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.-.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.Guanosine Diphosphate: A guanine nucleotide containing two phosphate groups esterified to the sugar moiety.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 3.6.1.47Amino 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.Guanosine 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.rab 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.-.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.cdc25 Phosphatases: A subclass of dual specificity phosphatases that play a role in the progression of the CELL CYCLE. They dephosphorylate and activate CYCLIN-DEPENDENT KINASES.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 3.6.1.47Pertussis 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.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.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.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.CDC2 Protein Kinase: Phosphoprotein with protein kinase activity that functions in the G2/M phase transition of the CELL CYCLE. It is the catalytic subunit of the MATURATION-PROMOTING FACTOR and complexes with both CYCLIN A and CYCLIN B in mammalian cells. The maximal activity of cyclin-dependent kinase 1 is achieved when it is fully dephosphorylated.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.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.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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.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.Thionucleotides: Nucleotides in which the base moiety is substituted with one or more sulfur atoms.GTPase-Activating Proteins: Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.Guanine Nucleotide Exchange Factors: Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.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.Cdc20 Proteins: Highly conserved proteins that specifically bind to and activate the anaphase-promoting complex-cyclosome, promoting ubiquitination and proteolysis of cell-cycle-regulatory proteins. Cdc20 is essential for anaphase-promoting complex activity, initiation of anaphase, and cyclin proteolysis during mitosis.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.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.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.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.Kinetics: The rate dynamics in chemical or physical systems.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.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.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.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.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).Tacrolimus Binding Proteins: A family of immunophilin proteins that bind to the immunosuppressive drugs TACROLIMUS (also known as FK506) and SIROLIMUS. EC 5.2.1.-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.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.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.Guanine NucleotidesPoly(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.Recombinant Proteins: Proteins prepared by recombinant DNA technology.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.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)Cell Line: Established cell cultures that have the potential to propagate indefinitely.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.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.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.RNA-Binding Proteins: Proteins that bind to RNA molecules. Included here are RIBONUCLEOPROTEINS and other proteins whose function is to bind specifically to RNA.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.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.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.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.CDC28 Protein Kinase, S cerevisiae: A protein kinase encoded by the Saccharomyces cerevisiae CDC28 gene and required for progression from the G1 PHASE to the S PHASE in the CELL CYCLE.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.Fungal Proteins: Proteins found in any species of fungus.cdc42 GTP-Binding Protein, Saccharomyces cerevisiae: A member of the Rho family of MONOMERIC GTP-BINDING PROTEINS from SACCHAROMYCES CEREVISIAE. It is involved in morphological events related to the cell cycle. This enzyme was formerly listed as EC 3.6.1.47.Guanosine Monophosphate: A guanine nucleotide containing one phosphate group esterified to the sugar moiety and found widely in nature.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.-.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.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.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.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.Bacterial Proteins: Proteins found in any species of bacterium.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.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.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.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.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.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.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.CDC2-CDC28 Kinases: A family of cell cycle-dependent kinases that are related in structure to CDC28 PROTEIN KINASE; S CEREVISIAE; and the CDC2 PROTEIN KINASE found in mammalian species.GTP Phosphohydrolase-Linked Elongation Factors: Factors that utilize energy from the hydrolysis of GTP to GDP for peptide chain elongation. EC 3.6.1.-.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.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.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.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.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.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.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).Molecular Weight: The sum of the weight of all the atoms in a molecule.Protein-Serine-Threonine Kinases: A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.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.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.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.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.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.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.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.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).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.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.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.Peptide Elongation Factors: Protein factors uniquely required during the elongation phase of protein synthesis.Genes, cdc: Genes that code for proteins that regulate the CELL DIVISION CYCLE. These genes form a regulatory network that culminates in the onset of MITOSIS by activating the p34cdc2 protein (PROTEIN P34CDC2).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.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.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.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.Ribosomes: Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.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.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.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.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.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.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.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.Mitosis: A type of CELL NUCLEUS division by means of which the two daughter nuclei normally receive identical complements of the number of CHROMOSOMES of the somatic cells of the species.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.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.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.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.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.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.PhosphoproteinsTATA-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.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.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.Insulin-Like Growth Factor Binding Protein 1: One of the six homologous proteins that specifically bind insulin-like growth factors (SOMATOMEDINS) and modulate their mitogenic and metabolic actions. The function of this protein is not completely defined. However, several studies demonstrate that it inhibits IGF binding to cell surface receptors and thereby inhibits IGF-mediated mitogenic and cell metabolic actions. (Proc Soc Exp Biol Med 1993;204(1):4-29)Cyclic AMP Response Element-Binding Protein: A protein that has been shown to function as a calcium-regulated transcription factor as well as a substrate for depolarization-activated CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASES. This protein functions to integrate both calcium and cAMP signals.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.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.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.Cell Cycle: The complex series of phenomena, occurring between the end of one CELL DIVISION and the end of the next, by which cellular material is duplicated and then divided between two daughter cells. The cell cycle includes INTERPHASE, which includes G0 PHASE; G1 PHASE; S PHASE; and G2 PHASE, and CELL DIVISION PHASE.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Cyclin B: A cyclin subtype that is transported into the CELL NUCLEUS at the end of the G2 PHASE. It stimulates the G2/M phase transition by activating CDC2 PROTEIN KINASE.Retinol-Binding Proteins: Proteins which bind with RETINOL. The retinol-binding protein found in plasma has an alpha-1 mobility on electrophoresis and a molecular weight of about 21 kDa. The retinol-protein complex (MW=80-90 kDa) circulates in plasma in the form of a protein-protein complex with prealbumin. The retinol-binding protein found in tissue has a molecular weight of 14 kDa and carries retinol as a non-covalently-bound ligand.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.Cell Nucleus: Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)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.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.CREB-Binding Protein: A member of the p300-CBP transcription factor family that was initially identified as a binding partner for CAMP RESPONSE ELEMENT-BINDING PROTEIN. Mutations in CREB-binding protein are associated with RUBINSTEIN-TAYBI SYNDROME.S100 Calcium Binding Protein G: A calbindin protein found in many mammalian tissues, including the UTERUS, PLACENTA, BONE, PITUITARY GLAND, and KIDNEYS. In intestinal ENTEROCYTES it mediates intracellular calcium transport from apical to basolateral membranes via calcium binding at two EF-HAND MOTIFS. Expression is regulated in some tissues by VITAMIN D.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.CCAAT-Enhancer-Binding Proteins: A class of proteins that were originally identified by their ability to bind the DNA sequence CCAAT. The typical CCAAT-enhancer binding protein forms dimers and consists of an activation domain, a DNA-binding basic region, and a leucine-rich dimerization domain (LEUCINE ZIPPERS). CCAAT-BINDING FACTOR is structurally distinct type of CCAAT-enhancer binding protein consisting of a trimer of three different subunits.Cytosol: Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.Phenotype: The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.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.Cross-Linking Reagents: Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.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.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Adenylate Cyclase: An enzyme of the lyase class that catalyzes the formation of CYCLIC AMP and pyrophosphate from ATP. EC 4.6.1.1.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Peptide Termination Factors: Proteins that are involved in the peptide chain termination reaction (PEPTIDE CHAIN TERMINATION, TRANSLATIONAL) on RIBOSOMES. They include codon-specific class-I release factors, which recognize stop signals (TERMINATOR CODON) in the MESSENGER RNA; and codon-nonspecific class-II release factors.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).)ran GTP-Binding Protein: A monomeric GTP-binding protein involved in nucleocytoplasmic transport of proteins into the nucleus and RNA into the cytoplasm. This enzyme was formerly listed as EC 3.6.1.47.Vitamin D-Binding Protein: An alpha-globulin found in the plasma of man and other vertebrates. It is apparently synthesized in the liver and carries vitamin D and its metabolites through the circulation and mediates the response of tissue. It is also known as group-specific component (Gc). Gc subtypes are used to determine specific phenotypes and gene frequencies. These data are employed in the classification of population groups, paternity investigations, and in forensic medicine.Schizosaccharomyces: A genus of ascomycetous fungi of the family Schizosaccharomycetaceae, order Schizosaccharomycetales.Mutagenesis: Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.Polypyrimidine Tract-Binding Protein: A RNA-binding protein that binds to polypyriminidine rich regions in the INTRONS of messenger RNAs. Polypyrimidine tract-binding protein may be involved in regulating the ALTERNATIVE SPLICING of mRNAs since its presence on an intronic RNA region that is upstream of an EXON inhibits the splicing of the exon into the final mRNA product.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Tumor Cells, Cultured: Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.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.Cell Division: The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.Insulin-Like Growth Factor Binding Protein 4: 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.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.Nucleotides: The monomeric units from which DNA or RNA polymers are constructed. They consist of a purine or pyrimidine base, a pentose sugar, and a phosphate group. (From King & Stansfield, A Dictionary of Genetics, 4th ed)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.Insulin-Like Growth Factor Binding Protein 5: 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.Repressor Proteins: Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.Protein Kinases: A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.Schizosaccharomyces pombe Proteins: Proteins obtained from the species Schizosaccharomyces pombe. 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.Subcellular Fractions: Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Chromatography, Affinity: A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Magnesium: A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.Dimerization: The process by which two molecules of the same chemical composition form a condensation product or polymer.Sterol Regulatory Element Binding Protein 1: A sterol regulatory element binding protein that regulates expression of GENES involved in FATTY ACIDS metabolism and LIPOGENESIS. Two major isoforms of the protein exist due to ALTERNATIVE SPLICING.Endoplasmic Reticulum: A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Dynamin I: A subtype of dynamin found primarily in the NEURONS of the brain.Cytoskeleton: The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.Peptide Elongation Factor 2: Peptide Elongation Factor 2 catalyzes the translocation of peptidyl-tRNA from the A site to the P site of eukaryotic ribosomes by a process linked to the hydrolysis of GTP to GDP.ras-GRF1: A guanine nucleotide exchange factor that is expressed primarily in neuronal tissue and may be specific for the Ha-ras homolog of the RAS PROTEINS.Ubiquitin-Protein Ligase Complexes: Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES).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.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.Anaphase-Promoting Complex-Cyclosome: An E3 ubiquitin ligase primarily involved in regulation of the metaphase-to-anaphase transition during MITOSIS through ubiquitination of specific CELL CYCLE PROTEINS. Enzyme activity is tightly regulated through subunits and cofactors, which modulate activation, inhibition, and substrate specificity. The anaphase-promoting complex, or APC-C, is also involved in tissue differentiation in the PLACENTA, CRYSTALLINE LENS, and SKELETAL MUSCLE, and in regulation of postmitotic NEURONAL PLASTICITY and excitability.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.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.Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Insulin-Like Growth Factor I: A well-characterized basic peptide believed to be secreted by the liver and to circulate in the blood. It has growth-regulating, insulin-like, and mitogenic activities. This growth factor has a major, but not absolute, dependence on GROWTH HORMONE. It is believed to be mainly active in adults in contrast to INSULIN-LIKE GROWTH FACTOR II, which is a major fetal growth factor.Plant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Cell Fractionation: Techniques to partition various components of the cell into SUBCELLULAR FRACTIONS.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.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.DNA Replication: The process by which a DNA molecule is duplicated.Nerve Tissue ProteinsMaltose-Binding Proteins: Periplasmic proteins that bind MALTOSE and maltodextrin. They take part in the maltose transport system of BACTERIA.Heterogeneous-Nuclear Ribonucleoproteins: A family of ribonucleoproteins that were originally found as proteins bound to nascent RNA transcripts in the form of ribonucleoprotein particles. Although considered ribonucleoproteins they are primarily classified by their protein component. They are involved in a variety of processes such as packaging of RNA and RNA TRANSPORT within the nucleus. A subset of heterogeneous-nuclear ribonucleoproteins are involved in additional functions such as nucleocytoplasmic transport (ACTIVE TRANSPORT, CELL NUCLEUS) of RNA and mRNA stability in the CYTOPLASM.Spectrometry, Fluorescence: Measurement of the intensity and quality of fluorescence.Brain: The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.Precipitin Tests: Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.Trypsin: A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.

