Abstract
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 intracellular trafficking and exocytotic function of this essential protein.
| Original language | English |
|---|---|
| Pages (from-to) | 163-166 |
| Number of pages | 4 |
| Journal | Biochemical Society Transactions |
| Volume | 38 |
| Issue number | Pt 1 |
| DOIs | |
| Publication status | Published - Feb 2010 |
| Externally published | Yes |
Keywords
- Acyltransferases
- Animals
- Exocytosis
- Humans
- Lipoylation
- Protein Transport
- Synaptosomal-Associated Protein 25
- Journal Article
- Research Support, Non-U.S. Gov't
- Review