期刊
FRONTIERS IN PHYSIOLOGY
卷 13, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fphys.2022.1040968
关键词
S-acylation; palmitoylation; protein acyltransferases; palmitoyl acyltransferases; T cell receptor; T cell signaling; DHHC enzymes
类别
资金
- National Institute of General Medical Sciences of the National Institutes of Health (NIH/NIGMS)
- NIH/NIGMS
- [F31GM140644]
- [R01GM115446]
- [R01GM130840]
S-acylation is a reversible lipidation process that plays a crucial role in regulating T cell function by controlling protein localization, stability, and interactions.
S-acylation, the reversible lipidation of free cysteine residues with long-chain fatty acids, is a highly dynamic post-translational protein modification that has recently emerged as an important regulator of the T cell function. The reversible nature of S-acylation sets this modification apart from other forms of protein lipidation and allows it to play a unique role in intracellular signal transduction. In recent years, a significant number of T cell proteins, including receptors, enzymes, ion channels, and adaptor proteins, were identified as S-acylated. It has been shown that S-acylation critically contributes to their function by regulating protein localization, stability and protein-protein interactions. Furthermore, it has been demonstrated that zDHHC protein acyltransferases, the family of enzymes mediating this modification, also play a prominent role in T cell activation and differentiation. In this review, we aim to highlight the diversity of proteins undergoing S-acylation in T cells, elucidate the mechanisms by which reversible lipidation can impact protein function, and introduce protein acyltransferases as a novel class of regulatory T cell proteins.
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