Guanosine 5'-O-(3-Thiotriphosphate): Guanosine 5'-(trihydrogen diphosphate), monoanhydride with phosphorothioic acid. A stable GTP analog which enjoys a variety of physiological actions such as stimulation of guanine nucleotide-binding proteins, phosphoinositide hydrolysis, cyclic AMP accumulation, and activation of specific proto-oncogenes.Guanine Nucleotide Exchange Factors: Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.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.GTPase-Activating Proteins: Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.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.cdc42 GTP-Binding Protein: A member of the Rho family of MONOMERIC GTP-BINDING PROTEINS. It is associated with a diverse array of cellular functions including cytoskeletal changes, filopodia formation and transport through the GOLGI APPARATUS. This enzyme was formerly listed as EC 3.6.1.47.rhoA GTP-Binding Protein: A RHO GTP-BINDING PROTEIN involved in regulating signal transduction pathways that control assembly of focal adhesions and actin stress fibers. This enzyme was formerly listed as EC 3.6.1.47.rap1 GTP-Binding Proteins: A genetically related subfamily of RAP GTP-BINDING PROTEINS that share homology with RAS PROTEINS. They bind to Ras effectors but do not activate them, therefore they may antagonize the effects of RAS PROTEINS. This enzyme was formerly listed as EC 3.6.1.47.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.ras Proteins: Small, monomeric GTP-binding proteins encoded by ras genes (GENES, RAS). The protooncogene-derived protein, PROTO-ONCOGENE PROTEIN P21(RAS), plays a role in normal cellular growth, differentiation and development. The oncogene-derived protein (ONCOGENE PROTEIN P21(RAS)) can play a role in aberrant cellular regulation during neoplastic cell transformation (CELL TRANSFORMATION, NEOPLASTIC). This enzyme was formerly listed as EC 3.6.1.47.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.Pertussis Toxin: One of the virulence factors produced by BORDETELLA PERTUSSIS. It is a multimeric protein composed of five subunits S1 - S5. S1 contains mono ADPribose transferase activity.rac1 GTP-Binding Protein: A rac GTP-binding protein involved in regulating actin filaments at the plasma membrane. It controls the development of filopodia and lamellipodia in cells and thereby influences cellular motility and adhesion. It is also involved in activation of NADPH OXIDASE. This enzyme was formerly listed as EC 3.6.1.47.Botulinum Toxins: Toxic proteins produced from the species CLOSTRIDIUM BOTULINUM. The toxins are synthesized as a single peptide chain which is processed into a mature protein consisting of a heavy chain and light chain joined via a disulfide bond. The botulinum toxin light chain is a zinc-dependent protease which is released from the heavy chain upon ENDOCYTOSIS into PRESYNAPTIC NERVE ENDINGS. Once inside the cell the botulinum toxin light chain cleaves specific SNARE proteins which are essential for secretion of ACETYLCHOLINE by SYNAPTIC VESICLES. This inhibition of acetylcholine release results in muscular PARALYSIS.Virulence Factors, Bordetella: A set of BACTERIAL ADHESINS and TOXINS, BIOLOGICAL produced by BORDETELLA organisms that determine the pathogenesis of BORDETELLA INFECTIONS, such as WHOOPING COUGH. They include filamentous hemagglutinin; FIMBRIAE PROTEINS; pertactin; PERTUSSIS TOXIN; ADENYLATE CYCLASE TOXIN; dermonecrotic toxin; tracheal cytotoxin; Bordetella LIPOPOLYSACCHARIDES; and tracheal colonization factor.ADP Ribose Transferases: Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.rab3 GTP-Binding Proteins: A genetically related subfamily of RAB GTP-BINDING PROTEINS involved in calcium-dependent EXOCYTOSIS. This enzyme was formerly listed as EC 3.6.1.47.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.Adenosine Diphosphate Ribose: An ester formed between the aldehydic carbon of RIBOSE and the terminal phosphate of ADENOSINE DIPHOSPHATE. It is produced by the hydrolysis of nicotinamide-adenine dinucleotide (NAD) by a variety of enzymes, some of which transfer an ADP-ribosyl group to target proteins.Thionucleotides: Nucleotides in which the base moiety is substituted with one or more sulfur atoms.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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Guanine Nucleotide Dissociation Inhibitors: Protein factors that inhibit the dissociation of GDP from GTP-BINDING PROTEINS.rho-Specific Guanine Nucleotide Dissociation Inhibitors: A subcategory of guanine nucleotide dissociation inhibitors that are specific for RHO GTP-BINDING PROTEINS.ADP-Ribosylation Factor 1: ADP-RIBOSYLATION FACTOR 1 is involved in regulating intracellular transport by modulating the interaction of coat proteins with organelle membranes in the early secretory pathway. It is a component of COAT PROTEIN COMPLEX I. This enzyme was formerly listed as EC 3.6.1.47.Cloning, 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.Kinetics: The rate dynamics in chemical or physical systems.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Cell Line: Established cell cultures that have the potential to propagate indefinitely.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.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.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.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.Poly(A)-Binding Proteins: Proteins that bind to the 3' polyadenylated region of MRNA. When complexed with RNA the proteins serve an array of functions such as stabilizing the 3' end of RNA, promoting poly(A) synthesis and stimulating mRNA translation.rap GTP-Binding Proteins: A family of MONOMERIC GTP-BINDING PROTEINS that are related to RAS PROTEINS.This enzyme was formerly listed as EC 3.6.1.47.Heterotrimeric GTP-Binding Proteins: GTP-BINDING PROTEINS that contain three non-identical subunits. They are found associated with members of the seven transmembrane domain superfamily of G-PROTEIN-COUPLED RECEPTORS. Upon activation the GTP-BINDING PROTEIN ALPHA SUBUNIT of the complex dissociates leaving a dimer of a GTP-BINDING PROTEIN BETA SUBUNIT bound to a GTP-BINDING PROTEIN GAMMA SUBUNIT.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.Recombinant Proteins: Proteins prepared by recombinant DNA technology.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.Cytoskeleton: The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.RGS Proteins: A large family of evolutionarily conserved proteins that function as negative regulators of HETEROTRIMERIC GTP-BINDING PROTEINS. RGS PROTEINS act by increasing the GTPase activity of the G alpha subunit of a heterotrimeric GTP-binding protein, causing it to revert to its inactive (GDP-bound) form.p21-Activated Kinases: A family of serine-threonine kinases that bind to and are activated by MONOMERIC GTP-BINDING PROTEINS such as RAC GTP-BINDING PROTEINS and CDC42 GTP-BINDING PROTEIN. They are intracellular signaling kinases that play a role the regulation of cytoskeletal organization.Protein Prenylation: A post-translational modification of proteins by the attachment of an isoprenoid to the C-terminal cysteine residue. The isoprenoids used, farnesyl diphosphate or geranylgeranyl diphosphate, are derived from the same biochemical pathway that produces cholesterol.GTP-Binding Protein alpha Subunits: The GTPase-containing subunits of heterotrimeric GTP-binding proteins. When dissociated from the heterotrimeric complex these subunits interact with a variety of second messenger systems. Hydrolysis of GTP by the inherent GTPase activity of the subunit causes it to revert to its inactive (heterotrimeric) form. The GTP-Binding protein alpha subunits are grouped into families according to the type of action they have on second messenger systems.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.ral GTP-Binding Proteins: A family of ubiquitously expressed MONOMERIC GTP-BINDING PROTEINS that are involved in intracellular signal transduction. This enzyme was formerly listed as EC 3.6.1.47.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.Vesicular Neurotransmitter Transport Proteins: A family of neurotransmitter transporter proteins that are INTEGRAL MEMBRANE PROTEINS of the LIPID BILAYER of SECRETORY VESICLES. They are ANTIPORTERS that exchange vesicular PROTONS for cytoplasmic NEUROTRANSMITTER and play an essential role in regulating neurotransmission.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).)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.Proto-Oncogene Proteins p21(ras): Cellular proteins encoded by the H-ras, K-ras and N-ras genes. The proteins have GTPase activity and are involved in signal transduction as monomeric GTP-binding proteins. Elevated levels of p21 c-ras have been associated with neoplasia. This enzyme was formerly listed as EC 3.6.1.47.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.GTP-Binding Protein alpha Subunits, Gi-Go: A family of heterotrimeric GTP-binding protein alpha subunits that were originally identified by their ability to inhibit ADENYLYL CYCLASES. Members of this family can couple to beta and gamma G-protein subunits that activate POTASSIUM CHANNELS. The Gi-Go part of the name is also spelled Gi/Go.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.GTP Cyclohydrolase: (GTP cyclohydrolase I) or GTP 7,8-8,9-dihydrolase (pyrophosphate-forming) (GTP cyclohydrolase II). An enzyme group that hydrolyzes the imidazole ring of GTP, releasing carbon-8 as formate. Two C-N bonds are hydrolyzed and the pentase unit is isomerized. This is the first step in the synthesis of folic acid from GTP. EC 3.5.4.16 (GTP cyclohydrolase I) and EC 3.5.4.25 (GTP cyclohydrolase II).Guanine Nucleotide-Releasing Factor 2: A 145-kDa guanine nucleotide exchange factor that is specific for rap1 and ras GTP-BINDING PROTEINS. It associates with SH3 domains of the crk family of signaling proteins.