Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 432, Issue 18, Pages 4983-4998Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2020.05.023
Keywords
S-acylation; membrane enzyme; membrane deformation; fatty acids; structure
Categories
Funding
- Intramural Research Program of the National Heart, Lung and Blood Institute
- Eunice Kennedy Shriver National Institute of Child Health and Human Development [ZIA HD008928]
- National Institutes of Health
- EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT [ZIAHD008928] Funding Source: NIH RePORTER
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S-acylation, whereby a fatty acid chain is covalently linked to a cysteine residue by a thioester linkage, is the most prevalent kind of lipid modification of proteins. Thousands of proteins are targets of this post-translational modification, which is catalyzed by a family of eukaryotic integral membrane enzymes known as DHHC protein acyltransferases (DHHC-PATs). Our knowledge of the repertoire of S-acylated proteins has been rapidly expanding owing to development of the chemoproteomic techniques. There has also been an increasing number of reports in the literature documenting the importance of S-acylation in human physiology and disease. Recently, the first atomic structures of two different DHHC-PATs were determined using X-ray crystallography. This review will focus on the insights gained into the molecular mechanism of DHHC-PATs from these structures and highlight representative data from the biochemical literature that they help explain. Published by Elsevier Ltd.
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