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J. Biol. Chem., Vol. 269, Issue 15, 10971-10974, Apr, 1994
G Fischer von Mollard, B Stahl, A Khokhlatchev, TC Sudhof and R Jahn
Rab3 proteins are small GTP-binding proteins of the Ras superfamily. Four
highly homologous Rab3 proteins termed Rab3A, Rab3B, Rab3C, and Rab3D have
been described. Rab3A has previously been shown to be a constituent of
synaptic vesicles in neurons that undergoes membrane
dissociation-association cycles during synaptic vesicle recycling. Here we
report that Rab3C copurifies with Rab3A during the isolation of synaptic
vesicles. Organelles immunoisolated with monoclonal antibodies directed
against Rab3A led to a coenrichment of Rab3A and Rab3C, demonstrating that
both Rab3 proteins are colocalized on the same organelle. In isolated nerve
terminals, stimulation of neurotransmitter release resulted in a
dissociation of Rab3C from synaptic vesicle and/or recycling membranes.
This dissociation parallels that of Rab3A observed under the same
conditions. In contrast, no change was observed in the membrane-association
of Rab5, a Rab protein localized on early endosomes. We conclude that in
the nervous system Rab3C is localized on synaptic vesicles and, like Rab3A,
cycles on and off the synaptic vesicle membrane in parallel with exocytotic
release of neurotransmitter.
Rab3C is a synaptic vesicle protein that dissociates from synaptic vesicles after stimulation of exocytosis
Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06510.
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