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

  • Zaballa ME a Global Health Institute, School of Life Sciences , Ecole Polytechnique Fédérale de Lausanne , Lausanne , Switzerland.
  • van der Goot FG a Global Health Institute, School of Life Sciences , Ecole Polytechnique Fédérale de Lausanne , Lausanne , Switzerland.
  • 2018-07-13
Published in:
  • Critical reviews in biochemistry and molecular biology. - 2018
Post-translational modification
S-acylation
dynamics
protein S-acyltransferases (PATs)
substrate recognition
thioesterases
Acylation
Animals
Humans
Lipoylation
Protein Processing, Post-Translational
English 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.
Language
  • English
Open access status
bronze
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Persistent URL
https://sonar.ch/global/documents/294394
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