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What does S-palmitoylation do to membrane proteins?


Blaskovic, Sanja; Blanc, Mathieu; van der Goot, F Gisou (2013). What does S-palmitoylation do to membrane proteins? FEBS Journal, 280(12):2766-2774.

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, as phosphory lation 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 will briefly review the current knowledge regarding the enzymes responsible for palmitate addition and removal. We will then describe various observed consequences of membrane protein palmitoylation. We propose that the direct effects of palmitoylation on transmembrane proteins might however 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 protein s and controlled interplay with other post;translational modifications.

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, as phosphory lation 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 will briefly review the current knowledge regarding the enzymes responsible for palmitate addition and removal. We will then describe various observed consequences of membrane protein palmitoylation. We propose that the direct effects of palmitoylation on transmembrane proteins might however 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 protein s and controlled interplay with other post;translational modifications.

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Additional indexing

Item Type:Journal Article, refereed, further contribution
Communities & Collections:Special Collections > SystemsX.ch
Special Collections > SystemsX.ch > Research, Technology and Development Projects > LipidX
Special Collections > SystemsX.ch > Research, Technology and Development Projects
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:2013
Deposited On:11 Sep 2013 15:02
Last Modified:07 Dec 2017 22:27
Publisher:Wiley-Blackwell
ISSN:1742-464X
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1111/febs.12263
PubMed ID:23551889

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