GTPase-activator protein for Ras-like GTPase is a family of evolutionarily related proteins. Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyze GTP to GDP.[1] This intrinsic GTPase activity of ras is stimulated by a family of proteins collectively known as 'GAP' or GTPase-activating proteins.[2][3] As it is the GTP bound form of ras which is active, these proteins are said to be down-regulators of ras.
The Ras GTPase-activating proteins are quite large (from 765 residues for sar1 to 3079 residues for IRA2) but share only a limited (about 250 residues) region of sequence similarity, referred to as the 'catalytic domain' or rasGAP domain.
Note: There are distinctly different GAPs for the rap and rho/rac subfamilies of ras-like proteins (reviewed in reference[4]) that do not share sequence similarity with ras GAPs.
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Conformational Change from active (GTP bound) to inactive (GDP bound) state of H-Ras protein.
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GTPase cycles control Ras and Tubulin
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G Protein Coupled Receptors
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Examples
Human genes encoding proteins containing this domain include:
References
- ^ McCormick F, Bourne HR, Sanders DA (1991). "The GTPase superfamily: conserved structure and molecular mechanism". Nature. 349 (6305): 117–127. Bibcode:1991Natur.349..117B. doi:10.1038/349117a0. PMID 1898771. S2CID 4349901.
- ^ Wang Y, Riggs M, Rodgers L, Wigler M, Boguski M (1991). "sar1, a gene from Schizosaccharomyces pombe encoding a protein that regulates ras1". Cell Regul. 2 (6): 453–465. doi:10.1091/mbc.2.6.453. PMC 361829. PMID 1883874.
- ^ Maruta H, Burgess AW (1994). "Regulation of the Ras signalling network". BioEssays. 16 (7): 489–496. doi:10.1002/bies.950160708. PMID 7945277. S2CID 22850138.
- ^ McCormick F, Boguski MS (1993). "Proteins regulating Ras and its relatives". Nature. 366 (6456): 643–654. Bibcode:1993Natur.366..643B. doi:10.1038/366643a0. PMID 8259209. S2CID 4338237.
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This page was last edited on 26 July 2023, at 16:29