Regulation of SNAP-25 trafficking and function by palmitoylation.

@article{Greaves2010RegulationOS,
  title={Regulation of SNAP-25 trafficking and function by palmitoylation.},
  author={Jennifer Greaves and Gerald R. Prescott and Oforiwa A. Gorleku and Luke H Chamberlain},
  journal={Biochemical Society transactions},
  year={2010},
  volume={38 Pt 1},
  pages={163-6}
}
The SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) protein SNAP-25 (25 kDa synaptosome-associated protein) is essential for regulated exocytosis in neuronal and neuroendocrine cells. Whereas the majority of SNARE proteins contain transmembrane domains, SNAP-25 is instead anchored to membranes by the palmitoylation of a central cysteine-rich region. In this review, we discuss the mechanisms of SNAP-25 palmitoylation and how this modification regulates the… CONTINUE READING

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Synaptic vesicle fusion

Nature Structural &Molecular Biology • 2008

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