Abstract:
:S-Acylation (commonly referred to as S-palmitoylation) is a post-translational modification consisting in the covalent attachment of an acyl chain to a cysteine residue of the target protein. The lability of the resulting thioester bond gives S-acylation an essential characteristic: its reversibility. S-acylation dynamically regulates different aspects in the life of a protein (including stability, localization, interactome, and function) and, thus, plays critical roles in cellular physiology. For long, the reversibility of S-acylation has been neglected and thereby its potential as a regulatory mechanism for protein function undervalued. Thanks to technological advances, the field has now entered its golden era. A great diversity of interesting targets is being identified, the physio-pathological importance of the modification is starting to be revealed, structural information on the enzymes is becoming available, and the regulatory dynamics are gradually being understood. Here we will review the most recent literature in the S-acylation field, with a special focus on the molecular aspects of the modification, its regulation, and its consequences.
journal_name
Crit Rev Biochem Mol Bioljournal_title
Critical reviews in biochemistry and molecular biologyauthors
Zaballa ME,van der Goot FGdoi
10.1080/10409238.2018.1488804subject
Has Abstractpub_date
2018-08-01 00:00:00pages
420-451issue
4eissn
1040-9238issn
1549-7798journal_volume
53pub_type
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