Reactive oxygen intermediate-dependent NF-kappaB activation by interleukin-1beta requires 5-lipoxygenase or NADPH oxidase activity. (1/1676)

We previously reported that the role of reactive oxygen intermediates (ROIs) in NF-kappaB activation by proinflammatory cytokines was cell specific. However, the sources for ROIs in various cell types are yet to be determined and might include 5-lipoxygenase (5-LOX) and NADPH oxidase. 5-LOX and 5-LOX activating protein (FLAP) are coexpressed in lymphoid cells but not in monocytic or epithelial cells. Stimulation of lymphoid cells with interleukin-1beta (IL-1beta) led to ROI production and NF-kappaB activation, which could both be blocked by antioxidants or FLAP inhibitors, confirming that 5-LOX was the source of ROIs and was required for NF-kappaB activation in these cells. IL-1beta stimulation of epithelial cells did not generate any ROIs and NF-kappaB induction was not influenced by 5-LOX inhibitors. However, reintroduction of a functional 5-LOX system in these cells allowed ROI production and 5-LOX-dependent NF-kappaB activation. In monocytic cells, IL-1beta treatment led to a production of ROIs which is independent of the 5-LOX enzyme but requires the NADPH oxidase activity. This pathway involves the Rac1 and Cdc42 GTPases, two enzymes which are not required for NF-kappaB activation by IL-1beta in epithelial cells. In conclusion, three different cell-specific pathways lead to NF-kappaB activation by IL-1beta: a pathway dependent on ROI production by 5-LOX in lymphoid cells, an ROI- and 5-LOX-independent pathway in epithelial cells, and a pathway requiring ROI production by NADPH oxidase in monocytic cells.  (+info)

Myelin and collapsin-1 induce motor neuron growth cone collapse through different pathways: inhibition of collapse by opposing mutants of rac1. (2/1676)

Precise growth cone guidance is the consequence of a continuous reorganization of actin filament structures within filopodia and lamellipodia in response to inhibitory and promoting cues. The small GTPases rac1, cdc42, and rhoA are critical for regulating distinct actin structures in non-neuronal cells and presumably in growth cones. Collapse, a retraction of filopodia and lamellipodia, is a typical growth cone behavior on contact with inhibitory cues and is associated with depolymerization and redistribution of actin filaments. We examined whether small GTPases mediate the inhibitory properties of CNS myelin or collapsin-1, a soluble semaphorin, in chick embryonic motor neuron cultures. As demonstrated for collapsin-1, CNS myelin-evoked growth cone collapse was accompanied by a reduction of rhodamine-phalloidin staining most prominent in the growth cone periphery, suggesting actin filament disassembly. Specific mutants of small GTPases were capable of desensitizing growth cones to CNS myelin or collapsin-1. Adenoviral-mediated expression of constitutively active rac1 or rhoA abolished CNS myelin-induced collapse and allowed remarkable neurite extension on a CNS myelin substrate. In contrast, expression of dominant negative rac1 or cdc42 negated collapsin-1-induced growth cone collapse and promoted neurite outgrowth on a collapsin-1 substrate. These findings suggest that small GTPases can modulate the signaling pathways of inhibitory stimuli and, consequently, allow the manipulation of growth cone behavior. However, the fact that opposite mutants of rac1 were effective against different inhibitory stimuli speaks against a universal signaling pathway underlying growth cone collapse.  (+info)

Activation of the Cdc42-associated tyrosine kinase-2 (ACK-2) by cell adhesion via integrin beta1. (3/1676)

Activated Cdc42-associated kinase-2 (ACK-2) is a non-receptor tyrosine kinase that appears to be a highly specific target for the Rho-related GTP-binding protein Cdc42. In order to understand better how ACK-2 activity is regulated in cells, we have expressed epitope-tagged forms of this tyrosine kinase in COS-7 and NIH3T3 cells. We find that ACK-2 can be activated by cell adhesion in a Cdc42-dependent manner. However, unlike the focal adhesion kinase, which also is activated by cell adhesion, the activation of ACK-2 is F-actin-independent and does not require cell spreading. In addition, overexpression of ACK-2 in COS-7 cells did not result in the stimulation of extracellular signal-regulated kinase activity but rather activated the c-Jun kinase. Both anti-integrin beta1 antibody and RGD peptides inhibited the activation of ACK-2 by cell adhesion. In addition, ACK-2 was co-immunoprecipitated with integrin beta1. Overall, these findings suggest that ACK-2 interacts with integrin complexes and mediates cell adhesion signals in a Cdc42-dependent manner.  (+info)

Rho GTPases control polarity, protrusion, and adhesion during cell movement. (4/1676)

Cell movement is essential during embryogenesis to establish tissue patterns and to drive morphogenetic pathways and in the adult for tissue repair and to direct cells to sites of infection. Animal cells move by crawling and the driving force is derived primarily from the coordinated assembly and disassembly of actin filaments. The small GTPases, Rho, Rac, and Cdc42, regulate the organization of actin filaments and we have analyzed their contributions to the movement of primary embryo fibroblasts in an in vitro wound healing assay. Rac is essential for the protrusion of lamellipodia and for forward movement. Cdc42 is required to maintain cell polarity, which includes the localization of lamellipodial activity to the leading edge and the reorientation of the Golgi apparatus in the direction of movement. Rho is required to maintain cell adhesion during movement, but stress fibers and focal adhesions are not required. Finally, Ras regulates focal adhesion and stress fiber turnover and this is essential for cell movement. We conclude that the signal transduction pathways controlled by the four small GTPases, Rho, Rac, Cdc42, and Ras, cooperate to promote cell movement.  (+info)

Inhibition of myosin light chain kinase by p21-activated kinase. (5/1676)

p21-activated kinases (PAKs) are implicated in the cytoskeletal changes induced by the Rho family of guanosine triphosphatases. Cytoskeletal dynamics are primarily modulated by interactions of actin and myosin II that are regulated by myosin light chain kinase (MLCK)-mediated phosphorylation of the regulatory myosin light chain (MLC). p21-activated kinase 1 (PAK1) phosphorylates MLCK, resulting in decreased MLCK activity. MLCK activity and MLC phosphorylation were decreased, and cell spreading was inhibited in baby hamster kidney-21 and HeLa cells expressing constitutively active PAK1. These data indicate that MLCK is a target for PAKs and that PAKs may regulate cytoskeletal dynamics by decreasing MLCK activity and MLC phosphorylation.  (+info)

Distinct roles for the small GTPases Cdc42 and Rho in endothelial responses to shear stress. (6/1676)

Shear stress, the tangential component of hemodynamic forces, plays an important role in endothelial remodeling. In this study, we investigated the role of Rho family GTPases Cdc42 and Rho in shear stress-induced signal transduction and cytoskeleton reorganization. Our results showed that shear stress induced the translocation of Cdc42 and Rho from cytosol to membrane. Although both Cdc42 and Rho were involved in the shear stress-induced transcription factor AP-1 acting on the 12-O-tetradecanoyl-13-phorbol-acetate-responsive element (TRE), only Cdc42 was sufficient to activate AP-1/TRE. Dominant-negative mutants of Cdc42 and Rho, as well as recombinant C3 exoenzyme, attenuated the shear stress activation of c-Jun NH2-terminal kinases (JNKs), suggesting that Cdc42 and Rho regulate the shear stress induction of AP-1/TRE activity through JNKs. Shear stress-induced cell alignment and stress fiber formation were inhibited by the dominant-negative mutants of Rho and p160ROCK, but not by the dominant-negative mutant of Cdc42, indicating that the Rho-p160ROCK pathway regulates the cytoskeletal reorganization in response to shear stress.  (+info)

Nucleotide binding to the G12V-mutant of Cdc42 investigated by X-ray diffraction and fluorescence spectroscopy: two different nucleotide states in one crystal. (7/1676)

The 2.5 A crystal structure of the full length human placental isoform of the Gly12 to Val mutant Cdc42 protein (Cdc42(G12V)) bound to both GDP/Mg2+ and GDPNH2 (guanosine-5'-diphospho-beta-amidate) is reported. The crystal contains two molecules in the asymmetric unit, of which one has bound GDP/Mg2+, while the other has bound GDPNH2 without a Mg2+ ion. Crystallization of the protein was induced via hydrolysis of the Cdc42 x GppNHp complex by the presence of contaminating alkaline phosphatase activity in combination with the crystallization conditions. This prompted us to compare the binding characteristics of GDPNH2 vs. GDP. The amino group of GDPNH2 drastically reduces the affinity to Cdc42 in comparison with that of GDP, causes the loss of the Mg2+ ion, and apparently also increases the conformational flexibility of the protein as seen in the crystal. Both the switch I and switch II regions are visible in the electron density of the GDP-bound molecule, but not in the molecule bound to GDPNH2. The C-terminus containing the CaaX-motif is partly ordered in both molecules due to an intramolecular disulfide bond formed between Cys105/Cys188 and Cys305/Cys388, respectively.  (+info)

The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. (8/1676)

Although small GTP-binding proteins of the Rho family have been implicated in signaling to the actin cytoskeleton, the exact nature of the linkage has remained obscure. We describe a novel mechanism that links one Rho family member, Cdc42, to actin polymerization. N-WASP, a ubiquitously expressed Cdc42-interacting protein, is required for Cdc42-stimulated actin polymerization in Xenopus egg extracts. The C terminus of N-WASP binds to the Arp2/3 complex and dramatically stimulates its ability to nucleate actin polymerization. Although full-length N-WASP is less effective, its activity can be greatly enhanced by Cdc42 and phosphatidylinositol (4,5) bisphosphate. Therefore, N-WASP and the Arp2/3 complex comprise a core mechanism that directly connects signal transduction pathways to the stimulation of actin polymerization.  (+info)

