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Cellular and Molecular Neurobiology

, Volume 30, Issue 8, pp 1321–1326 | Cite as

The t-SNARE Complex: A Close Up

  • Alison R. Dun
  • Colin Rickman
  • Rory R. Duncan
Report

Abstract

The SNARE proteins, syntaxin, SNAP-25, and synaptobrevin have long been known to provide the driving force for vesicle fusion in the process of regulated exocytosis. Of particular interest is the initial interaction between SNAP-25 and syntaxin to form the t-SNARE heterodimer, an acceptor for subsequent synaptobrevin engagement. In vitro studies have revealed at least two different dynamic conformations of t-SNARE heterodimer defined by the degree of association of the C-terminal SNARE motif of SNAP-25 with syntaxin. At the plasma membrane, these proteins are organized into dense clusters of 50–60 nm in diameter. More recently, the t-SNARE interaction within these clusters was investigated in live cells at the molecular level, estimating each cluster to contain 35–70 t-SNARE molecules. This work reported the presence of both partially and fully zippered t-SNARE complex at the plasma membrane in agreement with the earlier in vitro findings. It also revealed a spatial segregation into distinct clusters containing predominantly one conformation apparently patterned by the surrounding lipid environment. The reason for this dynamic t-SNARE complex in exocytosis is uncertain; however, it does take us one step closer to understand the complex sequence of events leading to vesicle fusion, emphasizing the role of both membrane proteins and lipids.

Keywords

Exocytosis SNAP-25 Syntaxin FLIM 

Abbreviations

SNARE

Soluble N-ethylmaleimide-sensitive-factor attachment protein receptor

SNAP-25

Synaptosome-associated protein of 25 kD

FLIM

Fluorescence lifetime imaging microscopy

STED

Stimulated emission depletion microscopy

PALM

Photoactivatable localisation microscopy

Notes

Acknowledgments

This work was supported by Wellcome Trust and Medical Research Council project grants to RRD and a BBSRC Studentship to AD.

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Copyright information

© Springer Science+Business Media, LLC 2010

Authors and Affiliations

  • Alison R. Dun
    • 1
  • Colin Rickman
    • 2
  • Rory R. Duncan
    • 1
  1. 1.Centre for Integrative PhysiologyUniversity of Edinburgh Medical SchoolEdinburghUK
  2. 2.School of Engineering and Physical SciencesHeriot-Watt UniversityEdinburghUK

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