Journal
CELLULAR AND MOLECULAR NEUROBIOLOGY
Volume 30, Issue 8, Pages 1321-1326Publisher
SPRINGER/PLENUM PUBLISHERS
DOI: 10.1007/s10571-010-9599-4
Keywords
Exocytosis; SNAP-25; Syntaxin; FLIM
Categories
Funding
- Biotechnology and Biological Sciences Research Council Funding Source: Medline
- Medical Research Council Funding Source: Medline
- Wellcome Trust Funding Source: Medline
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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.
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