The Ras guanine-nucleotide exchange factor Ras-GRF/Cdc25(Mn) harbors a complex array of structural motifs that include a Dbl-homology (DH) domain, usually found in proteins that interact functionally with the Rho family GTPases, and the role of which is not yet fully understood. Here, we present evidence that Ras-GRF requires its DH domain to translocate to the membrane, to stimulate exchange on Ras, and to activate mitogen-activated protein kinase (MAPK). In an unprecedented fashion, we have found that these processes are regulated by the Rho family GTPase Cdc42. We show that GDP- but not GTP-bound Cdc42 prevents Ras-GRF recruitment to the membrane and activation of Ras/MAPK, although no direct association of Ras-GRF with Cdc42 was detected. We also demonstrate that catalyzing GDP/GTP exchange on Cdc42 facilitates Ras-GRF-induced MAPK activation. Moreover, we show that the potentiating effect of ionomycin on Ras-GRF-mediated MAPK stimulation is also regulated by Cdc42. These results provide the ...
Here, we report a novel mechanism of PDZ (PSD-95/Dlg/ZO-1) domain regulation that distorts a conserved element of PDZ ligand recognition. The polarity regulator Par-6 assembles a conserved multiprotein complex and is directly modulated by the Rho GTPase Cdc42. Cdc42 binds the adjacent Cdc42/Rac interactive binding (CRIB) and PDZ domains of Par-6, increasing C-terminal ligand binding affinity by 10-fold. By solving structures of the isolated PDZ domain and a disulfide-stabilized CRIB-PDZ, we detected a conformational switch that controls affinity by altering the configuration of the conserved GLGF loop. As a result, lysine 165 is displaced from the PDZ core by an adjacent hydrophobic residue, disrupting coordination of the PDZ ligand-binding cleft. Stabilization of the CRIB:PDZ interface restores K165 to its canonical location in the binding pocket. We conclude that a unique dipeptide switch in the Par-6 PDZ transmits a signal for allosteric activation to the ligand-binding pocket. ...
Genghis khan was isolated in a search for proteins that physically interact with the Drosophila small GTPases Rac1 and Cdc42. Gek does not bind to Cdc42N17, a dominant negative mutant that preferentially stays in the GDP-bound state. The ability of Gek to bind Cdc42 in its GTP-bound form (but not in its GDP-bound form) suggests that Gek is an effector of Cdc42. A mutation in the Cdc42 effector domain (A35), which is important for signaling to downstream targets, eliminates Gek binding. Gek does not bind to Drosophila Rac. Deletion of three residues in Gek, which correspond to three conserved residues of the Cdc42/Rac interactive binding (CRIB) domain, disrupt Geks binding to Cdc42. Gek exhibits kinase activity using histone as a substrate (Luo, 1997).. Cdc42, a Rho family GTPase that acts through Gek The small GTPases of the Rac/Rho/Cdc42 subfamily are implicated in actin cytoskeleton-membraneinteraction in mammalian cells and budding yeast. The in vivo functions of these GTPases ...
S. pombe cdc42+ suppressed the S. cerevisiae cdc24-4ts mutation and the S. cerevisiae BEM3 and RGA1 GAPs reversed this suppression: Previous studies have shown that S. cerevisiae CDC42 on a low-copy vector was able to suppress the cdc24-4ts mutation in the presence of 1 m sorbitol (Bender and Pringle 1989). Presumably, levels of activated GTP-bound Cdc42p are reduced in the cdc24-4 mutant at 37° and suppression is through an increase in levels of GTP-bound Cdc42p upon overexpression. Addition of a high-copy vector containing either the S. cerevisiae BEM3 or RGA1-encoded GAP reverses this suppression, presumably by inactivation of the Cdc42-GTP to a GDP-bound state (Bi and Pringle 1996). S. pombe cdc42+ under S. cerevisiae CDC42 promoter control was inserted into a low-copy S. cerevisiae plasmid (pRS315-cdc42+) and transformed into cdc24-4ts strain Y147. This plasmid was able to suppress the cdc24-4ts mutant at 37° in the presence of 1 m sorbitol (Figure 1). In addition, high-copy plasmids ...
Kaur R., Liu X., Gjoerup O., Zhang A., Yuan X., Balk S.P., Schneider M.C., Lu M.L.. The p21-activated kinases (PAKs) contain an N-terminal Cdc42/Rac interactive binding domain, which in the group 1 PAKs (PAK1, 2, and 3) regulates the activity of an adjacent conserved autoinhibitory domain. In contrast, the group 2 PAKs (PAK4, 5, and 6) lack this autoinhibitory domain and are not activated by Cdc42/Rac binding, and the mechanisms that regulate their kinase activity have been unclear. This study found that basal PAK6 kinase activity was repressed by a p38 mitogen-activated protein (MAP) kinase antagonist and could be strongly stimulated by constitutively active MAP kinase kinase 6 (MKK6), an upstream activator of p38 MAP kinases. Mutation of a consensus p38 MAP kinase target site at serine 165 decreased PAK6 kinase activity. Moreover, PAK6 was directly activated by MKK6, and mutation of tyrosine 566 in a consensus MKK6 site (threonine-proline-tyrosine, TPY) in the activation loop of the PAK6 ...
J:149918 Fuchs S, Herzog D, Sumara G, Buchmann-Moller S, Civenni G, Wu X, Chrostek-Grashoff A, Suter U, Ricci R, Relvas JB, Brakebusch C, Sommer L, Stage-specific control of neural crest stem cell proliferation by the small rho GTPases Cdc42 and Rac1. Cell Stem Cell. 2009 Mar 6;4(3):236-47 ...
Prerequisites for all modes of cell migration are cell-substratum interactions that require a sophisticated interplay of membrane dynamics and cytoskeletal rearrangement. Generally, a migrating cell is polarized with a distinct rear and front, from which it extends a wide and thin membrane protrusion- lamellipodium, small fingerlike projections- filopodia, and membrane blisters- blebs. The development of these structures is primarily driven by cytoskeletal contractions and actin polymerization, which are under regulation of several actin-binding proteins and the small GTPases Cdc42, Rac and Rho. Lamellipodia and filopodia are assumed to arise from polymerizing actin, pushing the membrane forward through a Brownian-ratchet mechanism. However, other models based on shifts in the local hydrostatic pressure have also been suggested since blebs are initially void of actin. Recently, fluxes of water through membrane-anchored water channels, aquaporins (AQPs), have been implicated in cell motility, ...
Active Cdc42 ELISA Activation Assay - colorimetric format offers a sensitive and accurate dection of active Cdc42 GTPase. Additional assays for small GTPases including Rho, Ras, Cdc42, Rac, Ral, Arf also available in pull-down and G-LISA formats.
摘 要:胚胎干细胞的生长、增殖、分化和形状改变等过程受微环境、机械力等多种因素的影响。胚胎干细胞能够感知微小机械力刺激,并将其转化成生物化学信号,进而通过F-肌动蛋白、肌球蛋白-II、Cdc42、Rho和Src等产生一系列分子水平的应答反应,最终导致基因差异表达。胚胎干细胞应答外力基本过程的研究对于胚胎早期发育和分化机制研究、克隆和再生药物的研制与开发等均有重要意义。该文就机械力对胚胎干细胞结构、形态和分化的影响及其潜在机制等进行论述 ...
The Dbl family of guanine nucleotide exchange factors are multifunctional molecules that transduce diverse intracellular signals leading to the activation of Rho GTPases. The tandem Dbl-homology and pleckstrin-homology domains shared by all members of this family represent the structural module resp …
Many signaling pathways control cell shape, and these pathways ultimately do so, at least in part, by regulating polymerization of actin. Members of the WASP (Wiskott-Aldrich syndrome protein) family appear to integrate such signals and are thus subject to a complex array of regulatory mechanisms. Activation of WASP through the Rho family GTPase Cdc42 and interaction with phosphatidylinositol 4,5-bisphosphate (PIP2) stimulate the Arp2/3 complex, which in turn promotes nucleation of actin filaments. Papers by Higgs and Pollard and Rohatgi et al. characterizing native WASP from bovine thymus and in vitro-translated N-WASP (where N refers to neuronal, even though this family member is widely expressed) and the Commentary by Zigmond provide new details of this multifaceted regulation. The NH2-terminus of WASP appears to interact with the COOH-terminus and block binding to Arp2/3. Activation by Cdc42 and PIP2 reduces the autoinhibitory binding and exposes the Arp2/3 binding region. Rohatgi et al. use ...
RhoA of the Rho Family Small GTPases Is Essential for B Lymphocyte Development. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
The member of Rho family of small GTPases Cdc42 plays important and conserved roles in cell polarity and motility. The Cdc42ep family proteins have been identified to bind to Cdc42, yet how they interact with Cdc42 to regulate cell migration remains to be elucidated. In this study, we focus on Cdc42ep1, which is expressed predominantly in the highly migratory neural crest cells in frog embryos. Through morpholino-mediated knockdown, we show that Cdc42ep1 is required for the migration of cranial neural crest cells. Loss of Cdc42ep1 leads to rounder cell shapes and the formation of membrane blebs, consistent with the observed disruption in actin organization and focal adhesion alignment. As a result, Cdc42ep1 is critical for neural crest cells to apply traction forces at the correct place to migrate efficiently. We further show that Cdc42ep1 is localized to two areas in neural crest cells: in membrane protrusions together with Cdc42 and in perinuclear patches where Cdc42 is absent. Cdc42 directly ...
Prerequisites for all modes of cell migration are cell-substratum interactions that require a sophisticated interplay of membrane dynamics and cytoskeletal rearrangement. Generally, a migrating cell is polarized with a distinct rear and front, from which it extends a wide and thin membrane protrusion- lamellipodium, small fingerlike projections- filopodia, and membrane blisters- blebs. The development of these structures is primarily driven by cytoskeletal contractions and actin polymerization, which are under regulation of several actin-binding proteins and the small GTPases Cdc42, Rac and Rho. Lamellipodia and filopodia are assumed to arise from polymerizing actin, pushing the membrane forward through a Brownian-ratchet mechanism. However, other models based on shifts in the local hydrostatic pressure have also been suggested since blebs are initially void of actin. Recently, fluxes of water through membrane-anchored water channels, aquaporins (AQPs), have been implicated in cell motility, ...
The constant self renewal and differentiation of adult intestinal stem cells maintains a functional intestinal mucosa for a lifetime. However, the molecular mechanisms that regulate intestinal stem cell division and epithelial homeostasis are largely undefined. We report here that the small GTPases Cdc42 and Rab8a are critical regulators of these processes in mice. Conditional ablation of Cdc42 in the mouse intestinal epithelium resulted in the formation of large intracellular vacuolar structures containing microvilli (microvillus inclusion bodies) in epithelial enterocytes, a phenotype reminiscent of human microvillus inclusion disease (MVID), a devastating congenital intestinal disorder that results in severe nutrient deprivation. Further analysis revealed that Cdc42-deficient stem cells had cell division defects, reduced capacity for clonal expansion and differentiation into Paneth cells, and increased apoptosis. Cdc42 deficiency impaired Rab8a activation and its association with multiple ...
... DISCUSSION In the present study we investigated the effect of ionizing radiation (IR) on the expression of the
