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Ras GTPase-activating protein 3 is an enzyme that in humans is encoded by the RASA3gene.[5][6][7]
The protein encoded by this gene is member of the GAP1 family of GTPase-activating proteins. The gene product stimulates the GTPase activity of normal RAS p21 but not its oncogenic counterpart. Acting as a suppressor of RAS function, the protein enhances the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, thereby allowing control of cellular proliferation and differentiation. This family member is an inositol 1,3,4,5-tetrakisphosphate-binding protein, like the closely related RAS p21 protein activator 2. The two family members have distinct pleckstrin-homology domains, with this particular member having a domain consistent with its localization to the plasma membrane.[7]
It has been shown that RASA3 promotes a shift from noncanonical to canonical TGF-β signaling through SMAD3 in B cells.[8]
↑"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.
↑Cullen PJ, Hsuan JJ, Truong O, Letcher AJ, Jackson TR, Dawson AP, etal. (September 1995). "Identification of a specific Ins(1,3,4,5)P4-binding protein as a member of the GAP1 family". Nature. 376 (6540): 527–530. Bibcode:1995Natur.376..527C. doi:10.1038/376527a0. PMID7637787. S2CID4283160.
↑Mamand S, Liu H, Kashem M, Martin A (December 2024). "Suppression of Class Switch Recombination to IgA by RASA2 and RASA3 through Inhibition of TGF-β Signaling". Journal of Immunology. 213 (12). Baltimore: 1739–1745. doi:10.4049/jimmunol.2400353. PMID39451029.
Hjermstad SJ, Briggs SD, Smithgall TE (1993). "Phosphorylation of the ras GTPase-activating protein (GAP) by the p93c-fes protein-tyrosine kinase in vitro and formation of GAP-fes complexes via an SH2 domain-dependent mechanism". Biochemistry. 32 (39): 10519–10525. doi:10.1021/bi00090a031. PMID7691175.
Lockyer PJ, Vanlingen S, Reynolds JS, McNulty TJ, Irvine RF, Parys JB, etal. (February 1999). "Tissue-specific expression and endogenous subcellular distribution of the inositol 1,3,4,5-tetrakisphosphate-binding proteins GAP1(IP4BP) and GAP1(m)". Biochemical and Biophysical Research Communications. 255 (2): 421–426. doi:10.1006/bbrc.1999.0217. PMID10049724.
El-Daher SS, Patel Y, Siddiqua A, Hassock S, Edmunds S, Maddison B, etal. (June 2000). "Distinct localization and function of (1,4,5)IP(3) receptor subtypes and the (1,3,4,5)IP(4) receptor GAP1(IP4BP) in highly purified human platelet membranes". Blood. 95 (11): 3412–3422. doi:10.1182/blood.V95.11.3412. PMID10828023.
Koehler JA, Moran MF (2001). "RACK1, a protein kinase C scaffolding protein, interacts with the PH domain of p120GAP". Biochemical and Biophysical Research Communications. 283 (4): 888–895. doi:10.1006/bbrc.2001.4889. PMID11350068.
Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, etal. (January 2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nature Biotechnology. 23 (1): 94–101. doi:10.1038/nbt1046. PMID15592455. S2CID7200157.
