S-acylation: an orchestrator of the life cycle and function of membrane proteins
S-acylation is a covalent post-translational modification of proteins with fatty acids, achieved by enzymatic attachment via a labile thioester bond. This modification allows for dynamic control of protein properties and functions in association with cell membranes. This lipid modification regulates a substantial portion of the human proteome and plays an increasingly recognized role throughout the lifespan of affected proteins. Recent technical advancements have propelled the S-acylation field into a 'molecular era', unveiling new insights into its mechanistic intricacies and far-reaching implications. With a striking increase in the number of studies on this modification, new concepts are indeed emerging on the roles of S-acylation in specific cell biology processes and features. After a brief overview of the enzymes involved in S-acylation, this viewpoint focuses on the importance of S-acylation in the homeostasis, function, and coordination of integral membrane proteins. In particular, we put forward the hypotheses that S-acylation is a gatekeeper of membrane protein folding and turnover and a regulator of the formation and dynamics of membrane contact sites.
WOS:001084875800001
2023-10-16
291
1
45
56
REVIEWED
Funder | Grant Number |
This work was supported by the Swiss National Science Foundation (SNSF) Corona Call, a foundation advised by CARIGEST S.A., the EPFL Corona Research Task Force and the NCCR Chemical Biology to FGG, by SNSF (31CA30_196651/205321_192371). | |
Swiss National Science Foundation (SNSF) Corona Call | |
CARIGEST S.A. | |
EPFL Corona Research Task Force | |
NCCR Chemical Biology | 31CA30_196651/205321_192371 |
SNSF | |