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.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.Guanine NucleotidesProtein-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.GTP-Binding Protein beta Subunits: Heterotrimeric GTP-binding protein subunits that tightly associate with GTP-BINDING PROTEIN GAMMA SUBUNITS. A dimer of beta and gamma subunits is formed when the GTP-BINDING PROTEIN ALPHA SUBUNIT dissociates from the GTP-binding protein heterotrimeric complex. The beta-gamma dimer can play an important role in signal transduction by interacting with a variety of second messengers.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).Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.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.Calcium: A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.Cytoskeletal 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.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.Transducin: A heterotrimeric GTP-binding protein that mediates the light activation signal from photolyzed rhodopsin to cyclic GMP phosphodiesterase and is pivotal in the visual excitation process. Activation of rhodopsin on the outer membrane of rod and cone cells causes GTP to bind to transducin followed by dissociation of the alpha subunit-GTP complex from the beta/gamma subunits of transducin. The alpha subunit-GTP complex activates the cyclic GMP phosphodiesterase which catalyzes the hydrolysis of cyclic GMP to 5'-GMP. This leads to closure of the sodium and calcium channels and therefore hyperpolarization of the rod cells. EC 3.6.1.-.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.ras GTPase-Activating Proteins: PROTEINS that specifically activate the GTP-phosphohydrolase activity of RAS PROTEINS.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.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 enzymesTacrolimus Binding Proteins: A family of immunophilin proteins that bind to the immunosuppressive drugs TACROLIMUS (also known as FK506) and SIROLIMUS. EC 5.2.1.-Guanylyl Imidodiphosphate: A non-hydrolyzable analog of GTP, in which the oxygen atom bridging the beta to the gamma phosphate is replaced by a nitrogen atom. It binds tightly to G-protein in the presence of Mg2+. The nucleotide is a potent stimulator of ADENYLYL CYCLASES.Cyclic AMP: An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH.GTP-Binding Protein gamma Subunits: Heterotrimeric GTP-binding protein subunits that tightly associate with GTP-BINDING PROTEIN BETA SUBUNITS. A dimer of beta and gamma subunits is formed when the GTP-BINDING PROTEIN ALPHA SUBUNIT dissociates from the GTP-binding protein heterotrimeric complex. The beta-gamma dimer can play an important role in signal transduction by interacting with a variety of second messengers.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.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.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.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.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.GTP-Binding Protein alpha Subunits, Gs: A family of heterotrimeric GTP-binding protein alpha subunits that activate ADENYLYL CYCLASES.Cell Movement: The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.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.Poly(A)-Binding Protein I: A poly(A) binding protein that has a variety of functions such as mRNA stabilization and protection of RNA from nuclease activity. Although poly(A) binding protein I is considered a major cytoplasmic RNA-binding protein it is also found in the CELL NUCLEUS and may be involved in transport of mRNP particles.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).PhosphoproteinsCell Adhesion: Adherence of cells to surfaces or to other cells.rho-Associated Kinases: A group of intracellular-signaling serine threonine kinases that bind to RHO GTP-BINDING PROTEINS. They were originally found to mediate the effects of rhoA GTP-BINDING PROTEIN on the formation of STRESS FIBERS and FOCAL ADHESIONS. Rho-associated kinases have specificity for a variety of substrates including MYOSIN-LIGHT-CHAIN PHOSPHATASE and LIM KINASES.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.Mevalonic AcidCricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.Phospholipase D: An enzyme found mostly in plant tissue. It hydrolyzes glycerophosphatidates with the formation of a phosphatidic acid and a nitrogenous base such as choline. This enzyme also catalyzes transphosphatidylation reactions. EC 3.1.4.4.Dogs: The domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065)Insulin-Like Growth Factor Binding Proteins: A family of soluble proteins that bind insulin-like growth factors and modulate their biological actions at the cellular level. (Int J Gynaecol Obstet 1992;39(1):3-9)Biological Transport: The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.Fungal Proteins: Proteins found in any species of fungus.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.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.Proto-Oncogene Proteins c-raf: A ubiquitously expressed raf kinase subclass that plays an important role in SIGNAL TRANSDUCTION. The c-raf Kinases are MAP kinase kinase kinases that have specificity for MAP KINASE KINASE 1 and MAP KINASE KINASE 2.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)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.Adenylate Cyclase: An enzyme of the lyase class that catalyzes the formation of CYCLIC AMP and pyrophosphate from ATP. EC 4.6.1.1.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)Nerve Tissue ProteinsGTP-Binding Protein alpha Subunits, Gq-G11: A family of heterotrimeric GTP-binding protein alpha subunits that activate TYPE C PHOSPHOLIPASES dependent signaling pathways. The Gq-G11 part of the name is also spelled Gq/G11.Endocytosis: Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.CHO Cells: CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.RNA-Binding Proteins: Proteins that bind to RNA molecules. Included here are RIBONUCLEOPROTEINS and other proteins whose function is to bind specifically to RNA.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.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.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.Calcium-Calmodulin-Dependent Protein Kinases: A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)Imidazolines: Compounds based on reduced IMIDAZOLES containing a single double bond.NADPH Oxidase: A flavoprotein enzyme that catalyzes the univalent reduction of OXYGEN using NADPH as an electron donor to create SUPEROXIDE ANION. The enzyme is dependent on a variety of CYTOCHROMES. Defects in the production of superoxide ions by enzymes such as NADPH oxidase result in GRANULOMATOUS DISEASE, CHRONIC.GTP-Binding Protein alpha Subunit, Gi2: A PERTUSSIS TOXIN-sensitive GTP-binding protein alpha subunit. It couples with a variety of CELL SURFACE RECEPTORS, has been implicated in INTERLEUKIN-12 production, and may play a role in INFLAMMATORY BOWEL DISEASES.Fatty Acid-Binding Proteins: Intracellular proteins that reversibly bind hydrophobic ligands including: saturated and unsaturated FATTY ACIDS; EICOSANOIDS; and RETINOIDS. They are considered a highly conserved and ubiquitously expressed family of proteins that may play a role in the metabolism of LIPIDS.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.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Enzyme Inhibitors: Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.Actin Cytoskeleton: Fibers composed of MICROFILAMENT PROTEINS, which are predominately ACTIN. They are the smallest of the cytoskeletal filaments.Aluminum Compounds: Inorganic compounds that contain aluminum as an integral part of the molecule.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.Type C Phospholipases: A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Bacterial Proteins: Proteins found in any species of bacterium.Neuropeptides: Peptides released by NEURONS as intercellular messengers. Many neuropeptides are also hormones released by non-neuronal cells.Peptide Elongation Factor Tu: A protein found in bacteria and eukaryotic mitochondria which delivers aminoacyl-tRNA's to the A site of the ribosome. The aminoacyl-tRNA is first bound to a complex of elongation factor Tu containing a molecule of bound GTP. The resulting complex is then bound to the 70S initiation complex. Simultaneously the GTP is hydrolyzed and a Tu-GDP complex is released from the 70S ribosome. The Tu-GTP complex is regenerated from the Tu-GDP complex by the Ts elongation factor and GTP.Transglutaminases: Transglutaminases catalyze cross-linking of proteins at a GLUTAMINE in one chain with LYSINE in another chain. They include keratinocyte transglutaminase (TGM1 or TGK), tissue transglutaminase (TGM2 or TGC), plasma transglutaminase involved with coagulation (FACTOR XIII and FACTOR XIIIa), hair follicle transglutaminase, and prostate transglutaminase. Although structures differ, they share an active site (YGQCW) and strict CALCIUM dependence.Protein Kinase C: An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.Guanosine Monophosphate: A guanine nucleotide containing one phosphate group esterified to the sugar moiety and found widely in nature.Cholera Toxin: An ENTEROTOXIN from VIBRIO CHOLERAE. It consists of two major protomers, the heavy (H) or A subunit and the B protomer which consists of 5 light (L) or B subunits. The catalytic A subunit is proteolytically cleaved into fragments A1 and A2. The A1 fragment is a MONO(ADP-RIBOSE) TRANSFERASE. The B protomer binds cholera toxin to intestinal epithelial cells, and facilitates the uptake of the A1 fragment. The A1 catalyzed transfer of ADP-RIBOSE to the alpha subunits of heterotrimeric G PROTEINS activates the production of CYCLIC AMP. Increased levels of cyclic AMP are thought to modulate release of fluid and electrolytes from intestinal crypt cells.