DOCK-C subfamily proteins (DOCK6-8) partially conserve the Cdc42-interacting residues of DOCK939 and the Rac1-interacting residues of DOCK2.40 To understand the mechanism underlying the Cdc42 specificity of DOCK8, we performed X-crystallographic analysis of the complex between the DOCK8 DHR-2 domain and the dominant-negative T17N mutant of Cdc42 (supplemental Table 1). Two lobes (lobes B and C) of DOCK8 DHR-2 generate a cooperative interface with Cdc42 (Figure 6C) in a manner similar to DOCK9 DHR-2.39 Based on the DOCK6 structural model, it was predicted that Met1932 of DOCK6 would be incompatible with the aromatic side chain at position 56 (Phe, Tyr, or Trp) that is conserved in nearly all of the Rho family of GTPases.40 However, the DOCK8 DHR-2·Cdc42 complex structure revealed that DOCK8 Met1976, corresponding to Met1932 of DOCK6, assumes a bent side-chain conformation and thereby avoids the putative steric hindrance with the Phe56 side chain of Cdc42 (Figure 6D). When the structure of Rac1 ...
Zou W, Greenblatt MB, Shim JH, Kant S, Zhai B, Lotinun S, Brady N, Hu DZ, Gygi SP, Baron R, Davis RJ, Jones D, Glimcher LH. MLK3 regulates bone development downstream of the faciogenital dysplasia protein FGD1 in mice. J Clin Invest. 2011 Nov; 121(11):4383-92 ...
H Si, H Lu... Z Chen "TNF-α modulates genome-wide redistribution of ΔNp63α/TAp73 and NF-κB cREL interactive binding on TP53 and AP-1 motifs to promote an oncogenic gene program in squamous cancer." Oncogene 35:44 5781-5794 ...
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Cdc42 and Rac1 have distinct but overlapping binding sites on PICK1.Upper panel: GST pulldowns were carried out using purified his6flagCdc42 or his6mycRac1 and
Information on what to do if you have been exposed to TB, and links for patients and health care providers. Provided by the Centers for Disease Control and Prevention (CDC).
I logged on to this site after following a link from CDC. I was curious about CD and considering a change from LL. After reading the ridiculous opinions of...
PAK5兔多克隆抗体(ab110069)可与大鼠, 人样本反应并经WB, IHC实验严格验证,被1篇文献引用。所有产品均提供质保服务,中国75%以上现货。
PAK4兔多克隆抗体(ab17974)可与人样本反应并经WB, IP实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
Members of the Rho family of GTP‐binding proteins function as molecular switches in biological response pathways that result in changes in the actin cytoskeletal architecture, the stimulation of cell cycle progression and gene transcription, and the regulation of intracellular trafficking activities (Van Aelst and DSouza‐Schorey, 1997; Hall, 1998; Bar‐Sagi and Hall, 2000; Erickson and Cerione, 2001). Three classes of proteins, GTPase‐activating proteins (GAPs), guanine nucleotide dissociation inhibitors (GDIs), and guanine nucleotide exchange factors (GEFs), regulate the cycling of these GTP‐binding proteins between their GDP‐bound and GTP‐bound states (Boguski and McCormick, 1993). Rho family proteins, such as Cdc42 and Rac, are activated by a number of upstream stimuli, as mediated by members of the Dbl (diffuse B‐cell lymphoma) family of GEFs (Whitehead et al, 1997; Hoffman and Cerione, 2002). One subgroup of the Dbl family, the Cool/Pix proteins (Cool for cloned‐out of ...
TY - JOUR. T1 - Cdc42 overexpression induces hyperbranching in the developing mammary gland by enhancing cell migration. AU - Bray, Kristi. AU - Gillette, Melissa. AU - Young, Jeanette. AU - Loughran, Elizabeth. AU - Hwang, Melissa. AU - Sears, James C.. AU - Vargo-Gogola, Tracy. PY - 2013/9/30. Y1 - 2013/9/30. N2 - Introduction: The Rho GTPase Cdc42 is overexpressed and hyperactivated in breast tumors compared to normal breast tissue. Cdc42 regulates key processes that are critical for mammary gland morphogenesis and become disrupted during the development, progression, and metastasis of breast cancer. However, the contribution of Cdc42 to normal and neoplastic mammary gland development in vivo remains poorly understood. We were therefore interested in investigating the effects of Cdc42 overexpression on mammary gland morphogenesis as a first step toward understanding how its overexpression may contribute to mammary tumorigenesis.Methods: We developed a tetracycline-regulatable Cdc42 ...
In yeast, Cdc42 is required to polarize the site of bud formation, and several in vitro studies show that it may also be required for efficient polarization of eukaryotic cells (Etienne-Manneville, 2004). Furthermore, for monocytes in culture, blocking Cdc42 signaling leads to a failure to receive and respond to chemotactic cues (Allen et al., 1998; Chou et al., 2003; Srinivasan et al., 2003). However, our in vivo studies in the fly embryo reveal no significant effect on the numbers of hemocytes recruited to laser wounds after 1 h in Cdc42 mutant embryos. This finding is true also for embryos expressing the dominant-negative Cdc42N17 and Cdc42S89 transgenes specifically in hemocytes (Fig. 3 a). Both developmental dispersal of hemocytes and their recruitment to sites of tissue damage appears grossly normal. But on closer inspection, we observe that hemocyte motility is abnormal. During the migratory phase, and once hemocytes have reached the wound, we frequently see cells with several leading ...
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase alpha. Serine/Threonine Kinases (STKs), DMPK-like subfamily, DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK) alpha isoform, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCKalpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. ...
Objectives: The Rho subfamily of small GTPases, including RhoA, Rac1, and Cdc42, regulates diverse cellular functions, including polarity and migration. Our prior studies established an essential role for Cdc42 in vascular network assembly, demonstrating that the genetic inactivation of Cdc42 yields defective vascular morphogenesis due to impaired migration of endothelial precursor cells. We have further shown that protein kinase Ciota and glycogen synthase kinase-3 Beta are downstream effectors of Cdc42 involved in mediating vascular network assembly. The objective of this study was to elucidate the guanine nucleotide exchange factors (GEFs) that activate Cdc42; specifically, we investigated the role of Zizimin1 and its effects on Cdc42 and vasculogenesis.. Methods: We performed affinity pulldown assays using a nucleotide-free Cdc42 G15A mutant that specifically binds to Cdc42 GEFs. Mass spectrometric analysis identified Zizimin1 as a candidate Cdc42 GEF.. Results: During vasculogenesis in ...
Several studies have identified Rho family GTPases (i.e. Rho, Rac, Cdc42) as mediators of diverse critical cellular processes, such as actin cytoskeleton remodeling, gene transcription, cell-cell adhesion, and cell cycle progression. However, more recent data highlight an essential role for Rho GTPases as regulators of neuronal morphology and neuronal survival. In particular, Rac GTPase generally induces neurite outgrowth and promotes neuronal survival while Rho GTPase typically provokes neurite retraction and induces neuronal apoptosis. However, the precise signaling pathways that regulate neuronal survival downstream of Rho GTPases and the potential involvement of dysregulated activity of Rho GTPases as a causative factor in the progression of neurodegenerative diseases remains to be elucidated. Consistent with a pro-survival function for Rac in neurons, inhibition of Rac with Clostridium difficle toxin B (ToxB) or expression of a dominant negative Rac1 mutant significantly induces activation of the
The sequential and regulated recruitment of leukocytes into tissues by chemoattractants is essential for effective clearance of pathogens and healing. The Rho GTPases Cdc42, Rac, and Rho are important for establishing and maintaining migratory polarity. Most chemoattractants for phagocytes signal either through seven transmembrane G-protein-coupled receptors (GPCRs) or tyrosine kinase receptors. Y721 is the most important for chemotaxis because it recruits phospholipase-C-γ (PL C-γ) and the p85 subunit of class 1A PI3Ks, both of which are implicated in the initiation of chemotaxis. Several intracellular signaling complexes contribute to the polarization of phagocytes in response to chemoattractants, and they probably act together to allow optimal chemotaxis. Cdc42 is implicated in multiple types of cell polarity, including axon specification, yeast mating, and epithelial polarity. There are several PLC isoforms, of which PLCβ2 and PLCβ3 are activated by GPCR signaling in neutrophils, whereas PLCβ
PAK proteins are involved in the regulation of cellular processes such as gene transcription, cell morphology, motility and apoptosis (Bagrodia and Cerione, 1999; Daniels and Bokoch, 1999; Jaffer and Chernoff, 2002). Our results illustrate that different PAK proteins fulfil distinct functions in the same cell. In the developing photoreceptor cells, D-PAK is required in growth cones to control axon guidance (Hing et al., 1999) whereas Mbt is localised at AJs and is required for cell morphogenesis.. One major difference between group I and group II PAKs is the regulation of kinase activity. For group I PAK proteins it has been shown that binding of GTP-bound Cdc42 or Rac releases the inhibitory effect of the KID on catalytic activity (Buchwald et al., 2001; Chong et al., 2001; Lei et al., 2000). The lack of an obvious KID in group II PAKs (Fig. 5C) is reflected by their distinct biochemical properties. In contrast to group I PAKs, a slightly reduced rather than enhanced kinase activity is observed ...
The Rho family of GTPases is a family of small (~21 kDa) signaling G proteins, and is a subfamily of the Ras superfamily. The members of the Rho GTPase family have been shown to regulate many aspects of intracellular actin dynamics, and are found in all eukaryotic kingdoms, including yeasts and some plants. Three members of the family have been studied in detail: Cdc42, Rac1, and RhoA. All G proteins are "molecular switches", and Rho proteins play a role in organelle development, cytoskeletal dynamics, cell movement, and other common cellular functions. Identification of the Rho family of GTPases began in the mid-1980s. The first identified Rho member was RhoA, isolated serendipitously in 1985 from a low stringency cDNA screening. Rac1 and Rac2 were identified next, in 1989 followed by Cdc42 in 1990. Eight additional mammalian Rho members were identified from biological screenings until the late 1990s, a turning point in biology where availability of complete genome sequences allowed full ...
Rho GTPases are master regulators of many immunoreceptors, ranging from receptors required for differentiation and maturation of immune cells and for pathogen recognition to receptors involved in pathogen uptake and the subsequent host signaling responses. Several TLRs induce the activation of the Rho family GTPases Rac, Rho, and Cdc42. Almost every cell type, including professional innate immune cells such as macrophages, neutrophils, and dendritic cells, responds to TLR stimulation by activating Rho GTPases rapidly (8, 20, 31). Similarly, lung epithelial cells induce Rho GTPase activation when they encounter TLR ligands. It seems apparent that RhoA activation depends on the interaction of a specific TLR ligand with its cognate TLR, independently of the connecting adapters or the cellular compartment where TLR signaling occurs. A RhoA FRET probe was used to examine localized RhoA activity at early time points after initiation of TLR2 or TLR3 signaling. After 3-5 min of treatment with the TLR2 ...
