Protein S-palmitoylation is a reversible post-translational modification of proteins with fatty acids. In the last 5 years, improved proteomic methods have increased the number of proteins identified as substrates for palmitoylation from tens to hundreds. Palmitoylation regulates protein membrane interactions, activity, trafficking and stability and can be constitutive or regulated by signalling inputs. A family of PATs (protein acyltransferases) is responsible for modifying proteins with palmitate or other long-chain fatty acids on the cytoplasmic face of cellular membranes. PATs share a signature DHHC (Asp-His-His-Cys) cysteine-rich domain that is the catalytic centre of the enzyme. The biomedical importance of members of this family is underscored by their association with intellectual disability, Huntington's disease and cancer in humans, and raises the possibility of DHHC PATs as targets for therapeutic intervention. In the present paper, we discuss recent progress in understanding enzyme mechanism, regulation and substrate specificity.
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Conference Article|
January 29 2013
Mechanism and function of DHHC S-acyltransferases
Maurine E. Linder;
Maurine E. Linder
1
1Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, U.S.A.
1To whom correspondence should be addressed (email[email protected]).
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Benjamin C. Jennings
Benjamin C. Jennings
1Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, U.S.A.
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Publisher: Portland Press Ltd
Received:
November 06 2012
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2013 Biochemical Society
2013
Biochem Soc Trans (2013) 41 (1): 29–34.
Article history
Received:
November 06 2012
Citation
Maurine E. Linder, Benjamin C. Jennings; Mechanism and function of DHHC S-acyltransferases. Biochem Soc Trans 1 February 2013; 41 (1): 29–34. doi: https://doi.org/10.1042/BST20120328
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