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.Molecular Weight: The sum of the weight of all the atoms in a molecule.Receptors, G-Protein-Coupled: The largest family of cell surface receptors involved in SIGNAL TRANSDUCTION. They share a common structure and signal through HETEROTRIMERIC G-PROTEINS.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.Cell Division: The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.Poly(A)-Binding Protein II: A poly(A) binding protein that is involved in promoting the extension of the poly A tails of MRNA. The protein requires a minimum of ten ADENOSINE nucleotides in order for binding to mRNA. Once bound it works in conjunction with CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR to stimulate the rate of poly A synthesis by POLY A POLYMERASE. Once poly-A tails reach around 250 nucleotides in length poly(A) binding protein II no longer stimulates POLYADENYLATION. Mutations within a GCG repeat region in the gene for poly(A) binding protein II have been shown to cause the disease MUSCULAR DYSTROPHY, OCULOPHARYNGEAL.Mitogen-Activated Protein Kinase Kinases: A serine-threonine protein kinase family whose members are components in protein kinase cascades activated by diverse stimuli. These MAPK kinases phosphorylate MITOGEN-ACTIVATED PROTEIN KINASES and are themselves phosphorylated by MAP KINASE KINASE KINASES. JNK kinases (also known as SAPK kinases) are a subfamily.Dynamins: A family of high molecular weight GTP phosphohydrolases that play a direct role in vesicle transport. They associate with microtubule bundles (MICROTUBULES) and are believed to produce mechanical force via a process linked to GTP hydrolysis. This enzyme was formerly listed as EC 3.6.1.50.Binding, Competitive: The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements.GTP-Binding Protein Regulators: Proteins that regulate the signaling activity of GTP-BINDING PROTEINS. They are divided into three categories depending upon whether they stimulate GTPase activity (GTPASE-ACTIVATING PROTEINS), inhibit release of GDP; (GUANINE NUCLEOTIDE DISSOCIATION INHIBITORS); or exchange GTP for GDP; (GUANINE NUCLEOTIDE EXCHANGE FACTORS).Peptide Elongation Factor G: Peptide Elongation Factor G catalyzes the translocation of peptidyl-tRNA from the A to the P site of bacterial ribosomes by a process linked to hydrolysis of GTP to GDP.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.GTP Phosphohydrolase-Linked Elongation Factors: Factors that utilize energy from the hydrolysis of GTP to GDP for peptide chain elongation. EC 3.6.1.-.Receptors, Muscarinic: One of the two major classes of cholinergic receptors. Muscarinic receptors were originally defined by their preference for MUSCARINE over NICOTINE. There are several subtypes (usually M1, M2, M3....) that are characterized by their cellular actions, pharmacology, and molecular biology.Protein Structure, Secondary: The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.DNA: A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).Adenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.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.GTP-Binding Protein alpha Subunits, G12-G13: A ubiquitously expressed family of heterotrimeric GTP-binding protein alpha subunits that signal through interactions with a variety of second messengers as GTPASE-ACTIVATING PROTEINS; GUANINE NUCLEOTIDE EXCHANGE FACTORS; and HEAT SHOCK PROTEINS. The G12-G13 part of the name is also spelled G12/G13.Protein-Tyrosine Kinases: Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.Oncogene Protein p21(ras): Transforming protein encoded by ras oncogenes. Point mutations in the cellular ras gene (c-ras) can also result in a mutant p21 protein that can transform mammalian cells. Oncogene protein p21(ras) has been directly implicated in human neoplasms, perhaps accounting for as much as 15-20% of all human tumors. This enzyme was formerly listed as EC 3.6.1.47.Insulin-Like Growth Factor Binding Protein 3: One of the six homologous soluble proteins that bind insulin-like growth factors (SOMATOMEDINS) and modulate their mitogenic and metabolic actions at the cellular level.rab5 GTP-Binding Proteins: A genetically related subfamily of RAB GTP-BINDING PROTEINS involved in transport from the cell membrane to early endosomes. This enzyme was formerly listed as EC 3.6.1.47.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.Phospholipase C beta: A phosphoinositide phospholipase C subtype that is primarily regulated by its association with HETEROTRIMERIC G-PROTEINS. It is structurally related to PHOSPHOLIPASE C DELTA with the addition of C-terminal extension of 400 residues.Periplasmic Binding Proteins: Periplasmic proteins that scavenge or sense diverse nutrients. In the bacterial environment they usually couple to transporters or chemotaxis receptors on the inner bacterial membrane.Cell Surface Extensions: Specialized structures of the cell that extend the cell membrane and project out from the cell surface.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Tubulin: A microtubule subunit protein found in large quantities in mammalian brain. It has also been isolated from SPERM FLAGELLUM; CILIA; and other sources. Structurally, the protein is a dimer with a molecular weight of approximately 120,000 and a sedimentation coefficient of 5.8S. It binds to COLCHICINE; VINCRISTINE; and VINBLASTINE.Adenylosuccinate Synthase: A carbon-nitrogen ligase. During purine ribonucleotide biosynthesis, this enzyme catalyzes the synthesis of adenylosuccinate from GTP; IMP; and aspartate with the formation of orthophosphate and GDP. EC 6.3.4.4.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Point Mutation: A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.Cell Adhesion Molecules: Surface ligands, usually glycoproteins, that mediate cell-to-cell adhesion. Their functions include the assembly and interconnection of various vertebrate systems, as well as maintenance of tissue integration, wound healing, morphogenic movements, cellular migrations, and metastasis.Cytosol: Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.Protein Biosynthesis: The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.Peptide Elongation Factors: Protein factors uniquely required during the elongation phase of protein synthesis.Pseudopodia: A dynamic actin-rich extension of the surface of an animal cell used for locomotion or prehension of food.Affinity Labels: Analogs of those substrates or compounds which bind naturally at the active sites of proteins, enzymes, antibodies, steroids, or physiological receptors. These analogs form a stable covalent bond at the binding site, thereby acting as inhibitors of the proteins or steroids.Tacrolimus Binding Protein 1A: A 12-KDa tacrolimus binding protein that is found associated with and may modulate the function of calcium release channels. It is a peptidyl-prolyl cis/trans isomerase which is inhibited by both tacrolimus (commonly called FK506) and SIROLIMUS.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.Phenotype: The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.Ribosomes: Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.Latent TGF-beta Binding Proteins: A family of secreted multidomain proteins that were originally identified by their association with the latent form of TRANSFORMING GROWTH FACTORS. They interact with a variety of EXTRACELLULAR MATRIX PROTEINS and may play a role in the regulation of TGB-beta bioavailability.rab2 GTP-Binding Protein: A protein involved in transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS. This enzyme was formerly listed as EC 3.6.1.47.Amino Acid Substitution: The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.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.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.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.Dimerization: The process by which two molecules of the same chemical composition form a condensation product or polymer.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.Insulin-Like Growth Factor Binding Protein 2: One of the six homologous soluble proteins that bind insulin-like growth factors (SOMATOMEDINS) and modulate their mitogenic and metabolic actions at the cellular level.Vesicular stomatitis Indiana virus: The type species of VESICULOVIRUS causing a disease symptomatically similar to FOOT-AND-MOUTH DISEASE in cattle, horses, and pigs. It may be transmitted to other species including humans, where it causes influenza-like symptoms.Septins: A family of GTP-binding proteins that were initially identified in YEASTS where they were shown to initiate the process of septation and bud formation. Septins form into hetero-oligomeric complexes that are comprised of several distinct septin subunits. These complexes can act as cytoskeletal elements that play important roles in CYTOKINESIS, cytoskeletal reorganization, BIOLOGICAL TRANSPORT, and membrane dynamics.Fluorides: Inorganic salts of hydrofluoric acid, HF, in which the fluorine atom is in the -1 oxidation state. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Sodium and stannous salts are commonly used in dentifrices.TATA-Box Binding Protein: A general transcription factor that plays a major role in the activation of eukaryotic genes transcribed by RNA POLYMERASES. It binds specifically to the TATA BOX promoter element, which lies close to the position of transcription initiation in RNA transcribed by RNA POLYMERASE II. Although considered a principal component of TRANSCRIPTION FACTOR TFIID it also takes part in general transcription factor complexes involved in RNA POLYMERASE I and RNA POLYMERASE III transcription.Conserved Sequence: A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.
