Rab5, an early acting endosomal GTPase, supports in vitro endosome fusion without GTP hydrolysis.
作者： P. D. Stahl , Guangpu Li , M. A. Barbieri , M. I. Colombo
DOI: 10.1016/S0021-9258(17)32224-X
关键词: Biochemistry 、 Endosome 、 Prenylation 、 Cell biology 、 Guanosine 、 GTPase 、 GTP' 、 Lipid bilayer fusion 、 Biology 、 G protein 、 Heterotrimeric G protein
摘要: Endocytosis is regulated by several GTPases including Rab5 and one or more heterotrimeric G proteins. We show here that Rab5, in the GTP gamma S (guanosine 5'-O-(thiotriphosphate))-bound form, fully supports vitro endosome fusion, indicating hydrolysis not required, whereas Rab5:S34N Rab5:N133I, mutants unable to bind GTP, are potent inhibitors of fusion. Double (Rab5:S34N/delta C4 Rab5:N133I/delta C4) lacking C-terminal prenylation site were inactive, required. Endosomes became resistant inhibitory effects preincubating vesicles with cytosol prior addition inhibitor. The acquisition resistance was rapid than N-ethylmaleimide, early acting. beta subunits proteins block However effect abrogated Rab5-GTP S, a protein may operate upstream Rab5.
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