The molecular era of protein S-acylation: spotlight on structure, mechanisms, and dynamics.

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.

authors

Zaballa ME,van der Goot FG

doi

10.1080/10409238.2018.1488804

subject

Has Abstract

pub_date

2018-08-01 00:00:00

pages

420-451

issue

4

eissn

1040-9238

issn

1549-7798

journal_volume

53

pub_type

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