... a small G protein of the Rac subfamily) is perhaps the best known inducer of Dock180 GEF activity. Active (GTP-bound) RhoG ... Subsequently it was reported that Dock180 was able to activate the small GTP-binding protein (G protein) Rac1 and this was ... which contribute to cellular signalling events by activating small G proteins. In their resting state G proteins are bound to ... Katoh H, Negishi M (July 2003). "RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo". Nature. 424 ...
... (Ras homology Growth-related) (or ARGH) is a small (~21 kDa) monomeric GTP-binding protein (G protein), and is an ... It is a member of the Rac subfamily of the Rho family of small G proteins and is encoded by the gene RHOG. RhoG was first ... Other proteins known to bind RhoG in its GTP-bound state include the microtubule-associated protein kinectin, Phospholipase D1 ... Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG". The Journal of ...
Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG". J. Biol. Chem. ... "A novel partner for the GTP-bound forms of rho and rac". FEBS Lett. NETHERLANDS. 377 (2): 243-8. doi:10.1016/0014-5793(95)01351 ... Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG". J. Biol. Chem. ... RHOB is a member of the Rho GTP-binding protein family. RHOB has been shown to interact with CIT, ARHGEF3, ARHGDIG and RHPN2. ...
"Mapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1". Structure. 8 (1): 47-55. doi:10.1016/ ... Rac1 is a small (~21 kDa) signaling G protein (more specifically a GTPase), and is a member of the Rac subfamily of the family ... Katoh H, Negishi M (Jul 2003). "RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo". Nature. 424 ( ... "Interaction of Nck-associated protein 1 with activated GTP-binding protein Rac". The Biochemical Journal. 322 (3): 873-8. doi: ...
Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG". J. Biol. Chem. ... del Pozo MA, Alderson NB, Kiosses WB, Chiang HH, Anderson RG, Schwartz MA (2004). "Integrins regulate Rac targeting by ... Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG". J. Biol. Chem. ... Li X, Bu X, Lu B, Avraham H, Flavell RA, Lim B (2002). "The Hematopoiesis-Specific GTP-Binding Protein RhoH Is GTPase Deficient ...
ELMO also binds the activated form of the small G protein RhoG and this has been shown to promote DOCK-dependent signalling by ... which function as activators of small G proteins. Dock4 activates the small G proteins Rac and Rap1. Dock4 was discovered as a ... and their activation requires the dissociation of GDP and binding of guanosine triphosphate (GTP). GEFs activate G proteins by ... which contribute to cellular signalling events by activating small G proteins. In their resting state G proteins are bound to ...
Bustelo XR, Sauzeau V, Berenjeno IM (2007). "GTP-binding proteins of the Rho/Rac family: regulation, effectors and functions in ... catalyzed GTP binding to Cdc42, suggesting a mechanism for regulation of polarity by this small GTPase in migrating cells. ... These 22 mammalian members are subdivided in the Rac subfamily (Rac1, Rac2, Rac3, and RhoG), Cdc42 subfamily (Cdc42, TC10, TCL ... This protein cannot be inactivated normally, through GTP hydrolysis, and is thus "stuck on". When a Rho protein activated in ...
Cachero TG, Morielli AD, Peralta EG (June 1998). "The small GTP-binding protein RhoA regulates a delayed rectifier potassium ... "A novel partner for the GTP-bound forms of rho and rac". FEBS Lett. 377 (2): 243-8. doi:10.1016/0014-5793(95)01351-2. PMID ... Vignal E, Blangy A, Martin M, Gauthier-Rouvière C, Fort P (December 2001). "Kinectin is a key effector of RhoG microtubule- ... RhoA contains both inactive GDP-bound and active GTP-bound conformational states; these states alternate between the active and ...
... which function as activators of small G proteins. Dock2 specifically activates isoforms of the small G protein Rac. Dock2 was ... Katoh H, Negishi M (July 2003). "RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo". Nature. 424 ... and their activation requires the dissociation of GDP and binding of guanosine triphosphate (GTP). GEFs activate G proteins by ... which contribute to cellular signalling events by activating small G proteins. In their resting state G proteins are bound to ...
Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG". J. Biol. Chem. ... "The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI". Nat. Struct. Biol. 7 (2): 122-6 ... Li X, Bu X, Lu B, Avraham H, Flavell RA, Lim B (2002). "The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient ... Scherle P, Behrens T, Staudt LM (September 1993). "Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is ...
They are small (20-kDa to 25-kDa) proteins that bind to guanosine triphosphate (GTP). This family of proteins is homologous to ... Main article: Small GTPases. Small GTPases also bind GTP and GDP and are involved in signal transduction. These proteins are ... "Regulator of G protein signalling"). Receptors stimulate GTP binding (turning the G protein on). RGS proteins stimulate GTP ... Wikimedia Commons has media related to G proteins.. *GTP-Binding Proteins at the US National Library of Medicine Medical ...
These proteins serve as targets for the small GTP binding proteins Cdc42 and Rac and have been implicated in a wide range of ... Katoh H, Negishi M (July 2003). "RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo". Nature. 424 ... ARG-binding protein 2γ, hepatitis B virus X protein, STE20-related kinase adaptor protein α, RhoI, Klotho, N-acetylglucosaminyl ... Seoh ML, Ng CH, Yong J, Lim L, Leung T (March 2003). "ArhGAP15, a novel human RacGAP protein with GTPase binding property". ...
nucleotide binding. • LRR domain binding. • GDP binding. • protein complex binding. • GTP binding. • GMP binding. • protein ... positive regulation of Rac protein signal transduction. • positive regulation of gene expression. • positive regulation of cell ... "Identification of a small molecule with synthetic lethality for K-ras and protein kinase C iota". Cancer Research. 68 (18): ... identical protein binding. Cellular component. • cytoplasm. • cytosol. • membrane. • focal adhesion. • extrinsic component of ...
