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Molecular and Cellular Biology, June 1999, p. 4480-4494, Vol. 19, No. 6
Department of Molecular Genetics, Weizmann
Institute of Science, Rehovot 76100, Israel
Received 9 December 1998/Returned for modification 26 January
1999/Accepted 8 March 1999
We have screened for proteins that interact with v-SNAREs of the
late secretory pathway in the yeast Saccharomyces
cerevisiae. A novel protein, designated Vsm1, binds tightly to
the Snc2 v-SNARE in the two-hybrid system and can be
coimmunoprecipitated with Snc1 or Snc2 from solubilized yeast cell
extracts. Disruption of the VSM1 gene results
in an increase of proteins secreted into the medium but does not
affect the processing or secretion of invertase. In contrast,
VSM1 overexpression in cells which bear a
temperature-sensitive mutation in the Sec9 t-SNARE (sec9-4
cells) results in the accumulation of non-invertase-containing
low-density secretory vesicles, inhibits cell growth and the secretion
of proteins into the medium, and blocks rescue of the
temperature-sensitive phenotype by SNC1 overexpression.
Yet, VSM1 overexpression does not affect yeast bearing a
sec9-7 allele which, in contrast to sec9-4,
encodes a t-SNARE protein capable of forming a stable SNARE complex in
vitro at restrictive temperatures. On the basis of these results, we
propose that Vsm1 is a novel v-SNARE-interacting protein that appears
to act as negative regulator of constitutive exocytosis. Moreover, this
regulation appears specific to one of two parallel exocytic paths which
are operant in yeast cells.
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Yeast VSM1 Encodes a v-SNARE Binding
Protein That May Act as a Negative Regulator of Constitutive
Exocytosis
*
Corresponding author. Mailing address: Department of
Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel. Phone: 972-8-9342106. Fax: 972-8-9344108. E-mail:
lvjeff{at}weizmann.weizmann.ac.il.
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