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J. Biol. Chem., Vol. 269, Issue 29, 18720-18722, Jul, 1994
MA Barbieri, G Li, MI Colombo and PD Stahl
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 in vitro
endosome fusion, indicating that GTP hydrolysis is not required, whereas
Rab5:S34N and Rab5:N133I, mutants unable to bind GTP, are potent inhibitors
of endosome fusion. Double mutants (Rab5:S34N/delta C4 and Rab5:N133I/delta
C4) lacking the C-terminal prenylation site were inactive, indicating that
prenylation is required. Endosomes became resistant to the inhibitory
effects of Rab5:S34N by preincubating the vesicles with cytosol prior to
the addition of the inhibitor. The acquisition of resistance to Rab5:S34N
was more rapid than to N-ethylmaleimide, indicating that Rab5 mutants are
early acting. G beta gamma subunits of heterotrimeric G proteins block
endosome fusion. However the effect of G beta gamma was abrogated by
Rab5-GTP gamma S, indicating that a heterotrimeric G protein may operate
upstream of Rab5.
Rab5, an early acting endosomal GTPase, supports in vitro endosome fusion without GTP hydrolysis
Department of Cell Biology and Physiology, Washington University School of Medicine, St Louis, Missouri 63110.
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