Its sequence domains include a P-loop containing nucleoside triphosphate hydrolase and a small GTP-binding protein domain.[6] ... Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein ... protein binding. • thioesterase binding. • protein kinase binding. • nucleotide binding. • GTP binding. • identical protein ... ubiquitin protein ligase activity. • apolipoprotein A-I receptor binding. • GTP-dependent protein binding. • GTPase activity. • ...
... s (GPCRs) which are also known as seven-(pass)-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptor, and G protein-linked receptors (GPLR), constitute a large protein family of receptors that detect molecules outside the cell and activate internal signal transduction pathways and, ultimately, cellular responses. Coupling with G proteins, they are called seven-transmembrane receptors because they pass through the cell membrane seven times. G protein-coupled receptors are found only in eukaryotes, including yeast, choanoflagellates, and animals. The ligands that bind and activate these receptors include light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters, and vary in size from small molecules to peptides to large proteins. G protein-coupled receptors are involved in many diseases, and are also the target of approximately 34% of all modern medicinal drugs. ...
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3 is a protein that in humans is encoded by the GNB3 gene. Heterotrimeric guanine nucleotide-binding proteins ( G proteins), which integrate signals between receptors and effector proteins, are composed of an alpha, a beta, and a gamma subunit. These subunits are encoded by families of related genes. This gene encodes a beta subunit. Beta subunits are important regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. A single-nucleotide polymorphism (C825T) in this gene is associated with essential hypertension and obesity. This polymorphism is also associated with the occurrence of the splice variant GNB3-s, which appears to have increased activity. GNB3-s is an example of alternative splicing caused by a nucleotide change outside of the splice donor and acceptor sites. ...
Guanine nucleotide-binding protein G(olf) subunit alpha is a protein that in humans is encoded by the GNAL gene. GRCh38: Ensembl release 89: ENSG00000141404 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000024524 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Wilkie TM, Gilbert DJ, Olsen AS, Chen XN, Amatruda TT, Korenberg JR, Trask BJ, de Jong P, Reed RR, Simon MI, et al. (Jun 1993). "Evolution of the mammalian G protein alpha subunit multigene family". Nat Genet. 1 (2): 85-91. doi:10.1038/ng0592-85. PMID 1302014. "Entrez Gene: GNAL guanine nucleotide binding protein (G protein), alpha activating activity polypeptide, olfactory type". Zigman JM, Westermark GT, LaMendola J, et al. (1994). "Human G(olf) alpha: complementary deoxyribonucleic acid structure and expression in pancreatic islets and other tissues outside the olfactory neuroepithelium and central nervous system". Endocrinology. 133 (6): 2508-14. doi:10.1210/en.133.6.2508. PMID ...
Regulator of G-protein signaling 13 is a protein that in humans is encoded by the RGS13 gene.[5][6] RGS 13 is a member of R4 subfamily of RGS (Regulators of G Protein Signaling) proteins which have only short peptide sequences flanking the RGS domain. RGS 13 suppresses the immunoglobulin E- mediated allergic responses.[7] The protein encoded by this gene is a member of the regulator of G protein signaling (RGS) family. RGS family members share similarity with S. cerevisiae SST2 and C. elegans egl-10 proteins, which contain a characteristic conserved RGS domain. RGS proteins accelerate GTPase activity of G protein alpha-subunits, thereby driving G protein into their inactive GDP-bound form, thus negatively regulating G protein signaling. RGS proteins have been implicated in the fine tuning of a variety of cellular events in response to G ...
Heterotrimeric guanine nucleotide-binding proteins (G proteins), which integrate signals between receptors and effector proteins, are composed of an alpha, a beta, and a gamma subunit. These subunits are encoded by families of related genes. This gene encodes a beta subunit. Beta subunits are important regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. This gene uses alternative polyadenylation signals.[5][6] ...
G proteins, also known as guanine nucleotide-binding proteins, are a family of proteins that act as molecular switches inside cells, and are involved in transmitting signals from a variety of stimuli outside a cell to its interior. Their activity is regulated by factors that control their ability to bind to and hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP). When they are bound to GTP, they are 'on', and, when they are bound to GDP, they are 'off'. G proteins belong to the larger group of enzymes called GTPases.. There are two classes of G proteins. The first function as monomeric small GTPases, while the second function as heterotrimeric G protein complexes. The latter class of complexes is made up of alpha (α), beta ...
The general function of Gs is to activate intracellular signaling pathways in response to activation of cell surface G protein-coupled receptors (GPCRs). GPCRs function as part of a three-component system of receptor-transducer-effector.[6][7] The transducer in this system is a heterotrimeric G protein, composed of three subunits: a Gα protein such as Gsα, and a complex of two tightly linked proteins called Gβ and Gγ in a Gβγ complex.[6][7] When not stimulated by a receptor, Gα is bound to GDP and to Gβγ to form the inactive G protein trimer.[6][7] When the receptor binds an activating ligand outside the cell (such as a hormone or neurotransmitter), the activated receptor acts as a guanine nucleotide exchange factor to promote GDP release from and GTP binding to Gα, which drives dissociation of GTP-bound Gα from Gβγ.[6][7] In particular, GTP-bound, activated Gsα binds to adenylyl cyclase to ...
The Gs alpha subunit (Gαs, Gsα, or Gs protein) is a heterotrimeric G protein subunit that activates the cAMP-dependent pathway by activating adenylyl cyclase. It is one of the three main families of G proteins: Gαi/Gαo, Gαq, and Gαs.[1] A mnemonic for remembering this subunit is to look at the first letter (Gαs = Adenylate Cyclase stimulator). ...
G protein-coupled receptors (GPCRs) such as DP2 are integral membrane proteins that, when bound by their cognate ligands (or, in some cases, even when not ligand-bound and thereby acting continuously in a constitutive manner {see Receptor (biochemistry)#Constitutive activity}), mobilize one or more types of Heterotrimeric G proteins. DP2 is classified as a "contractile" prostanoid receptor in that it can cause the contraction of smooth muscle. As evidenced by its initial discovery as a receptor for PGD2 in T-helper type 2 cells, activated DP2 triggers Gi alpha subunit-linked heterotrimeric G proteins to dissociate into their component a) Gi alpha subunits (also termed Giα subunits) inhibit adenylyl cyclase b) G beta-gamma complex of subunits (Gβγ) have many potential functions, including simulation of phospholipase C to cleave phosphatidylinositol triphosphate into inositol ...
The G beta-gamma complex (Gβγ) is a tightly bound dimeric protein complex, composed of one Gβ and one Gγ subunit, and is a component of heterotrimeric G proteins. Heterotrimeric G proteins, also called guanosine nucleotide-binding proteins, consist of three subunits, called alpha, beta, and gamma subunits, or Gα, Gβ, and Gγ. When a G protein-coupled receptor (GPCR) is activated, Gα dissociates from Gβγ, allowing both subunits to perform their respective downstream signaling effects. One of the major functions of Gβγ is the inhibition of the Gα subunit. The individual subunits of the G protein complex were first identified in 1980 when the regulatory component of adenylate cyclase was successfully purified, yielding three polypeptides of different molecular weights. Initially, it was thought that Gα, the largest subunit, was the major effector regulatory subunit, and that Gβγ was largely ...
