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PMID: 9859990 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Defining the functions of trans-SNARE pairs.

Nature ·Vol. 396 ·No. 6711 ·1998-12-10 ·Pages 543-8

Ungermann C, Sato K, Wickner W

Abstract

The homotypic fusion of yeast vacuoles includes a 'docking' step, which we show here to consist of two sequential reactions: a reversible 'tethering' mediated by the GTPase Ypt7, and 'SNARE pairing', in which SNARE proteins from opposite membranes form a complex in trans. The function of this trans-SNARE complex must be transient, as the complex can be disassembled by excess Sec18 in the presence of Sec17 and ATP without influencing the fusion rate. These data indicate that SNARE pairing may transiently signal to downstream factors, leading to fusion.

MeSH Terms
Adenosine Triphosphatases Carrier Proteins/physiology Fungal Proteins/genetics,physiology GTP-Binding Proteins/physiology Guanine Nucleotide Dissociation Inhibitors Intracellular Membranes/physiology Membrane Fusion/physiology Membrane Proteins/physiology Qa-SNARE Proteins SNARE Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins Vacuoles/physiology Vesicular Transport Proteins rab GTP-Binding Proteins
Chemicals
Carrier Proteins Fungal Proteins GDP dissociation inhibitor 1 Guanine Nucleotide Dissociation Inhibitors Membrane Proteins Qa-SNARE Proteins SEC17 protein, S cerevisiae SNARE Proteins Saccharomyces cerevisiae Proteins Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins VAM3 protein, S cerevisiae Vesicular Transport Proteins Adenosine Triphosphatases GTP-Binding Proteins SEC18 protein, S cerevisiae YPT7 protein, S cerevisiae rab GTP-Binding Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Ungermann C
Dartmouth Medical School, Department of Biochemistry, Hanover, New Hampshire 03755, USA. [email protected]
Sato K
Wickner W
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
DOI
10.1038/25069
Email
[email protected]
Published
1998-12-10
Pages
543-8
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentIn
PMID: 9859980
External Links
PubMed source DOI: 10.1038/25069 View journal details
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