May be involved in several stages of intracellular trafficking (By similarity). Could play an important role in the regulation of glucose transport by insulin. May act as a downstream effector of RHOQ/TC10 in the regulation of insulin-stimulated glucose transport.
This gene encodes a member of a large family of proteins that activate Rho-type guanosine triphosphate (GTP) metabolizing enzymes. The encoded protein may pay a role in clathrin-mediated endocytosis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Aug 2013 ...
MKSRQKGKKKGSAKERVFGCDLQEHLQHSGQEVPQVLKSCAEFVEEYGVVDGIYRLSGVSSNIQKLRQEF 1 - 70 ESERKPDLRRDVYLQDIHCVSSLCKAYFRELPDPLLTYRLYDKFAEAVGVQLEPERLVKILEVLRELPVP 71 - 140 NYRTLEFLMRHLVHMASFSAQTNMHARNLAIVWAPNLLRSKDIEASGFNGTAAFMEVRVQSIVVEFILTH 141 - 210 VDQLFGGAALSGGEVESGWRSLPGTRASGSPEDLMPRPLPYHLPSILQAGDGPPQMRPYHTIIEIAEHKR 211 - 280 KGSLKVRKWRSIFNLGRSGHETKRKLPRGAEDREDKSNKGTLRPAKSMDSLSAAAGASDEPEGLVGPSSP 281 - 350 RPSPLLPESLENDSIEAAEGEQEPEAEALGGTNSEPGTPRAGRSAIRAGGSSRAERCAGVHISDPYNVNL 351 - 420 PLHITSILSVPPNIISNVSLARLTRGLECPALQHRPSPASGPGPGPGLGPGPPDEKLEASPASSPLADSG 421 - 490 PDDLAPALEDSLSQEVQDSFSFLEDSSSSEPEWVGAEDGEVAQAEAAGAAFSPGEDDPGMGYLEELLGVG 491 - 560 PQVEEFSVEPPLDDLSLDEAQFVLAPSCCSLDSAGPRPEVEEENGEEVFLSAYDDLSPLLGPKPPIWKGS 561 - 630 GSLEGEAAGCGRQALGQGGEEQACWEVGEDKQAEPGGRLDIREEAEGSPETKVEAGKASEDRGEAGGSQE 631 - 700 TKVRLREGSREETEAKEEKSKGQKKADSMEAKGVEEPGGDEYTDEKEKEIEREEDEQREEAQVEAGRDLE 701 - 770 QGAQEDQVAEEKWEVVQKQEAEGVREDEDKGQREKGYHEARKDQGDGEDSRSPEAATEGGAGEVSKERES 771 - 840 ...
Bosse, T., Ehinger, J., Czuchra, A., Benesch, S., Steffen, A., Wu, X., Schloen, K., Niemann, Hartmut, Scita, G., Stradal, T. E., Brakebusch, C., and Rottner, K. "Cdc42 and phosphoinositide 3-kinase drive Rac-mediated actin polymerization downstream of c-Met in distinct and common pathways". Mol Cell Biol 27.19 (2007): 6615-6628 ...
To further test the vector system, we designed both a synthetic siRNA and a pSUPER vector that target the same 19-nt sequence in theCDC20 transcript. As for CDH1, efficient suppression of endogenous CDC20 expression was achieved with both synthetic siRNA and with pSUPER-CDC20 (Fig. 2B). To measure the level of gene suppression accurately by the pSUPER system, we designed a construct to target polo like kinase-1 (PLK1). Introduction of pSUPER-PLK1 led to a significant decrease in PLK1 protein levels and a reduction in PLK1 kinase activity by a factor of 10 [Supplementary fig. 1A (4)]. To date, we were successful in knocking down the expression of more than 10 genes for which we designed a pSUPER siRNA vector, highlighting the efficiency with which genes can be targeted using this vector (6).. Next, we asked whether suppression of gene expression by the pSUPER vector is sufficient to affect cellular physiology. We designed a construct to knockdown p53, a transcription factor that is stabilized ...
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The biosensors developed in the authors laboratory have been based on different designs, each imparting specific strengths and weaknesses
The biosensors developed in the authors laboratory have been based on different designs, each imparting specific strengths and weaknesses
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Complete information for CDC37 gene (Protein Coding), Cell Division Cycle 37, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Mark D. Bass is the author of these articles in the Journal of Visualized Experiments: Induction of Adhesion-dependent Signals Using Low-intensity Ultrasound, Comparing the Affinity of GTPase-binding Proteins using Competition Assays
Homo sapiens CDC42 binding protein kinase alpha (DMPK-like) (CDC42BPA), transcript variant A, mRNA. (H00008476-R03) - Products - Abnova
The CDC gets it wrong again - the sun doesnt cause melanoma Last year, I reported on the incompetent way the Centers for Disease Control (CDC) handed the
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Cells depleted of Plk or cdc5-1 protein arrest at multiple points of M phase. (A) Growth of cdc5Δ mutant conditionally rescued by expressing either GAL1-HA-EGF
U.S. Centers for Disease Control and Prevention (CDC) has determined that sixty-five percent of those with cancer now survive five years or more after diagnosis.
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PAK inhibitors (inhibiting targets of signaling pathways) used for various assays, some have entered clinical trials, which would be new cancer therapies.
View mouse Arhgap24 Chr5:102481391-102897937 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
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The p21-activated kises (PAKs) are serine-threonine kises that bind to the active forms of Cdc42 and Rac. They are divided into two groups, the first…
The p21-activated kises (PAKs) are serine-threonine kises that bind to the active forms of Cdc42 and Rac. They are divided into two groups, the first…
Continuing a trend that emerged late last month, flu activity remains high across the United States but there are reports that the number of infections may be l
Plasmid pDONR223_RAC1_p.P29S from Dr. Jesse Boehms lab contains the insert RAC1 and is published in Cancer Discov. 2016 Jul;6(7):714-26. doi: 10.1158/2159-8290.CD-16-0160. Epub 2016 May 4. This plasmid is available through Addgene.
Plasmid pTriEX-Antenna-GDI Rac1 from Dr. Klaus Hahns lab contains the insert Rac1 and is published in Nat Chem Biol. 2016 Aug 8. doi: 10.1038/nchembio.2145. This plasmid is available through Addgene.
We purified native WASp (Wiskott-Aldrich Syndrome protein) from bovine thymus and studied its ability to stimulate actin nucleation by Arp2/3 complex. WASp alone is inactive in the presence or absence of 0.5 µM GTP-Cdc42. Phosphatidylinositol 4,5 bisphosphate (PIP2) micelles allowed WASp to activate actin nucleation by Arp2/3 complex, and this was further enhanced twofold by GTP-Cdc42. Filaments nucleated by Arp2/3 complex and WASp in the presence of PIP2 and Cdc42 concentrated around lipid micelles and vesicles, providing that Cdc42 was GTP-bound and prenylated. Thus, the high concentration of WASp in neutrophils (9 µM) is dependent on interactions with both acidic lipids and GTP-Cdc42 to activate actin nucleation by Arp2/3 complex. The results also suggest that membrane binding increases the local concentrations of Cdc42 and WASp, favoring their interaction ...
Ect2 is a guanine nucleotide exchange factor (GEF) and activator of Rho family small GTPases. Ect2 regulates RhoA, Rac1, and Cdc42, thereby playing an important role in the control of cell proliferation, survival, and migration. Originally identified as an oncogene in vitro, the role of Ect2 in regulating migration makes it of particular interest in ovarian cancer, in which local invasion and ascites are prevalent. Notably, ECT2 is located on 3q26.1-3q26.2, the most frequent amplicon in ovarian cancer, and it has been found to be overexpressed at the mRNA level in ovarian tumors. We first explored the role of Ect2 in ovarian cancer by knocking it down using shRNA and assessing anchorage-independent growth and both random and directed migration in a panel of ovarian cancer cell lines. Our findings reveal that Ect2 expression is required for each of these functions. Interestingly, we found that Ect2 utilization of specific Rho GTPase substrates is highly context-dependent. In addition, to ...
To generate the GAL1p-CDC42 allele, the oligonucleotides DJL42-1 (5′-GC CGGAACTCAAAAGGGTAATTTCGTGAAAAACAATCATCGACTACGT CGTAAGGCCG-3′ and DJL42-2 (5′-TCAGTAGAAGGATATGACAAGG G-3′) were used to amplify a DNA fragment containing the LEU2 gene, theGAL1 promoter, and flanking CDC42 sequences using PCR with the plasmid pGAL-CDC42Sc (55) as a template (the underlined sequence in DJL42-1 is the genomic sequence 733 to 693 bp upstream of the CDC42 start codon, whereas in DJL42-2 it is the reverse complement of nucleotides 204 to 226 in theCDC42 open reading frame). The PCR fragment was transformed into DLY1, replacing the endogenous CDC42 promoter (1 to 693 bp upstream of the start codon) with LEU2 and theGAL1 promoter, creating DLY3067. Leu+transformants were selected on galactose-containing plates, and promoter replacement was confirmed by the inability to grow on dextrose-containing plates (GAL1 promoter off) and by PCR.. To generate the cdc42::URA3 null allele, the oligonucleotides CDC42-5′ ...
Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8. The Rnd subfamily contains Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8. These novel Rho family proteins have substantial structural differences compared to other Rho members, including N- and C-terminal extensions relative to other Rhos. Rnd3/RhoE is farnesylated at the C-terminal prenylation site, unlike most other Rho proteins that are geranylgeranylated. In addition, Rnd members are unable to hydrolyze GTP and are resistant to GAP activity. They are believed to exist only in the GTP-bound conformation, and are antagonists of RhoA activity. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
β2 integrins of neutrophils play a critical role in innate immune defense, but they also participate in tissue destruction during autoimmune inflammation. p190RhoGAP (ArhGAP35), a regulator of Rho family small GTPases, is required for integrin signal transduction in fibroblasts. Prior studies have also suggested a role for p190RhoGAP in β2 integrin signaling in neutrophils. To directly test that possibility, we have generated a novel targeted mutation completely disrupting the p190RhoGAP-encoding gene in mice. p190RhoGAP deficiency led to perinatal lethality and defective neural development, precluding the analysis of neutrophil functions in adult p190RhoGAP−/− animals. This was overcome by transplantation of fetal liver cells from p190RhoGAP−/− fetuses into lethally irradiated wild-type recipients. Neutrophils from such p190RhoGAP−/− bone marrow chimeras developed normally and expressed normal levels of various cell surface receptors. Although p190RhoGAP−/− neutrophils showed ...
Although it is well understood that Rho GTPase activity is regulated by GEFs, very little is known about the specific role GEFs play in regulating cellular processes, such as migration. Our results show that Asef2 coordinately regulates the activities of Rho family members to promote cell migration by stimulating the rapid turnover of adhesions. Asef2 signaling leads to an overall decrease in the amount of active RhoA, which is crucial for the effect of Asef2 on migration. RhoA induces the formation of stress fibers and can promote the maturation of nascent cell-matrix contacts into large, focal adhesions (Chrzanowska-Wodnicka and Burridge, 1996; Ridley and Hall, 1992; Rottner et al., 1999). Thus, the loss of RhoA activity in GFP-Asef2 stable cells could inhibit the maturation of nascent adhesions and contribute to the more rapid turnover of these structures. These described activities of Rho would be expected to inhibit migration. Indeed, in some cell types, high levels of Rho have been shown ...
Rho GTPases are molecular switches that regulate many aspects of cell physiology. A number of Rho GTPases are essential for the formation of new vessels from pre-existing ones, a process known as angiogenesis. RhoJ/TCL belongs to the Cdc42 subfamily of Rho GTPases. Previous bioinformatic and primary cell line analyses identified RhoJ as being highly expressed in endothelial cells. The aim of this project was to investigate the expression pattern and endothelial function of RhoJ, particularly in the processes necessary for angiogenesis. Silencing RhoJ with siRNA impaired tube formation and migration. On the cellular level, RhoJ knockdown increased focal adhesions, actin stress fibres and collagen gel contraction, suggesting increased actomyosin contractility. Pharmacological inhibition of ROCK and myosin II, two regulators of actomyosin contractility, restored motility and tube formation after RhoJ knockdown. RhoJ localised to blood vessels of developing mice and in various human normal and ...
