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JBC, Vol. 270, Issue 19, 11257-11262, May, 1995
H Horiuchi, A Giner, B Hoflack and M Zerial
Small GTPases of the Rab family are key regulators of intracellular
transport. They are associated with the cytoplasmic surface of distinct
exocytic and endocytic organelles and with transport vesicles connecting
these compartments. Rab proteins are also present in the cytosol in the
GDP-bound conformation complexed to Rab GDP dissociation inhibitor
(RabGDI). Upon membrane association, RabGDI is released, and the Rab
protein is converted into the GTP-bound form. In this paper we have
investigated whether Rab5, which regulates the clathrin-coated
vesicle-mediated pathway of endocytosis, can directly associate with the
membrane of clathrin-coated vesicles (CCV) purified from bovine brain in
vitro. We found that RabGDI can specifically deliver Rab5 but not Rab7,
which is localized to late endosomes, to CCV. Furthermore, CCV contain a
heat- and trypsin-sensitive activity that stimulates the dissociation of
GDP from Rab5, but not from Rab7, and the subsequent binding of GTP. The
activity was found to be associated with the CCV membrane but not with the
coat components. CCV weakly stimulated GDP release from either
post-translationally modified or unmodified Rab5 alone. However, maximal
GDP dissociation stimulation required the presence of RabGDI, suggesting
that the factor(s) responsible for the membrane association and GDP/GTP
exchange of Rab5 recognize the protein complexed to RabGDI. These data
demonstrate that CCV are competent for acquiring Rab5 and for converting
the molecule into the GTP-bound active form.
A GDP/GTP exchange-stimulatory activity for the Rab5-RabGDI complex on clathrin-coated vesicles from bovine brain
European Molecular Biology Laboratory, Heidelberg, Federal Republic of Germany.
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