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ACS Chem Biol. 2013 Jan 18;8(1):46-57. doi: 10.1021/cb300607e. Epub 2012 Dec 18.

Fat chance! Getting a grip on a slippery modification.

Author information

1
Program in Chemical Biology and Department of Chemistry, University of Michigan, 930 N University Avenue, Ann Arbor, Michigan 48109, United States.

Abstract

Protein palmitoylation describes the post-translational fatty acyl thioesterification of cellular cysteine residues and is critical for the localization, trafficking, and compartmentalization of a large number of membrane proteins. This labile thioester modification facilitates a dynamic acylation cycle that directionally traffics key signaling complexes, receptors, and channels to select membrane compartments. Chemical enrichment and advanced mass spectrometry-based proteomics methods have highlighted a pervasive role for palmitoylation across all eukaryotes, including animals, plants, and parasites. Emerging chemical tools promise to open new avenues to study the enzymes, substrates, and dynamics of this distinct post-translational modification.

PMID:
23215442
PMCID:
PMC3693556
DOI:
10.1021/cb300607e
[Indexed for MEDLINE]
Free PMC Article

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