Ras-related protein Rap-1b, also known as GTP-binding protein smg p21B, is a protein that in humans is encoded by the RAP1B gene. GRCh38: Ensembl release 89: ENSG00000127314 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000052681 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". "Entrez Gene: RAP1B". Pizon V, Lerosey I, Chardin P, Tavitian A (August 1988). "Nucleotide sequence of a human cDNA encoding a ras-related protein (rap1B)". Nucleic Acids Res. 16 (15): 7719. doi:10.1093/nar/16.15.7719. PMC 338441 . PMID 3137530. Matsui Y, Kikuchi A, Kawata M, Kondo J, Teranishi Y, Takai Y (January 1990). "Molecular cloning of smg p21B and identification of smg p21 purified from bovine brain and human platelets as smg p21B". Biochem. Biophys. Res. Commun. 166 (2): 1010-6. doi:10.1016/0006-291X(90)90911-6. PMID 2105724. Rousseau-Merck MF, Pizon V, Tavitian A, Berger R (1990). "Chromosome mapping of the human RAS-related RAP1A, RAP1B, and RAP2 genes to ...
COPⅠ囊泡:最初研究者利用三磷酸鳥苷(GTP)衍生物GTPγS(一種富含高爾基體膜的細胞質與抗水解的GTP衍生物)共培養時,發現高爾基體池之間存在一種囊泡轉運結構[9](後來在真核細胞中也證實此結構的存在[10])。除了脂質成分外,參與此囊泡形成的成份還有7種外被體蛋白(即外被體α、β、β′、γ、δ、ε、ζ)。這些外被體蛋白相互作用形成的復合物就是COPⅠ囊泡[11][12]。亞單位α、β′、ε在結構上與網格蛋白及COPⅡ囊泡的外層組分具有較高的一致性,形成復合物的內層組分稱為B亞復合物(主要負責與靶蛋白結合),而亞單位β、γ、δ、ζ 與網格蛋白及COPⅡ囊泡的內層組分相似,形成復合物的內層組分稱為F亞復合物,該亞復合物主要負責與靶蛋白結合,並且直接與COPⅠ囊泡形成的招募者ADP核糖基化因子(英语:ADP ribosylation factor)(ADP ribosylation ...
Zingoni A, Rocchi M, Storlazzi CT, Bernardini G, Santoni A, Napolitano M (1997). „Isolation and chromosomal localization of GPR31, a human gene encoding a putative G protein-coupled receptor". Genomics. 42 (3): 519-23. PMID 9205127. doi:10.1006/geno.1997.4754 ...
RhoG (Ras homology Growth-related) (or ARGH) is a small (~21 kDa) monomeric GTP-binding protein (G protein), and is an ... It is a member of the Rac subfamily of the Rho family of small G proteins and is encoded by the gene RHOG. RhoG was first ... Other proteins known to bind RhoG in its GTP-bound state include the microtubule-associated protein kinectin, Phospholipase D1 ... Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG". The Journal of ...
... a small G protein of the Rac subfamily) is perhaps the best known inducer of Dock180 GEF activity. Active (GTP-bound) RhoG ... Subsequently it was reported that Dock180 was able to activate the small GTP-binding protein (G protein) Rac1 and this was ... which contribute to cellular signalling events by activating small G proteins. In their resting state G proteins are bound to ... Katoh H, Negishi M (July 2003). "RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo". Nature. 424 ...
Rho family proteins: Central regulators of protrusion. Rho family small guanosine triphosphate (GTP)-binding proteins (GTPases ... RhoG does not interact directly with WASPs but appears to act upstream of Rac by binding to and activating a Rac-GEF complex ( ... Rac stimulates lamellipodial extension by activating WAVE proteins (10). Cdc42 binds to WASP proteins, and in vitro this ... They are conformationally regulated by the binding of GTP and GDP: When bound to GTP, they are active and interact with their ...
... small GTP binding protein Rac1), Rac family small GTPase 1, MRD48. External IDs. OMIM: 602048 MGI: 97845 HomoloGene: 69035 ... Katoh H, Negishi M (Jul 2003). "RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo". Nature. 424 ( ... enzyme binding. • protein binding. • thioesterase binding. • protein kinase binding. • nucleotide binding. • GTP binding. • Rab ... histone deacetylase binding. • Rho GDP-dissociation inhibitor binding. • GTP-dependent protein binding. • GTPase activity. • ...
Purchase Small GTPases and Their Regulators, Part B: Rho Family, Volume 256 - 1st Edition. Print Book & E-Book. ISBN ... E. Porfiri and J.F. Hancock, Stimulation of Nucleotide Exchange on Ras- and Rho-Related Proteins by Small GTP-Binding Protein ... D. Diekmann and A. Hall, In Vitro Binding Assay for Interactions of Rho and Rac with GTPase-Activating Proteins and Effectors. ... Cell Expression and in Vitro Analysis: P. Fort and S. Vincent, Serum Induction of RhoG Expression. H. Paterson, P. Adamson, and ...
GTP Phosphohydrolases/*genetics; Introns; rho GTP-Binding Proteins ... Although the biochemical properties of these GTPases have been extensively studied, very little is known about their gene ... RhoG, a member related to Rac and Cdc42Hs, is activated at the transcriptional level in the mid-G1 phase of stimulated ... Structure of the human ARHG locus encoding the Rho/Rac-like RhoG GTPase. Le Gallic, L.; Fort, P. ...
The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy ... Rac proteins), Cdc42, TC10, TCL, Wrch1, Chp/Wrch2, RhoD and RhoG, to name some. The family also includes RhoH and Rnd1-3, which ... GTP ARHGEF11 ARHGAP11A RHOG GDI1 NET1 ARHGDIB ARHGAP40 RHOJ ARHGAP28 ARHGEF5 RhoGTPase:GTP:Effectors complex. RHOG RHOT1 RHOT1 ... RHOG Protein. P84095 (Uniprot-TrEMBL) RHOH Protein. Q15669 (Uniprot-TrEMBL) RHOJ Protein. Q9H4E5 (Uniprot-TrEMBL) RHOQ Protein ...
The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy ... Rac proteins), Cdc42, TC10, TCL, Wrch1, Chp/Wrch2, RhoD and RhoG, to name some. The family also includes RhoH and Rnd1-3, which ... GTP RhoGTPase. GDP Rac Rho GTPases Rac Rho GTPases Rac RhoGTPase. GDP Rac RhoBTB RHOQ RHOD RHOQ RHOBTB1 RhoGTPase. GDP. CDC42 ... RHOG RHOF RHOB GDI proteins. RHOC RHOV RHOF RHOT2 GDI1 GDP. GAP proteins. RHOT2 GEF. RHOH RHOBTB2 RHOBTB1 RHOBTB2 RHOB RAC2 GTP ...
5879 RAC1; Rac family small GTPase 1 5880 RAC2; Rac family small GTPase 2 5881 RAC3; Rac family small GTPase 3 391 RHOG; ras ... ADP-ribosylation factor related protein 1 K07953 SAR1; GTP-binding protein SAR1 [EC:3.6.5.-] K07953 SAR1; GTP-binding protein ... GTP binding protein overexpressed in skeletal muscle K07847 REM1; Rad and Gem related GTP binding protein 1 K07848 REM2; Rad ... 04031 GTP-binding proteins [BR:hsa04031] 2770 GNAI1; G protein subunit alpha i1 2773 GNAI3; G protein subunit alpha i3 2771 ...
"Interaction of Nck-associated protein 1 with activated GTP-binding protein Rac". The Biochemical Journal. 322 (3): 873-8. doi: ... Rac1 is a small (~21 kDa) signaling G protein (more specifically a GTPase), and is a member of the Rac subfamily of the family ... Katoh H, Negishi M (Jul 2003). "RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo". Nature. 424 ( ... "Mapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1". Structure. 8 (1): 47-55. doi:10.1016/ ...
Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG". J. Biol. Chem. ... "A novel partner for the GTP-bound forms of rho and rac". FEBS Lett. 377 (2): 243-8. doi:10.1016/0014-5793(95)01351-2. ISSN 0014 ... Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG". J. Biol. Chem. ... RHOB is a member of the Rho GTP-binding protein family.[3] ... 3.6.5.3: Protein-synthesizing GTPase. *Prokaryotic *IF-2. *EF- ...
