Tracking SNARE complex formation in live endocrine cells

Seong J. An, Wolfhard Almers

Research output: Contribution to journalArticle

110 Citations (Scopus)

Abstract

Syntaxin, synaptosome-associated protein of 25 kD (SNAP25), and vesicle-associated membrane protein/synaptobrevin are collectively called SNAP receptor (SNARE) proteins, and they catalyze neuronal exocytosis by forming a "core complex." The steps in core complex formation are unknown. Here, we monitored SNARE complex formation in vivo with the use of a fluorescent version of SNAP25. In PC12 cells, we found evidence for a syntaxin-SNAP25 complex that formed with high affinity, required only the amino-terminal SNARE motif of SNAP25, tolerated a mutation that blocks formation of other syntaxin-SNAP25 complexes, and assembled reversibly when Ca2+ entered cells during depolarization. The complex may represent a precursor to the core complex formed during a Ca2+-dependent priming step of exocytosis.

Original languageEnglish (US)
Pages (from-to)1042-1046
Number of pages5
JournalScience
Volume306
Issue number5698
DOIs
StatePublished - Nov 5 2004

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SNARE Proteins
Endocrine Cells
Synaptosomes
Qa-SNARE Proteins
R-SNARE Proteins
Proteins
Exocytosis
PC12 Cells
Mutation

ASJC Scopus subject areas

  • General

Cite this

Tracking SNARE complex formation in live endocrine cells. / An, Seong J.; Almers, Wolfhard.

In: Science, Vol. 306, No. 5698, 05.11.2004, p. 1042-1046.

Research output: Contribution to journalArticle

An, Seong J. ; Almers, Wolfhard. / Tracking SNARE complex formation in live endocrine cells. In: Science. 2004 ; Vol. 306, No. 5698. pp. 1042-1046.
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