VAV2
Guanine nucleotide exchange factor VAV2 is a protein that in humans is encoded by the VAV2 gene.[5][6]
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.[6]
Interactions
VAV2 is a GEF for RAC1, specifically in fibroblasts VAV2 is necessary for integrin, but not growth factor–dependent activation of RAC leading to lamellipodia formation.[7] Double DH domain mutations, L342R/L343SVav2 function as a dominant negative, blocking VAV2 GEF activity for RAC1[7] and a PH domain mutant is required for recruitment of VAV2 to the membrane in order to elicit GEF activity.[7] VAV2 has also been shown to regulate collagen phagocytosis in a RAC1-dependent manner[8] and interact with CD19[9] and Grb2.[10][11]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000160293 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000009621 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Henske EP, Short MP, Jozwiak S, Bovey CM, Ramlakhan S, Haines JL, et al. (June 1995). "Identification of VAV2 on 9q34 and its exclusion as the tuberous sclerosis gene TSC1". Annals of Human Genetics. 59 (Pt 1): 25–37. doi:10.1111/j.1469-1809.1995.tb01603.x. PMID 7762982. S2CID 27548854.
- ^ a b "Entrez Gene: VAV2 vav 2 oncogene".
- ^ a b c Marignani PA, Carpenter CL (July 2001). "Vav2 is required for cell spreading". The Journal of Cell Biology. 154 (1): 177–186. doi:10.1083/jcb.200103134. PMC 2196856. PMID 11448999.
- ^ Arora PD, Marignani PA, McCulloch CA (July 2008). "Collagen phagocytosis is regulated by the guanine nucleotide exchange factor Vav2". American Journal of Physiology. Cell Physiology. 295 (1): C130–7. doi:10.1152/ajpcell.00168.2008. PMC 2493554. PMID 18434624.
- ^ Doody GM, Billadeau DD, Clayton E, Hutchings A, Berland R, McAdam S, et al. (November 2000). "Vav-2 controls NFAT-dependent transcription in B- but not T-lymphocytes". The EMBO Journal. 19 (22): 6173–6184. doi:10.1093/emboj/19.22.6173. PMC 305817. PMID 11080163.
- ^ Blagoev B, Kratchmarova I, Ong SE, Nielsen M, Foster LJ, Mann M (March 2003). "A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling". Nature Biotechnology. 21 (3): 315–318. doi:10.1038/nbt790. PMID 12577067. S2CID 26838266.
- ^ Bourguignon LY, Zhu H, Zhou B, Diedrich F, Singleton PA, Hung MC (December 2001). "Hyaluronan promotes CD44v3-Vav2 interaction with Grb2-p185(HER2) and induces Rac1 and Ras signaling during ovarian tumor cell migration and growth". The Journal of Biological Chemistry. 276 (52): 48679–48692. doi:10.1074/jbc.M106759200. PMID 11606575.
Further reading
- Romero F, Fischer S (1997). "Structure and function of vav". Cellular Signalling. 8 (8): 545–553. doi:10.1016/S0898-6568(96)00118-0. PMID 9115846.
- Smit L, van der Horst G, Borst J (1996). "Sos, Vav, and C3G participate in B cell receptor-induced signaling pathways and differentially associate with Shc-Grb2, Crk, and Crk-L adaptors". The Journal of Biological Chemistry. 271 (15): 8564–8569. doi:10.1074/jbc.271.15.8564. PMID 8621483.
- Tamma SM, Chirmule N, Yagura H, Oyaizu N, Kalyanaraman V, Pahwa S (August 1997). "CD4 cross-linking (CD4XL) induces RAS activation and tumor necrosis factor-alpha secretion in CD4+ T cells". Blood. 90 (4): 1588–1593. doi:10.1182/blood.V90.4.1588. PMID 9269777.
- De Sepulveda P, Okkenhaug K, Rose JL, Hawley RG, Dubreuil P, Rottapel R (February 1999). "Socs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferation". The EMBO Journal. 18 (4): 904–915. doi:10.1093/emboj/18.4.904. PMC 1171183. PMID 10022833.
- Pandey A, Podtelejnikov AV, Blagoev B, Bustelo XR, Mann M, Lodish HF (January 2000). "Analysis of receptor signaling pathways by mass spectrometry: identification of vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors". Proceedings of the National Academy of Sciences of the United States of America. 97 (1): 179–184. Bibcode:2000PNAS...97..179P. doi:10.1073/pnas.97.1.179. PMC 26636. PMID 10618391.
- Moores SL, Selfors LM, Fredericks J, Breit T, Fujikawa K, Alt FW, et al. (September 2000). "Vav family proteins couple to diverse cell surface receptors". Molecular and Cellular Biology. 20 (17): 6364–6373. doi:10.1128/MCB.20.17.6364-6373.2000. PMC 86111. PMID 10938113.
- Liu BP, Burridge K (2000). "Vav2 activates Rac1, Cdc42, and RhoA downstream from growth factor receptors but not beta1 integrins". Molecular and Cellular Biology. 20 (19): 7160–7169. doi:10.1128/MCB.20.19.7160-7169.2000. PMC 86269. PMID 10982832.
- Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–1795. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
- Tartare-Deckert S, Monthouel MN, Charvet C, Foucault I, Van Obberghen E, Bernard A, et al. (June 2001). "Vav2 activates c-fos serum response element and CD69 expression but negatively regulates nuclear factor of activated T cells and interleukin-2 gene activation in T lymphocyte". The Journal of Biological Chemistry. 276 (24): 20849–20857. doi:10.1074/jbc.M010588200. PMID 11262396.
- Teckchandani AM, Feshchenko EA, Tsygankov AY (2001). "c-Cbl facilitates fibronectin matrix production by v-Abl-transformed NIH3T3 cells via activation of small GTPases". Oncogene. 20 (14): 1739–1755. doi:10.1038/sj.onc.1204246. PMID 11313921. S2CID 28410819.
- Jevremovic D, Billadeau DD, Schoon RA, Dick CJ, Leibson PJ (June 2001). "Regulation of NK cell-mediated cytotoxicity by the adaptor protein 3BP2". Journal of Immunology. 166 (12). Baltimore: 7219–7228. doi:10.4049/jimmunol.166.12.7219. PMID 11390470.
- Tamás P, Solti Z, Buday L (2001). "Membrane-targeting is critical for the phosphorylation of Vav2 by activated EGF receptor". Cellular Signalling. 13 (7): 475–481. doi:10.1016/S0898-6568(01)00172-3. PMID 11516622.
- Booden MA, Campbell SL, Der CJ (2002). "Critical but distinct roles for the pleckstrin homology and cysteine-rich domains as positive modulators of Vav2 signaling and transformation". Molecular and Cellular Biology. 22 (8): 2487–2497. doi:10.1128/MCB.22.8.2487-2497.2002. PMC 133724. PMID 11909943.
- Tamás P, Solti Z, Bauer P, Illés A, Sipeki S, Bauer A, et al. (February 2003). "Mechanism of epidermal growth factor regulation of Vav2, a guanine nucleotide exchange factor for Rac". The Journal of Biological Chemistry. 278 (7): 5163–5171. doi:10.1074/jbc.M207555200. PMID 12454019.
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