title: What does S-palmitoylation do to membrane proteins?
abstract: 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.
authors.affiliation: Global Health Institute, Ecole Polytechnique Fédérale de Lausanne, Switzerland.
authors.forename: Sanja
authors.initials: S
authors.lastname: Blaskovic
authors.forename: Mathieu
authors.initials: M
authors.lastname: Blanc
authors.forename: F Gisou
authors.initials: FG
authors.lastname: van der Goot
mesh_terms: D000217:Acyltransferases / Q000502:physiology; D000818:Animals; D006801:Humans; D054878:Lipoylation; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D019308:Palmitic Acid / Q000378:metabolism*; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary
chemical_list: D008565:Membrane Proteins; D019308:Palmitic Acid; D000217:Acyltransferases