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Biochem Soc Trans. 2017 Feb 8;45(1):275-285. doi: 10.1042/BST20160236.

Protein S-palmitoylation in cellular differentiation.

Author information

1
Metabolic Engineering Research Laboratory, Science and Engineering Institutes, Agency for Science, Technology and Research, Singapore.
2
Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY, U.S.A. hhang@rockefeller.edu.

Abstract

Reversible protein S-palmitoylation confers spatiotemporal control of protein function by modulating protein stability, trafficking and activity, as well as protein-protein and membrane-protein associations. Enabled by technological advances, global studies revealed S-palmitoylation to be an important and pervasive posttranslational modification in eukaryotes with the potential to coordinate diverse biological processes as cells transition from one state to another. Here, we review the strategies and tools to analyze in vivo protein palmitoylation and interrogate the functions of the enzymes that put on and take off palmitate from proteins. We also highlight palmitoyl proteins and palmitoylation-related enzymes that are associated with cellular differentiation and/or tissue development in yeasts, protozoa, mammals, plants and other model eukaryotes.

KEYWORDS:

S-palmitoylation; cellular differentiation; fatty-acylation; lipidation; posttranslational modification

PMID:
28202682
PMCID:
PMC5310721
DOI:
10.1042/BST20160236
[Indexed for MEDLINE]
Free PMC Article

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