Defining the functions of trans-SNARE pairs

Christian Ungermann (), Ken Sato and William Wickner
Additional contact information
Christian Ungermann: Dartmouth Medical School
Ken Sato: Dartmouth Medical School
William Wickner: Dartmouth Medical School

Nature, 1998, vol. 396, issue 6711, 543-548

Abstract: 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.

Date: 1998
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/25069 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:396:y:1998:i:6711:d:10.1038_25069

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/25069

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().