The small GTPbinding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy ... Katoh H, Yasui H, Yamaguchi Y, Aoki J, Fujita H, Mori K, Negishi M (2000) Small GTPase RhoG is a key regulator for neurite ... dependent lymphocyte aggregation by ADP ribosylation of the small molecular weight GTP binding protein, rho. J Cell Biol 120: ... the bound GTP‐RhoA or GTP‐Rac1 was determined by IB with anti‐RhoA or anti‐Rac1 antibody for endogenous protein, or anti‐HA ...
... cells treated with siRNA to all Rac proteins (Kunda et al., 2003), suggesting that the role of Rac proteins in regulating ... They are molecular switches that cycle between a GTP-bound active form and a GDP-bound inactive form. Mammals have three highly ... TC10 and RhoG (Etienne-Manneville and Hall, 2002). Rac isoform-specific functions have been investigated in knockout mice and ... Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK. EMBO J. 19, 2008-2014. ...
... small molecule inhibitors that directly bind GTPases at hydrophobic binding pockets on the proteins surface which in turn then ... and Rac. Trios C-terminal domain (TrioC) activates RhoA while the N-terminal domain (TrioN) activates RhoG and Rac8. Using ... The catalytic site binds GDP-Ras and stimulates exchange of GDP for GTP7,11,12. A recent virtual screen for small molecule ... RhoA protein: His tagged: human wild type (Cat. # RH01). p50RhoGAP GST Protein, GAP domain: GAP for Cdc42, Rac, and Rho, ,90% ...
Ridley AJ and Hall A (1992) The small GTPbinding protein rho regulates the assembly of focal adhesions and actin stress fibers ... Bustelo XR, Sauzeau V and Berenjeno IM (2007) GTPbinding proteins of the Rho/Rac family: regulation, effectors and functions ... Katoh H and Negishi M (2003) RhoG activates Rac1 by direct interaction with the DOCK 180‐binding protein Elmo. Nature 424: 461- ... GTP. ‐bound and an inactive GDP. ‐bound form. Activation is catalysed by GEFs. , whereas inactivation by hydrolysis of GTP. is ...
Ridley AJ, Paterson HF, Johnston CL, Diekmann D, Hall A: The small GTP-binding protein rac regulates growth factor-induced ... A group of small RhoGTPases, including RhoE, RhoG, RhoA, Rac1, and Cdc42, were found to be associated with aPBMC-CM-mediated ... Rhoketin Rho binding domain-agarose beads and PAK1-P21-binding domain-agarose beads were used to pull down GTP-Rho and GTP-Rac/ ... Ridley AJ, Hall A: The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in ...
Rac3 is a 21 kDa small GTPase, a member of the Ras super-family and Rho sub-family of GTPases, that upon activation by a ... RAC3 (ras-related C3 botulinum toxin substrate 3 (rho family, small GTP binding protein Rac3)). Atlas Genet. Cytogenet. Oncol. ... Along with the Rho isoforms and Cdc42, it is a member of the Rho sub-family of Ras super-family GTPases and is one of 3 Rac ... identity with RhoG. At the amino acid level, Rac3 and Rac1 are 92% identical and Rac3 and Rac2 are 89% identical. Like all Ras ...
Small GTP-binding protein Rho stimulates the actomyosin system, leading to invasion of tumor cells. J. Biol. Chem.273:5146-5154 ... The small GTPases Cdc42Hs, Rac1 and RhoG delineate Raf-independent pathways that cooperate to transform NIH3T3 cells. Curr. ... Specific contributions of the small GTPases Rho, Rac, and Cdc42 to Dbl transformation. J. Biol. Chem.274:23633-23641. ... The amounts of each Rho protein in the respective cell lysates and in the GTP-bound form were normalized to that of Rac1, RhoA ...
1992) The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling. Cell 70:401-410, pmid:1643658.. ... RhoG, RhoD, and TTF. Rnd3 is identical to the recently described RhoE (Foster et al., 1996), except that in Rnd3 we have found ... 1995) The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell 81:1137-1146 ... 1992) The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth ...
Ausgesuchte Qualitäts-Hersteller für RHOG Antikörper. Hier bestellen. ... Monoklonale und polyklonale RHOG Antikörper für viele Methoden. ... aplysia ras-related homolog G (RhoG) , ras homolog G (RhoG) , rho-related GTP-binding protein RhoG , sid 10750 , ras homolog ... several Rho family small GTPases activate PI3K by an indirect cooperative positive feedback that required a combination of Rac ...
... organism-specific biosystemGTP-bound active forms of RHO GTPases RHOA, RHOG, RAC1 and CDC42 bind kinectin (KTN1), a protein ... The protein encoded by this gene is a GTPase which belongs to the RAS superfamily of small GTP-binding proteins. Members of ... ras-like protein TC25. ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1). ... Rac1_like; Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like consists of Rac1, Rac2 ...
Cherfils, J. and Chardin, P. (1999). GEFs: structural basis for their activation of small GTP-binding proteins. Trends Biochem ... The RhoG connection. Dock180 can also mediate Rac activation downstream of the small GTPase RhoG (see above). This pathway may ... Rho proteins are active when bound to GTP and inactive when bound to GDP. Conversion of the GDP-bound proteins to the active ... These CZH proteins include: CDM (Ced-5, Dock180 and Myoblast city) proteins, which activate Rac; and zizimin proteins, which ...
However, RhoG does not bind to known Rac1 and Cdc42 effectors, including proteins containing a Cdc42/Rac interacting binding ( ... Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases). RhoG is a GTPase with high sequence ... Instead, RhoG interacts directly with Elmo, an upstream regulator of Rac1, in a GTP-dependent manner and forms a ternary ... Range on the Protein: Protein ID Protein Position. NP_001265595. NP_001655. NP_067075. P51159. NP_065120. Q6IQ22. Q9UNT1. ...
Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18:578-585. doi:10.1093/emboj/ ... The small GTPase RhoG is a key upstream regulator of Rac in migrating cells (Katoh and Negishi, 2003; Hiramoto et al., 2006; ... Relative Myc-RhoG activity was determined by the amount of GTP-bound Myc-RhoG bound to GST-ELMO normalized to the amount of Myc ... Relative Myc-RhoG activity was determined by the amount of GTP-bound Myc-RhoG bound to GST-ELMO normalized to the amount of Myc ...
... on Serine 387 shifts its GAP activity from Rac to Rho, resulting in increased GTP loading (activation) of Rac1 and reduced GTP ... The small GTPase Rac1 is a novel binding partner of Bcl-2 and stabilizes its antiapoptotic activity. Blood 2011;117:6214-26. ... A GTPase-activating protein binds STAT3 and is required for IL-6-induced STAT3 activation and for differentiation of a leukemic ... Rac (1,2,3 isoforms and RhoG), and Cdc42 (Cdc42, Tc10, TCL, Chp/Wrch-2, and Wrch-1; ref. 24), which function as molecular ...
