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PMID: 9628864 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion.

The EMBO journal ·Vol. 17 ·No. 12 ·1998-06-15 ·Pages 3269-76

Ungermann C, Wickner W

Abstract

The vacuole v-t-SNARE complex is disassembled by Sec17p/alpha-SNAP and Sec18p/NSF prior to vacuole docking and fusion. We now report a functional characterization of the vacuolar SNARE Vam7p, a SNAP-25 homolog. Although Vam7p has no hydrophobic domains, it is tightly associated with the vacuolar membrane. Vam7p is a constituent of the vacuole SNARE complex and is released from this complex by the Sec17p/Sec18p/ATP-mediated priming of the vacuoles. Even in the absence of the vacuolar v-SNARE Nyv1p, a subcomplex which includes Vam7p and the t-SNARE Vam3p is preserved. Vam7p is necessary for the stability of the vacuolar SNARE complex, since vacuoles from mutants deleted in VAM7 do not have a Vam3p-Nyv1p complex. Furthermore, Vam7p alone, in the absence of Nyv1p and Vam3p, cannot mediate fusion with wild-type vacuoles, whereas vacuoles with only Nyv1p or Vam3p alone can fuse with wild-type vacuoles in the absence of the other two SNAREs. Thus, Vam7p is important for the stable assembly and efficient function of the vacuolar SNARE complex and maintenance of the vacuolar morphology. This functional characterization of Vam7p suggests a general role for SNAP-25 homologs, not only on the plasma membrane but along the secretory pathway.

MeSH Terms
Adenosine Triphosphatases Fungal Proteins/physiology Membrane Proteins/metabolism,physiology Nerve Tissue Proteins/chemistry,genetics,physiology Qc-SNARE Proteins SNARE Proteins Saccharomyces cerevisiae/physiology Saccharomyces cerevisiae Proteins Synaptosomal-Associated Protein 25 Vacuoles/physiology Vesicular Transport Proteins
Chemicals
Fungal Proteins Membrane Proteins Nerve Tissue Proteins Qc-SNARE Proteins SNARE Proteins Saccharomyces cerevisiae Proteins Synaptosomal-Associated Protein 25 VAM7 protein, S cerevisiae Vesicular Transport Proteins Adenosine Triphosphatases SEC18 protein, S cerevisiae
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ungermann C
Dartmouth Medical School, Department of Biochemistry, Hanover, NH 03755, USA.
Wickner W
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
DOI
10.1093/emboj/17.12.3269
Published
1998-06-15
Pages
3269-76
Language
English
Region
England
NLM ID
8208664
PMCID
PMC1170665
Subset
IM
External Links
PubMed source DOI: 10.1093/emboj/17.12.3269 PMC Full Text View journal details
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