... is a member of the CDC25 family of phosphatases. CDC25A is required for progression from G1 to the S phase of the cell cycle. It activates the cyclin-dependent kinase CDC2 by removing two phosphate groups. CDC25A is specifically degraded in response to DNA damage, which prevents cells with chromosomal abnormalities from progressing through cell division. CDC25A is an oncogene, although its exact role in oncogenesis has not been demonstrated. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008 ...
Lymphocytes depend on external signals from cytokines for survival and proliferation. Here we have examined the mechanisms by which IL-3 and IL-7 induce proliferation of lymphoid cell lines and primary lymphocytes and find that this pathway differs from that of better-studied factors that induce growth of mesenchymal cells. Rather than inducing synthesis of cyclins, these cytokines appear to protect lymphocytes from a stress response. Withdrawal of IL-3 or IL-7 induced cell cycle arrest through activation of a stress kinase, p38 MAPK, which occurred in the first few hours after cytokine withdrawal. p38 MAPK then directly phosphorylated the phosphatase Cdc25A at S75 and S123, targeting the phosphatase for degradation. Because Cdc25A is required to remove an inhibitory phosphate (Y15) from Cdk2, the latter kinase was inactive, failed to phosphorylate Rb and the cells arrested at the G1-S boundary. We show that inhibiting either component of this pathway, blocking p38 MAPK activity or expressing a ...
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Rho GTPases are a family of molecular switches that critically mediate many cellular processes such as proliferation, survival, and death. The most well described members of the Rho GTPase family are RhoA, Rac1, and Cdc42 which are each known to regulate actin cytoskeletal dynamics. Thus, it is not surprising that Rho GTPases play a crucial function in neuronal growth cone dynamics and dendritic spine morphogenesis. Specifically, Rac1 and Cdc42 generally induce neurite outgrowth and dendritic spine morphogenesis, while RhoA typically stimulates neurite retraction. In addition to regulating neuronal cytoskeletal dynamics, previous work has demonstrated a critical function for Rho GTPase family members in neuronal development and survival. Indeed, dysregulation of Rho GTPase family members has been implicated in several disorders of the central nervous system including, Down Syndrome, Fragile X Mental Retardation Syndrome, Amyotrophic Lateral Sclerosis, amongst many others. In addition to typical Rho
Myr 3, a member of the myosin-I family from rat, is shown in this study to be localized at adherens-type intercellular junctions in epithelial and nonepithelial tissues. Formation of intercellular junctions and the accompanying recruitment of myr 3 to these junctions involves signaling by the Rho subfamily of small GTP-binding proteins. This conclusion is based on studies with HtTA-1 HeLa cells that were induced by overexpression of constitutively active Cdc42Hs to form typical adherens-type intercellular junctions enriched in cadherins (N-cadherin), beta-catenin, filamentous actin and myr 3. Recruitement of myr 3 to Cdc42-induced adherens junctions in HeLa cells was dependent on a short region of the tail domain and a functional myosin motor domain, but was independent of its myosin-I tail homology and SH3 regions. Overexpression of constitutively active Rac1 induced a distinct type of adherens junction in HeLa cells that was characterized by elaborate intercellular interdigitations enriched in ...
Aarskog affection is an affiliated disease. The Aarskog Scott affection is a ataxia with abrupt height, hypertelorism, downslanting palpebral fissures, anteverted nostrils, multilateral laxity, capote scrotum, and cerebral retardation. The concrete phenotype varies with age and postpuberal males may get artlessly bush balance manifestations of the prepuberal phenotype. It is a X-linked backward ancestral disorder, thus, mainly males are affected, although females may get a milder announcement of some of the features. The Aarskog affection is too accepted as the Aarskog Scott syndrome, faciodigitogenital syndrome, capote scrotum affection and faciogenital dysplasia. It is acquired by mutations in a gene alleged "faciogenital dysplasia" authorize on the X chromosome.. A accident agency is article that increases your adventitious of accepting a ache or condition. This ataxia mainly affects males. Aarskog affection cannot be convalescent but there may be surgical procedures and physiotherapy ...
TY - JOUR. T1 - DLC1 negatively regulates angiogenesis in a paracrine fashion. AU - Shih, Yi Ping. AU - Liao, Yi Chun. AU - Lin, Yuan. AU - Lo, Su Hao. PY - 2010/11/1. Y1 - 2010/11/1. N2 - The Rho GTPase-activating protein DLC1 is a tumor suppressor that is often deleted in liver cancer and downregulated in other cancers. DLC1 regulates the actin cytoskeleton, cell shape, adhesion, migration, and proliferation through its Rho GTPase-activating protein activity and focal adhesion localization. In this study, we silenced DLC1 in nonmalignant prostate epithelial cells to explore its tumor suppression functions. Small hairpin RNA-mediated silencing of DLC1 was insufficient to promote more aggressive phenotypes associated with tumor cell growth. In contrast, DLC1 silencing promoted pro-angiogenic responses through vascular endothelial growth factor (VEGF) upregulation, accompanied by the accumulation of hypoxia-inducible factor 1α and its nuclear localization. Notably, modulation of VEGF expression ...
The cellular functions of Dock6 and Dock8 are largely unknown. Dock6 is reported to exhibit dual guanine nucleotide exchange specificity towards the small GTPases Rac1 and Cdc42. Mutations in the DOCK6 gene are associated with Adams-Oliver syndrome 2, a rare congenital disorder characterized by defects of the scalp, cranium, and limbs, and mottling of the skin. Mutations in the DOCK8 gene have been reported in a human lung cancer cell line, and Dock8 deficiency is associated with a variant of combined immunodeficiency, known as Hyperimmunoglobulin E syndrome (HIES). Dock6 alternative names include dedicator of cytokinesis protein 6, AOS2, ZIR1, and KIAA1395. Dock8 alternative names include dedicator of cytokinesis protein 8, ZIR8, MRD2, FLJ00026, FLJ00152, FLJ00346, and 1200017A24Rik.. Dock7 expression has been reported in neurons and in HEK 293 cells. It binds the small GTPases Rac1 and Rac3, but does not bind Cdc42. Dock7 is required for proliferation and differentiation of neurocytes and ...
A. Growth cone motility and neurite branch formation are activated (+) by Rac1 and Cdc42 and negatively regulated (-) by RhoA. Reelin participates in the regulation of growth cone motility and branching by regulating Rho GTPase activity (B). Filopodia formation and the formation of neuronal transport vesicles, both known to be mediated by Cdc42, are triggered by Reelin. B. Binding of the extracellular matrix protein Reelin to its transmembrane receptors Apoer2 and Vldlr triggers Dab1 tyrosine phosphorylation by Src-family-kinases (SFK). This leads to the activation of several downstream signals, including phosphatidylinositol-3-kinase (PI3K), which activates Cdc42 via an unknown intermediate effector. There is evidence that Reelin also might locally activate Rac1. N-WASP and WAVE link Cdc42 and Rac1 activity to changes of the actin cytoskeleton, leading to increased growth cone motility, filopodia and vesicle formation, and dendritic branching (A). Cdc42 and Rac1 also contribute to activation of ...
Hsieh CL, Swaroop A, Francke U (1990). "Chromosomal localization and cDNA sequence of human ralB, a GTP binding protein". Somat ... RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity". J. Biol. Chem. 270 (38): 22473-7. doi:10.1074/jbc. ... "Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of ... Jilkina O, Bhullar RP (1997). "Generation of antibodies specific for the RalA and RalB GTP-binding proteins and determination ...
"The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42". Proceedings of the National ... Actin-related protein 3 is a protein that in humans is encoded by the ACTR3 gene. The specific function of this gene has not ... Winter D, Podtelejnikov AV, Mann M, Li R (Jul 1997). "The complex containing actin-related proteins Arp2 and Arp3 is required ... Higgs HN, Blanchoin L, Pollard TD (Nov 1999). "Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the ...
Hoffman GR, Nassar N, Cerione RA (2000). "Structure of the Rho family GTP-binding protein Cdc42 in complex with the ... "Mapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1". Structure. 8 (1): 47-55. doi:10.1016/ ... "Mapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1". Structure. 8 (1): 47-55. doi:10.1016/ ... Li X, Bu X, Lu B, Avraham H, Flavell RA, Lim B (February 2002). "The hematopoiesis-specific GTP-binding protein RhoH is GTPase ...
... a transcriptionally inducible adapter protein that binds GTP-Cdc42 and activates SAPK/JNK. A potential marker transcript for ... ERBB receptor feedback inhibitor 1 is a protein that in humans is encoded by the ERRFI1 gene. MIG6 is a Cytoplasmic protein ... 2002). "A novel mechanism of nuclear factor kappaB activation through the binding between inhibitor of nuclear factor- ... a mitogen-induced signal transducer which binds to the ErbB-2 kinase domain". Mol Cell Biol. 20 (20): 7735-7750. doi:10.1128/ ...
... and CDC42 (MIM 116952). GTPase-activating proteins (GAPs) bind activated forms of Rho GTPases and stimulate GTP hydrolysis. ... a new human GTPase-activating protein for Rac and Cdc42 similar to Drosophila rotundRacGAP gene product, is expressed in male ... Rac GTPase-activating protein 1 is an enzyme that in humans is encoded by the RACGAP1 gene. Rho GTPases control a variety of ... Tapon N, Nagata K, Lamarche N, Hall A (March 1998). "A new rac target POSH is an SH3-containing scaffold protein involved in ...
They serve as targets for the small GTP binding proteins Cdc42 and Rac and have been implicated in a wide range of biological ... PAK4 interacts specifically with the GTP-bound form of Cdc42Hs and weakly activates the JNK family of MAP kinases. PAK4 is a ... PAK proteins, a family of serine/threonine p21-activating kinases, include PAK1, PAK2, PAK3 and PAK4. PAK proteins are critical ... Serine/threonine-protein kinase PAK 4 is an enzyme that in humans is encoded by the PAK4 gene. PAK4 is one of six members of ...
They serve as targets for the small GTP binding proteins CDC42 and Rac and have been implicated in a wide range of biological ... PAK1 p21/Cdc42/Rac1-activated kinase 1 (STE20 homolog, yeast)". "Entrez Gene: PAK2 p21 (CDKN1A)-activated kinase 2". "Entrez ...
These proteins serve as targets for the small GTP binding proteins Cdc42 and Rac and have been implicated in a wide range of ... 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". ... Manser E, Leung T, Salihuddin H, Zhao ZS, Lim L (January 1994). "A brain serine/threonine protein kinase activated by Cdc42 and ...
