SNARE complex oligomerization by synaphin/complexin is essential for synaptic vesicle exocytosis

Hiroshi Tokumaru, Keiko Umayahara, Lorenzo L. Pellegrini, Toru Ishizuka, Hideo Saisu, Heinrich Betz, George J. Augustine, Teruo Abe

Research output: Contribution to journalArticlepeer-review

125 Citations (Scopus)

Abstract

Synaphin/complexin is a cytosolic protein that preferentially binds to syntaxin within the SNARE complex. We find that synaphin promotes SNAREs to form precomplexes that oligomerize into higher order structures. A peptide from the central, syntaxin binding domain of synaphin competitively inhibits these two proteins from interacting and prevents SNARE complexes from oligomerizing. Injection of this peptide into squid giant presynaptic terminals inhibited neurotransmitter release at a late prefusion step of synaptic vesicle exocytosis. We propose that oligomerization of SNARE complexes into a higher order structure creates a SNARE scaffold for efficient, regulated fusion of synaptic vesicles.

Original languageEnglish
Pages (from-to)421-432
Number of pages12
JournalCell
Volume104
Issue number3
DOIs
Publication statusPublished - 2001 Feb 9
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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