α-SNAP interferes with the zippering of the SNARE protein membrane fusion machinery

Yongsoo Park, Wensi Vennekate, Halenur Yavuz, Julia Preobraschenski, Javier M. Hernandez, Dietmar Riedel, Peter Jomo Walla, Reinhard Jahn*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

35 Citations (Scopus)

Abstract

Neuronal exocytosis is mediated by soluble N-ethylmaleimidesensitive factor attachment protein receptor (SNARE) proteins. Before fusion, SNARE proteins form complexes bridging the membrane followed by assembly toward the C-terminal membrane anchors, thus initiating membrane fusion. After fusion, the SNARE complex is disassembled by the AAAATPase N-ethylmaleimide-sensitive factor that requires the cofactor α-SNAP to first bind to the assembled SNARE complex. Using chromaffin granules and liposomes we now show that α-SNAP on its own interferes with the zippering of membraneanchored SNARE complexes midway through the zippering reaction, arresting SNAREs in a partially assembled transcomplex and preventing fusion. Intriguingly, the interference does not result in an inhibitory effect on synaptic vesicles, suggesting that membrane properties also influence the final outcome of α-SNAP interference with SNARE zippering. We suggest that binding of α-SNAP to the SNARE complex affects the ability of the SNARE complex to harness energy or transmit force to the membrane.

Original languageEnglish
Pages (from-to)16326-16335
Number of pages10
JournalJournal of Biological Chemistry
Volume289
Issue number23
DOIs
Publication statusPublished - 6 Jun 2014
Externally publishedYes

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