Journal
EXPERIMENTAL BIOLOGY AND MEDICINE
Volume 242, Issue 11, Pages 1150-1157Publisher
SAGE PUBLICATIONS LTD
DOI: 10.1177/1535370217707732
Keywords
Lipidation; S-palmitoylation; protein acyl transferases; aspartate-histidine-histidine-cysteine protein; depalmitoylation; palmitoyltransferases
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Funding
- National Science Centre, Poland (Narodowe Centrum Nauki, Polska) via a postdoctoral research grant [DEC-2014/12/S/NZ1/00604]
- NCN [DEC-2012/05/B/NZ1/01638]
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A plethora of novel information has emerged over the past decade regarding protein lipidation. The reversible attachment of palmitic acid to cysteine residues, termed S-palmitoylation, has focused a special attention. This is mainly due to the unique role of this modification in the regulation of protein trafficking and function. A large family of protein acyltransferases (PATs) containing a conserved aspartate-histidine-histidine-cysteine motif use ping-pong kinetic mechanism to catalyze S-palmitoylation of a substrate protein. Here, we discuss the topology of PAT proteins and their cellular localization. We will also give an overview of the mechanism of protein palmitoylation and how it is regulated. New information concerning the recent discovery of depalmitoylating enzymes belonging to the family of /-hydrolase domain-containing protein 17 (ABHD17A) is included. Considering the recent advances that have occurred in understanding the mechanisms underlying the interplay between palmitoylation and depalmitoylation, it is clear that we are beginning to understand the fundamental nature of how cellular signal-transduction mediates membrane-level organization in health and disease.
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