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What does S ‐palmitoylation do to membrane proteins?
Author(s) -
Blaskovic Sanja,
Blanc Mathieu,
Goot F. Gisou
Publication year - 2013
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12263
Subject(s) - palmitoylation , transmembrane protein , membrane protein , peripheral membrane protein , transmembrane domain , microbiology and biotechnology , cytosol , chemistry , phosphorylation , biochemistry , ubiquitin , biology , membrane , integral membrane protein , enzyme , cysteine , receptor , gene
S ‐palmitoylation is post‐translational modification, which consists in the addition of a C16 acyl chain to cytosolic cysteines and which is unique amongst lipid modifications in that it is reversible. It can thus, like phosphorylation or ubiquitination, act as a switch. While palmitoylation of soluble proteins allows them to interact with membranes, the consequences of palmitoylation for transmembrane proteins are more enigmatic. We briefly review the current knowledge regarding the enzymes responsible for palmitate addition and removal. We then describe various observed consequences of membrane protein palmitoylation. We propose that the direct effects of palmitoylation on transmembrane proteins, however, might be limited to four non‐mutually exclusive mechanistic consequences: alterations in the conformation of transmembrane domains, association with specific membrane domains, controlled interactions with other proteins and controlled interplay with other post‐translational modifications.