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(Received for publication, February 27, 1997, and in revised form, April 14, 1997)
From the Department of Molecular Genetics, Weizmann Institute of
Science, Rehovot 76100, Israel
We are studying yeast homologs of the
synaptobrevin/VAMP family of vesicle-associated membrane proteins,
which act as vesicular compartment-soluble
N-ethylmaleimide-sensitive factor attachment protein
receptors (v-SNAREs) in cells having a capacity for stimulus-coupled secretion, as well as in other cell types. The yeast homologs, Snc1 and
Snc2, localize to secretory vesicles and are required for normal bulk
secretion in Saccharomyces cerevisiae. Here we have used
Snc deletion mutants and chimeric Snc-VAMP proteins to demonstrate that
these v-SNAREs can be dissected into regions that are either
indispensable or dispensable for exocytic function in
vivo.
We have found that a region encompassing two predicted amphipathic
Volume 272, Number 26,
Issue of June 27, 1997
pp. 16591-16598
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
-Helical Segments on Yeast Homologs of the
Synaptobrevin/VAMP Family of v-SNAREs Mediate Exocytic
Function
-helices (helix 1 and helix 2) (residues 32-85), which are thought
to form coiled-coil structures, is essential for conferring exocytosis
in yeast. Deletions in either the helix 1 or helix 2 segments result in
a complete loss in the ability of the protein to confer secretion
competence to snc cells and to interact genetically with
components of the proposed fusion complex: the Sec9 and Sso2 t-SNAREs
and the Sec17 -SNAP homolog. In contrast, deletions in either the
variable (residues 2-27) or putative intravesicular (residues
115-117) regions have no deleterious effect upon v-SNARE function.
This makes it unlikely that sequences in either the amino or carboxyl
terminus act in an exocytic capacity. Along with additional studies
utilizing chimeric Snc-VAMP proteins, we suggest that although the Snc
and synaptobrevin/VAMP proteins have evolved to mediate vastly
different exocytic programs, their structural requirements and actions
have remained remarkably well-conserved in evolution.
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