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HOPS prevents the disassembly of trans ‐SNARE complexes by Sec17p/Sec18p during membrane fusion
Author(s) -
Xu Hao,
Jun Youngsoo,
Thompson James,
Yates John,
Wickner William
Publication year - 2010
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2010.97
Subject(s) - snare complex , lipid bilayer fusion , biology , vesicular transport proteins , microbiology and biotechnology , vacuole , membrane , fusion , biophysics , snap25 , biochemistry , vesicle , synaptic vesicle , cytoplasm , linguistics , philosophy , vacuolar protein sorting
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.