Syntaxin clusters assemble reversibly at sites of secretory granules in live cells

S. Barg, M. K. Knowles, X. Chen, M. Midorikawa, Wolfhard Almers

Research output: Contribution to journalArticle

70 Citations (Scopus)

Abstract

Syntaxin resides in the plasma membrane, where it helps to catalyze membrane fusion during exocytosis. The protein also forms clusters in cell-free and granule-free plasma-membrane sheets. We imaged the interaction between syntaxin and single secretory granules by two-color total internal reflection microscopy in PC12 cells. Syntaxin-GFP assembled in clusters at sites where single granules had docked at the plasma membrane. Clusters were intermittently present at granule sites, as syntaxin molecules assembled and disassembled in a coordinated fashion. Recruitment to granules required the N-terminal domain of syntaxin, but not the entry of syntaxin into SNARE complexes. Clusters facilitated exocytosis and disassembled once exocytosis was complete. Syntaxin cluster formation defines an intermediate step in exocytosis.

Original languageEnglish (US)
Pages (from-to)20804-20809
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume107
Issue number48
DOIs
StatePublished - Nov 30 2010

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Qa-SNARE Proteins
Secretory Vesicles
Exocytosis
Cell Membrane
SNARE Proteins
Membrane Fusion
PC12 Cells
Microscopy
Color

Keywords

  • Dynamic instability
  • Molecular docking
  • Nanodomains
  • Total internal reflection fluorescence

ASJC Scopus subject areas

  • General

Cite this

Syntaxin clusters assemble reversibly at sites of secretory granules in live cells. / Barg, S.; Knowles, M. K.; Chen, X.; Midorikawa, M.; Almers, Wolfhard.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 107, No. 48, 30.11.2010, p. 20804-20809.

Research output: Contribution to journalArticle

Barg, S. ; Knowles, M. K. ; Chen, X. ; Midorikawa, M. ; Almers, Wolfhard. / Syntaxin clusters assemble reversibly at sites of secretory granules in live cells. In: Proceedings of the National Academy of Sciences of the United States of America. 2010 ; Vol. 107, No. 48. pp. 20804-20809.
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