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Vol. 10, Issue 12, 4149-4161, December 1999
Department of Cell Biology, Yale University School of Medicine, New
Haven, Connecticut 06520-8002
Fusion of post-Golgi secretory vesicles with the plasma membrane in
yeast requires the function of a Rab protein, Sec4p, and a set of v-
and t-SNAREs, the Snc, Sso, and Sec9 proteins. We have tested the
hypothesis that a selective interaction between Sec4p and the exocytic
SNAREs is responsible for ensuring that secretory vesicles fuse with
the plasma membrane but not with intracellular organelles. Assembly of
Sncp and Ssop into a SNARE complex is defective in a
sec4-8 mutant strain. However, Snc2p binds in vivo to
many other syntaxin-like t-SNAREs, and binding of Sncp to the
endosomal/Golgi t-SNARE Tlg2p is also reduced in sec4-8
cells. In addition, binding of Sncp to Ssop is reduced by mutations in
two other Rab genes and four non-Rab genes that block the secretory
pathway before the formation of secretory vesicles. In an alternate
approach to look for selective Rab-SNARE interactions, we report that
the nucleotide-free form of Sec4p coimmunoprecipitates with Ssop.
However, Rab-SNARE binding is nonselective, because the
nucleotide-free forms of six Rab proteins bind with similar low
efficiency to three SNARE proteins, Ssop, Pep12p, and Sncp. We conclude
that Rabs and SNAREs do not cooperate to specify the target membrane.
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