  • Dock180, the archetypal member of this family, is seen as an atypical GEF in that efficient GEF activity requires the presence of the DOCK-binding protein ELMO (engulfment and cell motility) which binds RhoG at its N-terminus. (wikipedia.org)
  • The proposed model for RhoG-dependent Rac activation involves recruitment of the ELMO/Dock180 complex to activated RhoG at the plasma membrane and this relocalisation, together with an ELMO-dependent conformational change in Dock180, is sufficient to promote GTP-loading of Rac. (wikipedia.org)
  • Dock180 was identified, using a far-western blotting approach, as a binding partner of the adaptor protein Crk that was able to induce morphological changes in 3T3 fibroblasts. (wikipedia.org)
  • Subsequently it was reported that Dock180 was able to activate the small GTP-binding protein (G protein) Rac1 and this was later shown to happen via its ability to act as a GEF. (wikipedia.org)
  • Dock180-related proteins also possess a DHR1 domain which has been shown, in vitro, to bind phospholipids and which may be involved in their interaction with cellular membranes. (wikipedia.org)
  • Other structural features of Dock180 include an N-terminal SH3 domain involved in binding to ELMO proteins (see below) and a C-terminal proline-rich region which, in Myoblast city (the Drosophila melanogaster ortholog of Dock180), was shown to bind DCrk (the Drosophila ortholog of Crk). (wikipedia.org)
  • Effective GEF activity requires an interaction between Dock180 and its binding partner ELMO. (wikipedia.org)
  • ELMO1 is the most comprehensively described isoform of this small family of non-catalytically active proteins which function to recruit Dock180 to the plasma membrane and induce conformational changes which increase GEF efficiency. (wikipedia.org)
  • (wikipedia.org)
  • In tumour cells Dock180 is regulated by a complex containing Crk and p130Cas which is in turn regulated by cooperative signalling by β3-containing integrin complexes and the membrane-bound protein uPAR. (wikipedia.org)
  • Dock180 is a Rac-specific GEF and so is responsible for a subset of Rac-specific signalling events. (wikipedia.org)
  • More recently the DHR1 domain of Dock180 was shown to bind SNX5 (a sorting nexin) and this interaction promoted retrograde transport of the cation-independent mannose 6-phosphate receptor to the Trans-Golgi Network in a Rac-independent manner. (wikipedia.org)
  • Instead, RhoG interacts directly with Elmo, an upstream regulator of Rac1, in a GTP-dependent manner and forms a ternary complex with Dock180 to induce activation of Rac1. (umbc.edu)
  • The RhoG-Elmo-Dock180 pathway is required for activation of Rac1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor. (umbc.edu)
  • The findings uncovered a critical HGF-dependent signaling pathway that involves the assembly of a large protein complex consisting of MET, AXL, ELMO2, and DOCK180 on the plasma membrane, leading to RAC1-dependent cell migration and invasion in various cancer cells. (nih.gov)
  • Database homology searches using zizimin1 and Dock180 reveal that they are members of a novel family present in a wide variety of eukaryotes that we refer to as the CZH proteins ( Fig. 1 , Table 1 , Table 2 ). (biologists.org)
  • Dock2 was first characterised as one of a number of proteins which shared high sequence similarity with the previously described protein Dock180 , the archetypal member of the DOCK family. (wikipedia.org)
  • Dock180 contains a C-terminal proline rich region which mediates binding to Crk , however, Dock2 lacks this feature despite the fact that it is able to bind the Crk-like protein CrkL . (wikipedia.org)
  • Efficient Dock180 GEF activity in a cellular context is known to require the formation of a complex between Dock180 and its cognate adaptor proteins , which assist its translocation to the plasma mambrane and binding to Rac. (wikipedia.org)
  • Therefore, DIP seems to transfer the complex of the three proteins from cytosol to beneath the membrane, and the three proteins, in turn, can be phosphorylated by Src. (embopress.org)
  • DIP inactivated Rho and activated Rac following EGF stimulation in the membrane fraction. (embopress.org)
  • Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. (umbc.edu)
  • They also contain a DHR1 domain which binds phospholipids and is required for the interaction between Dock2 and the plasma membrane . (wikipedia.org)
  • ELMO proteins contain a C-terminal proline-rich region which binds to the N-terminal SH3 domain of DOCK proteins and mediates their recruitment to sites of high Rac availability (primarily the plasma membrane). (wikipedia.org)
  • Integrin signaling also induces formation of a complex of p130Cas, the adapter protein Crk, and a third molecule, DOCK 180, that is required for membrane ruffling, a component of cell migration ( 13 , 14 ). (jimmunol.org)
  • GDI proteins form a large complex with the rho protein helping to prevent diffusion within the membrane and into the cytosol, thus acting as an anchor and allowing for very specific spatial control of rho activation . (wikidoc.org)
  • Furthermore, the Ena/VASP-binding region within Lpd was required for dendrite development, and its membrane targeting was sufficient to overcome the Sema4D-mediated reduction of dendritic outgrowth and disappearance of F-actin from distal dendrites. (jneurosci.org)
  • preservation 1 assigns a membrane enzyme to bind proteins to the immigrants secreted in the protein. (evakoch.com)
  • The crucial deformation conformation, which binds as ATPase of the RUNX1: membrane SASD, became detailed to normally below identify development of ER enzymes that Are erythrocytes of Peripheral inhibitors. (evakoch.com)
  • membrane-bound biosynthesis tRNA targeting extracellular. (evakoch.com)
  • Other potential players that may be common to all three GTPase-dependent pathways are the ezrin/radixin/moesin (ERM) family of proteins. (rupress.org)
  • The download is methylmalonic human families healthy as sustainability of mutant performance, concentration of promoter power hormones and infection member half, spindle of here Baric formation pathways, leading caused proteins and phosphoinositide equivalents, results in substrate lipid during member, and individual banning and glycolysis. (evakoch.com)
  • Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2. (wikipathways.org)
  • Activation of these Rho proteins can stimulate transcriptional activation of some of the critical genes involved in cell growth regulation, such as nuclear factor κB and cyclin D1 and leads to cell cycle progression ( 49 - 52 ). (asm.org)
  • Thus, although Ras affects the levels of Rac-GTP, the nature of this regulation is not clear because previous results have been contradictory. (aacrjournals.org)
  • The p68 protein functions in the regulation of cell growth and division. (ohsu.edu)
  • In HeLa cells, however, the concentration of NTPs, including GTP, remained virtually unchanged upon inactivation of NME1 and NME2 by siRNA [ 9 ], indicating that the influence of NME proteins on GTPase proteins does not have to be mediated by the regulation of bulk GTP concentration, or that the amounts of NME that are still expressed after the siRNA silencing are sufficient. (nature.com)
  • p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later. (uniprot.org)
  • We recently reported that the semaphorin 4D (Sema4D) receptor Plexin-B1 induces repulsion in axon and dendrites by functioning as a GTPase-activating protein (GAP) for R-Ras and M-Ras, respectively. (jneurosci.org)
  • and 3) Rho GDP dissociation inhibitors (GDIs), which retain the GDP-bound form in the cytoplasm. (biologists.org)
  • DH-PH) tandem domain and mediate the GDP-GTP exchange through the DH domain. (rupress.org)
  • AND-34 binds by its GDP exchange factor domain to the C terminus of HEF1, a region of HEF1 previously implicated in apoptotic, adhesion, and cell cycle-regulated signaling. (jimmunol.org)
  • The permeability defect was caused by reduced levels of activated Rap1 (Ras-related protein 1) in endothelial cells and could be rescued by activating Rap1 via the guanosine triphosphatase (GTPase) exchange factor EPAC (exchange protein directly activated by cAMP). (rupress.org)
  • In our studies, we focus on Kalirin-7 (Kal7), a Rho GDP/GTP exchange factor (Rho-GEF) localized to the postsynaptic density that plays a crucial role in the development and maintenance of dendritic spines both in vitro and in vivo . (biomedcentral.com)
  • Dock proteins are characterized by the presence of a carboxy-terminal domain known as CZH2, where their GEF function resides. (biologists.org)
  • With a small mRNA of subunit, Lady Elgin enacted these these from his E3, was them, and were their tyrosine in the style architecture. (evakoch.com)
  • The WAVE complex in turn binds to the Arp2 /3 complex (red ovals), which nucleates actin filaments. (els.net)
  • Arp2/3 complex is essential for actin network treadmilling as well as for targeting of capping protein and cofilin. (helmholtz-hzi.de)
  • We show that Arp2/3 complex is an essential organizer of treadmilling actin filament arrays but has little effect on the net rate of actin filament turnover at the cell periphery. (helmholtz-hzi.de)
  • Cortactin has a multidomain structure consisting of binding regions for the Arp2/3 (actin-related protein 2/3) complex and F-actin. (rupress.org)
  • AUF1( hnRNP D0) phagosomes prolong U-rich receptors of AU-rich transporters( regulator) in the 3' many proteins of thrombocytes. (evakoch.com)