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Vav (protein)
Vav is a family of proteins involved in cell signalling. They act as guanine nucleotide exchange factors (GEFs) for small G proteins of the Rho family. GEF activity is mediated via module of tandem DH- PH domains. Vav proteins also appear to exhibit GEF-independent functions. Although it was originally thought that Vav proteins would only be present in multicellular organisms, Vav family proteins have been observed in Choanoflagellates. Function Some functions of the Vav protein are important for the immune system. Specifically the ability of Vav to change the cytoskeletal structure of lymphocytes, which is particularly used to "aim" cytokines towards bound pathogens or cells. In humans there are three Vav proteins: *Vav1 *Vav2 *Vav3 Guanine nucleotide exchange factor VAV3 is a protein that in humans is encoded by the ''VAV3'' gene. This gene is a member of the VAV gene family. The Vav (protein), VAV proteins are guanine nucleotide exchange factors (GEFs) for Rho family GTPas ...
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Proteins
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues ...
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Cell Signalling
In biology, cell signaling (cell signalling in British English) or cell communication is the ability of a cell to receive, process, and transmit signals with its environment and with itself. Cell signaling is a fundamental property of all cellular life in prokaryotes and eukaryotes. Signals that originate from outside a cell (or extracellular signals) can be physical agents like mechanical pressure, voltage, temperature, light, or chemical signals (e.g., small molecules, peptides, or gas). Cell signaling can occur over short or long distances, and as a result can be classified as autocrine, juxtacrine, intracrine, paracrine, or endocrine. Signaling molecules can be synthesized from various biosynthetic pathways and released through passive or active transports, or even from cell damage. Receptors play a key role in cell signaling as they are able to detect chemical signals or physical stimuli. Receptors are generally proteins located on the cell surface or within the interio ...
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Guanine Nucleotide Exchange Factors
Guanine nucleotide exchange factors (GEFs) are proteins or protein domains that activate monomeric GTPases by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP). A variety of unrelated structural domains have been shown to exhibit guanine nucleotide exchange activity. Some GEFs can activate multiple GTPases while others are specific to a single GTPase. Function Guanine nucleotide exchange factors (GEFs) are proteins or protein domains involved in the activation of small GTPases. Small GTPases act as molecular switches in intracellular signaling pathways and have many downstream targets. The most well-known GTPases comprise the Ras superfamily and are involved in essential cell processes such as cell differentiation and proliferation, cytoskeletal organization, vesicle trafficking, and nuclear transport. GTPases are active when bound to GTP and inactive when bound to GDP, allowing their activity to be regulated by GEFs and th ...
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G Protein
G proteins, also known as guanine nucleotide-binding proteins, are a family of proteins that act as molecular switches inside cells, and are involved in transmitting signals from a variety of stimuli outside a cell to its interior. Their activity is regulated by factors that control their ability to bind to and hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP). When they are bound to GTP, they are 'on', and, when they are bound to GDP, they are 'off'. G proteins belong to the larger group of enzymes called GTPases. There are two classes of G proteins. The first function as monomeric small GTPases (small G-proteins), while the second function as heterotrimeric G protein complexes. The latter class of complexes is made up of '' alpha'' (α), ''beta'' (β) and ''gamma'' (γ) subunits. In addition, the beta and gamma subunits can form a stable dimeric complex referred to as the beta-gamma complex . Heterotrimeric G proteins located within the cell are activ ...
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Rho Family
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. History 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 seq ...
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RhoGEF Domain
RhoGEF domain describes two distinct structural domains with guanine nucleotide exchange factor (GEF) activity to regulate small GTPases in the Rho family. Rho small GTPases are inactive when bound to GDP but active when bound to GTP; RhoGEF domains in proteins are able to promote GDP release and GTP binding to activate specific Rho family members, including RhoA, Rac1 and Cdc42. The largest class of RhoGEFs is composed of proteins containing the " Dbl-homology" (DH) domain, which almost always is found together with a pleckstrin-homology (PH) domain to form a combined DH/PH domain structure. A distinct class of RhoGEFs is those proteins containing the DOCK/CZH/DHR-2 domain. This structure has no sequence similarity with DBL-homology domains. Human proteins containing DH/PH RhoGEF domain ABR; AKAP13/ARHGEF13/Lbc; ALS2; ALS2CL; ARHGEF1/p115-RhoGEF; ARHGEF10; ARHGEF10L; ARHGEF11/PDZ-RhoGEF.; ARHGEF12/LARG; ARHGEF15; ARHGEF16; ARHGEF17; ARHGEF18; ...
