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 |
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Pages (from-to) | 67-79 |
Number of pages | 13 |
Journal | Molecular Membrane Biology |
Volume | 26 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 2009 |
Keywords
- Palmitoylation
- protein sorting
- membrane microdomains
- lipid rafts
- protein trafficking
- CYSTEINE-STRING PROTEIN
- GPI-ANCHORED PROTEINS
- SRC-FAMILY KINASE
- PLASMA-MEMBRANE
- LIPID RAFTS
- MODEL MEMBRANES
- CELL-MEMBRANES
- H-RAS
- SUBCELLULAR-LOCALIZATION
- SACCHAROMYCES-CEREVISIAE