... and Cdc42 regulate their activity by alternating between an active GTP-bound state, and an inactive GDP-bound state. Guanine ... Just I, Selzer J, von Eichel-Streiber C, Aktories K (March 1995). "The low molecular mass GTP-binding protein Rho is affected ... In Rac and Cdc42, the sugar moiety is transferred to the Thr-35. The glucosylation prevents proper binding of GTP and blocks ... TcdA acts preferentially on the GDP-bound form of the GTPase proteins since this configuration exposes the threonine residue ...
The example of substrate includes H-Ras, N-ras, R-Ras, RhoB, Cdc42 inform 2, Rab10, Galpha subunit of trimeric GTP binding ... The protein polymitoylation is a reversible process. The addition of palmitoyl group increase the membrane association of the ... Palmitoyl acyltransferase is a group of enzymes that transfer palmityl group to -SH group on cysteine on a protein. This ... The catalytic domain of the protein has aspartate-histidine-histidine-cystein (DHHC) in the core and therefore is called DHHC ...
The PAK proteins are a family of serine/threonine kinases that serve as targets for the small GTP binding proteins, CDC42 and ... The PAK proteins are a family of serine/threonine kinases that serve as targets for the small GTP binding proteins, CDC42 and ... Serine/threonine-protein kinase PAK 2 is an enzyme that in humans is encoded by the PAK2 gene. PAK2 is one of three members of ... The protein encoded by this gene is activated by proteolytic cleavage during caspase-mediated apoptosis, and may play a role in ...
Instead, it binds the active (GTP-bound) forms of RAC1 and CDC42 with higher affinity than GDP-bound forms, and stabilizes the ... Bashour AM, Fullerton AT, Hart MJ, Bloom GS (1997). "IQGAP1, a Rac- and Cdc42-binding protein, directly binds and cross-links ... This domain binds calmodulin, a protein known as a calcium sensor that can bind and regulate many target proteins. A GRD ( ... which mediates actin-binding and binds calponin. The WW, or poly-proline protein-protein domain, so named because of two ...
... GTP-Binding Protein at the US National Library of Medicine Medical Subject Headings (MeSH) CDC42 Info with links in the ... "CDC42 (cell division cycle 42 (GTP binding protein, 25kDa))". atlasgeneticsoncology.org. Retrieved 2016-04-22. Stengel K, Zheng ... Cdc42 cycles between an active GTP-bound state and an inactive GDP-bound state. This process is regulated by guanine nucleotide ... a transcriptionally inducible adapter protein that binds GTP-Cdc42 and activates SAPK/JNK. A potential marker transcript for ...
... like many other small G-protein associating domains) and selectively binds GTP-bound Ras proteins only. (You can see this ... upon tyrosine phosphorylation by the Cdc42-regulated kinase ACK1". J. Biol. Chem. 275 (38): 29788-93. doi:10.1074/jbc. ... "The small GTP-binding protein, Rhes, regulates signal transduction from G protein-coupled receptors". Oncogene. 23 (2): 559-68 ... most importantly GTP-bound Ras. Activated small G-proteins can thus break up the intramolacular interactions: this results in a ...
TIAM1 modulates the activity of Rho GTP-binding proteins and connects extracellular signals to cytoskeletal activities. In ... Wennerberg K, Ellerbroek SM, Liu RY, Karnoub AE, Burridge K, Der CJ (Dec 2002). "RhoG signals in parallel with Rac1 and Cdc42 ... UMich Orientation of Proteins in Membranes protein/pdbid-1foe - Calculated spatial position of TIAM1-RAC2 complex in membrane. ... T-cell lymphoma invasion and metastasis-inducing protein 1 is a protein that in humans is encoded by the TIAM1 gene. TIAM1 is ...
Septins are a group of the highly conserved GTP binding proteins found in eukaryotes. Different septins form protein complexes ... Rac for lamellipodia and Cdc42 for filopodia. Functions include: Muscle contraction Cell movement Intracellular transport/ ... Actin structures are controlled by the Rho family of small GTP-binding proteins such as Rho itself for contractile acto-myosin ... The same holds true for the actin-like proteins and their structure and ATP binding domain. Cytoskeletal proteins are usually ...
The GTP-binding protein Rac is the regulator of this membrane ruffling. Changes in the Polyphosphoinositide metabolism and ... Rac1 and cdc42. Some bacteria such as enteropathogenic E. coli and enterohemorrhagic E. coli can induce membrane ruffling by ... A number of actin-binding and organizing proteins localize to membrane ruffles and potentially target to transducing molecules ...
This protein has been shown to bind both CDC42 and TC10 GTPases in a GTP-dependent manner. When overexpressed in fibroblasts, ... "Entrez Gene: CDC42EP4 CDC42 effector protein (Rho GTPase binding) 4". Human CDC42EP4 genome location and CDC42EP4 gene details ... The product of this gene is a member of the CDC42-binding protein family. Members of this family interact with Rho family ... Cdc42 effector protein 4 is a protein that in humans is encoded by the CDC42EP4 gene. ...
Wang KL, Roufogalis BD (May 1999). "Ca2+/calmodulin stimulates GTP binding to the ras-related protein ral-A". The Journal of ... RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity". The Journal of Biological Chemistry. 270 (38): 22473 ... "Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of ... "Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of ...
... functions to enhance the GTPase activity of the Rho-GTPase proteins RhoA and Cdc42, promoting the hydrolysis of their bound GTP ... its ability to enhance activated GTP-bound Rho-GTPases' (specifically, RhoA and Cdc42) intrinsic ability to convert their GTP ... Constitutive activation of Cdc42 due to the absence of RhoGAP proteins such as DLC1 will contribute to the continual repetition ... Deleted in Liver Cancer 1 also known as DLC1 and StAR-related lipid transfer protein 12 (STARD12) is a protein which in humans ...
... is a GTPase activating protein specific for RAC GTP-binding proteins. It is expressed primarily in the brain and may ... CHN1 is transferred to the plasma membrane and negatively regulates Rho-family small GTPases RAC1 and CDC42, thus causing the ... Buttery P, Beg AA, Chih B, Broder A, Mason CA, Scheiffele P (February 2006). "The diacylglycerol-binding protein α1-chimaerin ... the C-terminal RhoGAP domain and the central C1 domain similar to protein kinase C. When lipid diacylglycerol (DAG) binds to ...
The cooperative binding of CDC42 and PIP2 is thermodynamically favored; binding of one enhances binding of the other. CDC42 and ... WASp and N-WASP are analogs, they contain an N-terminal EVH1 domain, a C-terminal VCA domain and central B and GBD (GTP binding ... "Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules". The Journal of ... "Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the ...
... this link is broken when GTP-bound Rho binds to the GBD and activates the protein. The addition of the DAD to mammalian cells ... Mammalian Drf3 contains a CRIB-like motif within its GBD for binding to Cdc42, which is required for Cdc42 to activate and ... including the actin-binding protein profilin, SH3 (Src homology 3) domain proteins, and WW domain proteins. The actin ... The FH2 domain is required for the self-association of formin proteins through the ability of FH2 domains to directly bind each ...
... interacting only with the GTP bound forms of rho and rac 1. Displaying a distinctive protein organization, this protein defines ... myotonic dystrophy protein kinase (MDPK) and the CDC42 effector known as MRCK or GEK. Citron kinase, which resembles the ROCK ... This GTPase cycles between an inactive GDP-bound form and an active GTP-bound form, and this RhoA flux seems important for ... Madaule P, Furuyashiki T, Reid T, Ishizaki T, Watanabe G, Morii N, Narumiya S (Dec 1995). "A novel partner for the GTP-bound ...
... small GTP-binding proteins of the ras superfamily, that are involved in vesicular trafficking of molecules between cellular ... GDI1 has been shown to interact with CDC42. GRCh38: Ensembl release 89: ENSG00000203879 - Ensembl, May 2017 GRCm38: Ensembl ... "Molecular cloning and characterization of a novel type of regulatory protein (GDI) for smg p25A, a ras p21-like GTP-binding ... GDIs slow the rate of dissociation of GDP from rab proteins and release GDP from membrane-bound rabs. GDI1 is expressed ...
... belongs to a family of Rho-like GTPases that act as molecular switches by cycling from the active GTP-bound state to ... the inactive GDP-bound state. These proteins are key regulators of the actin cytoskeleton and are involved in cell signaling.[ ... "Entrez Gene: ARHGEF9 Cdc42 guanine nucleotide exchange factor (GEF) 9". Kins S, Betz H, Kirsch J (2000). "Collybistin, a newly ... "Identification of a gephyrin-binding motif in the GDP/GTP exchange factor collybistin". Biol. Chem. 382 (10): 1455-62. doi: ...
The cooperative binding of CDC42 and PIP2 is thermodynamically favored; binding of one enhances binding of the other.[9] CDC42 ... WASp and N-WASP are analogs, they contain an N-terminal EVH1 domain, a C-terminal VCA domain and central B and GBD (GTP binding ... SH3 domain binding. • protein binding. • identical protein binding. • actin binding. • protein kinase binding. • small GTPase ... "Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules". The Journal of ...
A typical G-protein is active when bound to GTP and inactive when bound to GDP (i.e. when the GTP is hydrolyzed to GDP). The ... the human homolog of the yeast cell cycle gene CDC42". Mol Cell Biol. 10 (11): 5977-82. ISSN 0270-7306. PMC 361395 . PMID ... GTP-binding protein regulators Wennerberg K, Rossman KL, Der CJ (March 2005). "The Ras superfamily at a glance". J. Cell Sci. ... Therefore, a G-protein can be switched on and off. GTP hydrolysis is accelerated by GTPase activating proteins (GAPs), while ...
... binding proteins between their GDP‐bound and GTPbound states (Boguski and McCormick, 1993). Rho family proteins, such as Cdc42 ... bound Cdc42 or Rac and the Cool‐2 monomer. The βγ subunit complex of large GTPbinding proteins, by interacting with PAK, ... 1 has been shown to bind preferentially to activated (GTPbound) Cdc42 and to act as a target/scaffold protein in mediating the ... 2 acting as a GEF for Cdc42 and/or Rac, as the GTPbound forms of these proteins stimulate PAK activity (Manser et al, 1994; ...
... we have found that these processes are regulated by the Rho family GTPase Cdc42. We show that GDP- but not GTP-bound Cdc42 ... These results provide the first evidence for the involvement of a Rho family G protein in the control of the activity of a Ras ... We also demonstrate that catalyzing GDP/GTP exchange on Cdc42 facilitates Ras-GRF-induced MAPK activation. Moreover, we show ... The Rho family GTPase Cdc42 regulates the activation of Ras/MAP kinase by the exchange factor Ras-GRF. ...
GTP-binding proteins then were added. To avoid light scattering from the beads, GTP-binding proteins used here were eluted by ... Extracts were stimulated by Cdc42-GTPγS (25 nM), Cdc42-GDPβS (25 nM), and Rho-GTPγS (50 nM) (left) or by Cdc42-GTPγS at ... Actin polymerization also depends on the nucleotide bound to Cdc42: GTPγS-charged Cdc42 was active, but GDPβS-charged Cdc42 was ... The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42. Le Ma, Rajat Rohatgi, and Marc ...
