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Vol. 10, Issue 6, 1837-1849, June 1999
Department of Pharmacology, Wayne State University School of
Medicine, Detroit, Michigan 48201
Rab2 immunolocalizes to pre-Golgi intermediates (vesicular-tubular
clusters [VTCs]) that are the first site of segregation of
anterograde- and retrograde-transported proteins and a major peripheral
site for COPI recruitment. Our previous work showed that Rab2
Q65L (equivalent to Ras Q61L) inhibited endoplasmic reticulum
(ER)-to-Golgi transport in vivo. In this study, the biochemical
properties of Rab2 Q65L were analyzed. The mutant protein binds GDP and
GTP and has a low GTP hydrolysis rate that suggests that Rab2 Q65L is
predominantly in the GTP-bound-activated form. The purified protein
arrests vesicular stomatitis virus glycoprotein transport from
VTCs in an assay that reconstitutes ER-to-Golgi traffic. A quantitative
binding assay was used to measure membrane binding of 
-COP
when incubated with the mutant. Unlike Rab2 that stimulates
recruitment, Rab2 Q65L showed a dose-dependent decrease in
membrane-associated -COP when incubated with rapidly sedimenting
membranes (ER, pre-Golgi, and Golgi). The mutant protein does not
interfere with -COP binding but stimulates the release of slowly
sedimenting vesicles containing Rab2, -COP, and p53/gp58 but lacking
anterograde grade-directed cargo. To complement the biochemical
results, we observed in a morphological assay that Rab2 Q65L caused
vesiculation of VTCs that accumulated at 15°C. These data suggest
that the Rab2 protein plays a role in the low-temperature-sensitive step that regulates membrane flow from VTCs to the Golgi complex and
back to the ER.
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