Protein-tyrosine kinases regulate the phosphorylation, protein interactions, subcellular distribution, and activity of p21ras GTPase-activating protein.
阅读量：
45
摘要：
Thep21rasGTPase-activatingprotein(GAP)down-regulatesp21rasbystimulatingitsintrinsicGTPaseactivityGAPisfoundpredominantlyasamonomerinthecytosolofnormalcellsHowever,incellsexpressinganactivatedcytoplasmicprotein-tyrosinekinase,p60v-src,orstimulatedwithepidermalgrowthfactor,GAPbecomesphosphorylatedontyrosineandserineandformsdistinctcomplexeswithtwophosphoproteinsof62and190kDa(p62andp190)Inv-src-transformedRat-2cells,aminorfractionofGAPassociateswiththehighlytyrosinephosphorylatedp62toformacomplexthatislocalizedattheplasmamembraneandinthecytosolIncontrast,themajorityofGAPentersadistinctcomplexwithp190thatisexclusivelycytosolicandcontainspredominantlyphosphoserineEpidermalgrowthfactorstimulationalsoinducesamarkedconversionofmonomericGAPtohigher-molecular-weightspeciesinratfibroblastsTheGAP-p190complexisdependentonphosphorylationandshowsreducedGAPactivityTheseresultsindicatethatprotein-tyrosinekinasesinduceGAPtoformmultipleheteromericcomplexes,whicharestrongcandidatesforregulatorsortargetsofp21ras
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关键词：
GAPbecomesphosphorylatedontyrosineandserineandformsdistinctcomplexeswithtwophosphoproteinsof62and190kDa(p62andp190)Inv-src-transformedRat-2cells whicharestrongcandidatesforregulatorsortargetsofp21ras orstimulatedwithepidermalgrowthfactor
DOI：
10.1128/mcb.11.4.1804
被引量：
年份：
1991
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