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MBC in Press, published online ahead of print May 23, 2007
Mol. Biol. Cell 10.1091/mbc.E06-08-0756

A more recent version of this article appeared on August 1, 2007
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Submitted on August 28, 2006
Revised on April 16, 2007
Accepted on May 15, 2007

Interaction of SNAREs with ArfGAPs Precedes Recruitment of Sec18p/NSF

Christina Schindler and Anne Spang

Biozentrum, University of Basel, CH-4056 Basel, Switzerland

Monitoring Editor: Randy Schekman

SNARE proteins are key components of the fusion machinery in vesicular transport and in homotypic membrane fusion. We previously found that ArfGAPs promoted a conformational change on SNAREs, which allowed recruitment of the small GTPase Arf1p in stoichiometric amounts. Here we show that the ArfGAP Gcs1p accelerates v-t-SNARE complex formation in vitro, indicating that ArfGAPs may act as folding chaperones. These SNARE complexes were resolved in the presence of ATP by the yeast homologues of {alpha}-SNAP and NSF, Sec17p and Sec18p, respectively. In addition, Sec18p and Sec17p also recognized the ‘activated’ SNAREs even when they were not engaged in v/t-SNARE complexes. Here again, the induction of a conformational change by ArfGAPs was essential. Surprisingly, recruitment of Sec18p to SNAREs did not require Sec17p or ATP hydrolysis. Moreover, Sec18p displaced pre-bound Arf1p from SNAREs, indicating that Sec18p may have more than one function: first to ensure that all vesicle coat proteins are removed from the SNAREs before the engagement in a trans-SNARE complex and second to resolve cis-SNARE complexes after fusion has occurred.

Address correspondence to: Anne Spang (anne.spang{at}unibas.ch)






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