The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway.. Coso OA1, Chiariello M ... GTP-Binding Proteins. *cdc42 GTP-Binding Protein, Saccharomyces cerevisiae. *rac GTP-Binding Proteins ... Taken together, these findings strongly support a critical role for Rac1 and Cdc42 in controlling the JNK signaling pathway. ... c-Jun amino-terminal kinases (JNKs) and mitogen-activated protein kinases (MAPKs) are closely related; however, they are ...
Functional analysis of the interaction between the small GTP binding protein Cdc42 and the Ste20 protein kinase in yeast.. ... but it has been demonstrated recently that binding of the small GTP binding protein Cdc42 is able to activate Ste20 in vitro. ... In contrast, a Ste20 mutant protein unable to bind Cdc42 was found diffusely throughout the cytoplasm, suggesting that Cdc42 is ... suggesting that binding of Cdc42 and Ste20 was not required to activate Ste20. Wild-type Ste20 protein was visualized as a ...
GTP binding protein, 25kDa)), Authors: Fátima Valdés-Mora, Teresa Gómez del Pulgar, Juan Carlos Lacal. Published in: Atlas ... BCL7A--CDC42 BTD--CDC42 C11ORF96--CDC42 CDC42--ABCF2 CDC42--ACK CDC42--CAPZB CDC42--CELA3A CDC42--CELA3B CDC42--CLEC2D CDC42-- ... CDC42 PRDM16--CDC42 RABEP1--CDC42 RAC--CDC42 RAC1--CDC42 RNF38--CDC42 STAU2--CDC42 TAOK1--CDC42 TC10--CDC42 TFRC--CDC42 USP48-- ... CDC42 GRHL2--CDC42 GRHL3--CDC42 HNRNPC--CDC42 IL1R2--CDC42 KDM1A--CDC42 KIF1B--CDC42 KLHL21--CDC42 LGALS3--CDC42 LRRC47--CDC42 ...
... "cdc42 GTP-Binding Protein" by people in this website by year, and whether "cdc42 GTP-Binding Protein" was a major or minor ... cdc42 GTP-Binding Protein*cdc42 GTP-Binding Protein. *GTP-Binding Protein, cdc42 ... G25K GTP-Binding Protein, Placental Isoform*G25K GTP-Binding Protein, Placental Isoform ... "cdc42 GTP-Binding Protein" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ...
G proteins. GTP-binding proteins, GDI, guanine-nucleotide dissociation inhibitor. GEF. guanine-nucleotide exchange factor. NBD ... GTPγS is an agonist with a broad spectrum and can activate any GTP-binding proteins in the extracts. To determine whether the ... Corequirement of Specific Phosphoinositides and Small GTP-binding Protein Cdc42 in Inducing Actin Assembly in Xenopus Egg ... Corequirement of Specific Phosphoinositides and Small GTP-binding Protein Cdc42 in Inducing Actin Assembly in Xenopus Egg ...
Atypical Protein Kinases Cλ and -ζ Associate with the GTP-Binding Protein Cdc42 and Mediate Stress Fiber Loss. Matthew P. ... GST-Cdc42 associates with aPKC in rat brain cytosol.GST fusions of the Rho family GTP-binding proteins RhoA, Rac1, and Cdc42 ... V12 Cdc42 bound well to aPKCs, wild-type Cdc42 bound less well, and little binding was detected with N17 Cdc42. The V12/T35A ... Atypical Protein Kinases Cλ and -ζ Associate with the GTP-Binding Protein Cdc42 and Mediate Stress Fiber Loss ...
Activation of Other Small G Proteins by Ang II. Cdc42 Activation by Ang II. Cdc42 regulates formation of filopodia in the ... Small GTP-binding proteins (G proteins) are monomeric G proteins with a low molecular weight of 20 to 40 kDa. A small G protein ... Also, eIF4E is released from eIF4E binding protein/PHAS-I on phosphorylation of eIF4E binding protein/PHAS-I regulated through ... Angiotensin II Signal Transduction Through Small GTP-Binding Proteins. Haruhiko Ohtsu, Hiroyuki Suzuki, Hidekatsu Nakashima, ...
... detectable GTPase activity but its high intrinsic guanine nucleotide exchange activity suggests it is constitutively GTP-bound ... Cdc42 protein signal transduction Source: GO_CentralInferred from biological aspect of ancestori*21873635 ... GTP-binding, Magnesium, Metal-binding, Nucleotide-binding. Enzyme and pathway databases. Reactome - a knowledgebase of ... Rho-related GTP-binding protein RhoUAdd BLAST. 258. Amino acid modifications. Feature key. Position(s). DescriptionActions. ...
protein binding. • thioesterase binding. • protein kinase binding. • nucleotide binding. • GTP binding. • identical protein ... "Protein Data Bank in Europe. EMBL-EBI. Retrieved 2016-04-22.. *^ "CDC42 (cell division cycle 42 (GTP binding protein, 25kDa))" ... Wikimedia Commons has media related to CDC42.. *cdc42+GTP-Binding+Protein at the US National Library of Medicine Medical ... ubiquitin protein ligase activity. • apolipoprotein A-I receptor binding. • GTP-dependent protein binding. • GTPase activity. • ...
... cdc42 GTP-Binding Proteincdc42 GTP-Binding Protein, Saccharomyces cerevisiae • Cell Membrane Permeability • Cell Polarity • ... Protein BindingProtein Isoforms • Protein Transport • Quail • Rats • Rats, Inbred SHR • Rats, Wistar • Renal Circulation • ... Saccharomyces cerevisiae • Saccharomyces cerevisiae Proteins • Septins • Signal Transduction • SNARE Proteins • Sodium • Sodium ... Membrane Transport Proteins • Mice • Microvessels • Models, Animal • Models, Biological • Models, Statistical • Models, ...
... cdc42 GTP-Binding Proteincdc42 GTP-Binding Protein, Saccharomyces cerevisiae • Cell Membrane Permeability • Cell Polarity • ... Protein BindingProtein Isoforms • Protein Transport • Quail • Rats • Rats, Inbred SHR • Rats, Wistar • Renal Circulation • ... Saccharomyces cerevisiae • Saccharomyces cerevisiae Proteins • Septins • Signal Transduction • SNARE Proteins • Sodium • Sodium ... Membrane Transport Proteins • Mice • Microvessels • Models, Animal • Models, Biological • Models, Statistical • Models, ...
Purchase G Protein Pathways, Part C: Effector Mechanisms, Volume 345 - 1st Edition. Print Book & E-Book. ISBN 9780121822460, ... Section VI: Small GTP-Binding Proteins: Assay of Cdc42, Rac, and Rho GTPase Activation by Affinity Methods. Assays of ADP- ... Regulation of Mitogen-Activated Protein Kinases by G-Protein-Coupled Receptors. Analysis of Protein Kinase B/Akt. Direct ... Overexpression of Tightly Regulated Proteins: Protein Phosphatase 2A Overexpression in NIH 3T3 Cells. Monitoring G-Protein- ...
Nucleotide binding to the G12V-mutant of Cdc42 investigated by X-ray diffraction and fluorescence spectroscopy: two different ... G25K GTP-BINDING PROTEIN protein, length: 191 (BLAST) Sequence Similarity Cutoff. Rank. Chains in Cluster. Cluster ID / Name. ... Structures of protein chains with identical sequences (sequence identity > 95%) are aligned, superimposed and clustered. ... This allows for the easy identification of regions and types of structural flexibility present in a protein of interest. ...
cdc42 GTP-Binding Protein / metabolism* Substances * Fungal Proteins * cdc42 GTP-Binding Protein ... We demonstrate that the nucleotide cycling of Cdc42 converts cellular energy into a stable cluster of activated Cdc42. This ... Dynamics of Cdc42 Network Embodies a Turing-type Mechanism of Yeast Cell Polarity FEBS Lett. 2008 Apr 30;582(10):1437-43. doi: ... The roles of the prototypical activator and substrate are played by GTPase Cdc42 in its active and inactive states, ...
Cdc42 Gtp-binding Protein, Saccharomyces Cerevisiae. A member of the Rho family of MONOMERIC GTP-BINDING PROTEINS from ... Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the ... Silent Information Regulator Proteins, Saccharomyces Cerevisiae. A set of nuclear proteins in SACCHAROMYCES CEREVISIAE that are ... Enzymes are proteins that catalyze (i.e., increase the rates of) chemical reactions. In enzymatic reactions, the molecules at ...
Cdc42 antibody validated for WB. Referenced in 1 publication. Immunogen corresponding to synthetic peptide ... Ras like protein TC25 antibody. *Small GTP binding protein Cdc42 antibody. *TC25 antibody ... Cdc42/Rac is an important upstream regulator of the protein kinase cascade that controls the SAPK/JNK and p38 activity. Recent ... ab18758 detects recombinant human Rac and cdc42 proteins (Rho subfamily), and does not cross-react with members of the Ras or ...
FRZB (Frizzled-Related Protein): FRZB antibodies FRZB ELISA Kits FRZB Proteins IGFBP4 (Insulin-Like Growth Factor Binding ... This protein is highly similar to Saccharomyces cerevisiae Cdc 42, and is able to complement the yeast cdc42-1 mutant. The ... Protein 4): IGFBP4 antibodies IGFBP4 ELISA Kits IGFBP4 Proteins IGFBP5 (Insulin-Like Growth Factor Binding Protein 5): IGFBP5 ... IGFBP6 (Insulin-Like Growth Factor Binding Protein 6): IGFBP6 antibodies IGFBP6 ELISA Kits IGFBP6 Proteins ...
This protein is highly similar to Saccharomyces cerevisiae Cdc 42, and is able to complement the yeast cdc42-1 mutant. The ... FRZB (Frizzled-Related Protein): FRZB Antikörper FRZB ELISA Kits FRZB Proteine IGFBP4 (Insulin-Like Growth Factor Binding ... The protein encoded by this gene is a receptor protein tyrosine kinase and type I transmembrane protein that belongs to the ROR ... This protein also acts as a co-receptor with Frizzled protein family members for transducing signals by Wnt proteins and was ...
0 (Cadherins); 0 (beta Catenin); EC 3.6.5.2 (cdc42 GTP-Binding Protein). ... Prote na cdc42 de Liga o ao GTP/metabolismo. [Mh] Termos MeSH secund rio:. Animais. Caderinas/metabolismo. Ades o Celular. ... 0 (Membrane Proteins); 0 (PGRMC1 protein, mouse); 0 (PGRMC2 protein, mouse); 0 (Receptors, Progesterone). ... Trp-Asp (WD) repeat domain 1 (WDR1) is a highly conserved actin-binding protein across all eukaryotes and is involved in ...
Ack1 was identified as a 120-kDa protein that interacts with activated GTP-bound Cdc42. Structural studies have revealed sites ... ligand binding, nuclear translocation, DNA binding, and protein-protein interactions). The amino-terminal 485 amino acids of AR ... Subsequently, Ack1 binds and phosphorylates AR protein. The AR-Ack1 complex translocates to the nucleus and binds to the AREs ... TAD, transactivation domain; DBD, DNA-binding domain; LBD, ligand-binding domain. (D) Purified GST-AR and GST-cAR proteins were ...
The role of GTP-Binding Proteins in Endothelial Signaling. The effect of TNF on rac and Cdc42 on cell-cell adhesion and ... The effects of junctional protein phosphorylation on endothelial signaling and dysfunction.. *Robert Wood Johnson Minority ... Novel Roles for Junctional Proteins. Vascular endothelial cadherin and vascular endothelial growth factor signaling ...
EC 3.6.5.2/cdc42 GTP-Binding Protein, Saccharomyces cerevisiae From MEDLINE®/PubMed®, a database of the U.S. National Library ...
  • To separate activation of Pak1 by Cdc42 versus activation by Rac, we devised a genetic screen in yeast that enabled us to create and identify Pak1 mutants that selectively couple to Cdc42 but not Rac1. (fccc.edu)
  • Pak1 mutants that associate with Cdc42 but not Rac1 were also activated by Cdc42 but not Rac1. (fccc.edu)
  • In rat 3Y1 cells expressing oncogenic Ha-Ras, the Pak1 mutants defective in Rac1 binding are not activated, suggesting that Ras signals through a GTPase other than Cdc42 to activate Pakl. (fccc.edu)
  • RNA interference for AKAP350 also induced an increase in cdc42 activity during microtubule regrowth. (vanderbilt.edu)
  • Redox sensors and redox signalling A redox sensor is a redox sensitive specialized protein, that may be in a position to sense intracellular ranges of ROS by a redox primarily based mechanism affecting one particular or far more residues/ domains within its 3 dimensional framework, then transforming the redox change right into a particular signal in a position to positively influence signalling pathways and transcription of redox delicate genes. (interleukin-receptor.com)
  • However, Pak1 mutants that are unable to bind Rac are nonetheless well activated by calf serum, implying that this stimulus may induce Pak activation independent of Rac. (fccc.edu)
  • Enzyme activities, mRNA and protein expression, and respiration rates were measured. (courtfield.tk)