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Protein S-palmitoylation in cellular differentiation.
Zhang, Mingzi M; Hang, Howard C.
Affiliation
  • Zhang MM; Metabolic Engineering Research Laboratory, Science and Engineering Institutes, Agency for Science, Technology and Research, Singapore.
  • Hang HC; Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY, U.S.A. hhang@rockefeller.edu.
Biochem Soc Trans ; 45(1): 275-285, 2017 02 08.
Article in En | MEDLINE | ID: mdl-28202682
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.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Palmitates / Cell Differentiation / Protein Processing, Post-Translational / Cysteine Limits: Animals / Humans Language: En Journal: Biochem Soc Trans Year: 2017 Document type: Article Affiliation country: Singapore Country of publication: United kingdom

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Palmitates / Cell Differentiation / Protein Processing, Post-Translational / Cysteine Limits: Animals / Humans Language: En Journal: Biochem Soc Trans Year: 2017 Document type: Article Affiliation country: Singapore Country of publication: United kingdom