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HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion

Academic Article
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Overview

authors

  • Xu, H.
  • Jun, Y.
  • Thompson, J.
  • Yates III, John
  • Wickner, W.

publication date

  • June 2010

journal

  • EMBO Journal  Journal

abstract

  • SNARE-dependent membrane fusion requires the disassembly of cis-SNARE complexes (formed by SNAREs anchored to one membrane) followed by the assembly of trans-SNARE complexes (SNAREs anchored to two apposed membranes). Although SNARE complex disassembly and assembly might be thought to be opposing reactions, the proteins promoting disassembly (Sec17p/Sec18p) and assembly (the HOPS complex) work synergistically to support fusion. We now report that trans-SNARE complexes formed during vacuole fusion are largely associated with Sec17p. Using a reconstituted proteoliposome fusion system, we show that trans-SNARE complex, like cis-SNARE complex, is sensitive to Sec17p/Sec18p mediated disassembly. Strikingly, HOPS inhibits the disassembly of SNARE complexes in the trans-, but not in the cis-, configuration. This selective HOPS preservation of trans-SNARE complexes requires HOPS:SNARE recognition and is lost when the apposed bilayers are dissolved in Triton X-100; it is also observed during fusion of isolated vacuoles. HOPS thus directs the Sec17p/Sec18p chaperone system to maximize functional trans-SNARE complex for membrane fusion, a new role of tethering factors during membrane traffic.

subject areas

  • Adenosine Triphosphatases
  • Cell Membrane
  • Membrane Fusion
  • Models, Biological
  • SNARE Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
  • Vacuoles
  • Vesicular Transport Proteins
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Research

keywords

  • HOPS
  • membrane fusion
  • tethering factor
  • trans-SNARE complex
  • yeast vacuole
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Identity

PubMed Central ID

  • PMC2892374

International Standard Serial Number (ISSN)

  • 0261-4189

Digital Object Identifier (DOI)

  • 10.1038/emboj.2010.97

PubMed ID

  • 20473271
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Additional Document Info

start page

  • 1948

end page

  • 1960

volume

  • 29

issue

  • 12

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