Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes.

ABSTRACT: Protein S-acylation (palmitoylation), a reversible post-translational modification, is critically involved in regulating protein subcellular localization, activity, stability, and multimeric complex assembly. However, proteome scale characterization of S-acylation has lagged far behind that of phosphorylation, and global analysis of the localization of S-acylated proteins within different membrane domains has not been reported. Here we describe a novel proteomics approach, designated palmitoyl protein identification and site characterization (PalmPISC), for proteome scale enrichment and characterization of S-acylated proteins extracted from lipid raft-enriched and non-raft membranes. In combination with label-free spectral counting quantitation, PalmPISC led to the identification of 67 kno

SUBMITTER: Yang W 

PROVIDER: S-EPMC2808267 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature