Abstract
The attachment of palmitic acid to the amino acid cysteine via thioester linkage (S-palmitoylation) is a common post-translational modification of eukaryotic proteins. In this review, we discuss the role of palmitoylation as a versatile protein sorting signal, regulating protein trafficking between distinct intracellular compartments and the micro-localization of proteins within membranes.
Original language | English |
---|---|
Pages (from-to) | 67-79 |
Number of pages | 13 |
Journal | Molecular Membrane Biology |
Volume | 26 |
Issue number | 1 |
DOIs | |
Publication status | Published - Jan 2009 |
Externally published | Yes |
Keywords
- Humans
- Lipoylation
- Membrane Microdomains
- Protein Processing, Post-Translational
- Protein Sorting Signals
- Protein Transport
- Proteins
- Journal Article
- Research Support, Non-U.S. Gov't
- Review