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PH Domain
In chemistry, pH (), historically denoting "potential of hydrogen" (or "power of hydrogen"), is a scale used to specify the acidity or basicity of an aqueous solution. Acidic solutions (solutions with higher concentrations of ions) are measured to have lower pH values than basic or alkaline solutions. The pH scale is logarithmic and inversely indicates the concentration of hydrogen ions in the solution.Bates, Roger G. ''Determination of pH: theory and practice''. Wiley, 1973. :\ce = - \log(a_\ce) = -\log( ce\ce M) where M = mol dm−3. At 25 °C (77 °F), solutions with a pH less than 7 are acidic, and solutions with a pH greater than 7 are basic. Solutions with a pH of 7 at this temperature are neutral (i.e. have the same concentration of H+ ions as OH− ions, i.e. pure water). The neutral value of the pH depends on the temperaturebeing lower than 7 if the temperature increases above 25 °C. The pH value can be less than 0 for very concentrated strong acids, ...
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Choanoflagellates
The choanoflagellates are a group of free-living unicellular and colonial flagellate eukaryotes considered to be the closest living relatives of the animals. Choanoflagellates are collared flagellates, having a funnel shaped collar of interconnected microvilli at the base of a flagellum. Choanoflagellates are capable of both asexual and sexual reproduction. They have a distinctive cell morphology characterized by an ovoid or spherical cell body 3–10  µm in diameter with a single apical flagellum surrounded by a collar of 30–40 microvilli (see figure). Movement of the flagellum creates water currents that can propel free-swimming choanoflagellates through the water column and trap bacteria and detritus against the collar of microvilli, where these foodstuffs are engulfed. This feeding provides a critical link within the global carbon cycle, linking trophic levels. In addition to their critical ecological roles, choanoflagellates are of particular interest to evolutio ...
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VAV1
Proto-oncogene vav is a protein that in humans is encoded by the ''VAV1'' gene. Function The protein encoded by this proto-oncogene is a member of the Dbl family of guanine nucleotide exchange factors (GEF) for the Rho family of GTP binding proteins. The protein is important in hematopoiesis, playing a role in T-cell and B-cell development and activation. This particular GEF has been identified as the specific binding partner of Nef proteins from HIV-1. Coexpression and binding of these partners initiates profound morphological changes, cytoskeletal rearrangements and the JNK/SAPK signaling cascade, leading to increased levels of viral transcription and replication. Interactions VAV1 has been shown to interact with: * ARHGDIB, * Abl gene, * Cbl gene * EZH2, * Grb2, * JAK2, * Ku70, * LAT, * LCP2, * MAPK1, * PIK3R1, * PLCG1, * PRKCQ, * S100B, * SHB, * SIAH2, and * Syk Tyrosine-protein kinase SYK, also known as spleen tyrosine kinase, is an enzyme which in ...
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VAV2
Guanine nucleotide exchange factor VAV2 is a protein that in humans is encoded by the ''VAV2'' gene. VAV2 is the second member of the VAV oncogene family. Unlike VAV1, which is expressed exclusively in hematopoietic cells, VAV2 transcripts were found in most tissues. Interactions VAV2 has been shown to interact with CD19 B-lymphocyte antigen CD19, also known as CD19 molecule ( Cluster of Differentiation 19), B-Lymphocyte Surface Antigen B4, T-Cell Surface Antigen Leu-12 and CVID3 is a transmembrane protein that in humans is encoded by the gene ''CD19''. In humans, ... and Grb2. References Further reading * * * * * * * * * * * * * * * * * * External links

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VAV3
Guanine nucleotide exchange factor VAV3 is a protein that in humans is encoded by the ''VAV3'' gene. This gene is a member of the VAV gene family. The VAV proteins are guanine nucleotide exchange factors (GEFs) for Rho family GTPases that activate pathways leading to actin cytoskeletal rearrangements and transcriptional alterations. This gene product acts as a GEF preferentially for RhoG, RhoA, and to a lesser extent, RAC1, and it associates maximally with the nucleotide-free states of these GTPases. Alternatively spliced transcript variants encoding different isoforms have been described for this gene. Interactions VAV3 has been shown to interact with Grb2. See also * Actin * Cytoskeleton * GTPase GTPases are a large family of hydrolase enzymes that bind to the nucleotide guanosine triphosphate (GTP) and hydrolyze it to guanosine diphosphate (GDP). The GTP binding and hydrolysis takes place in the highly conserved P-loop "G domain", a pro ... References Further read ...
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