Revealing the dynamics of the 20 S proteasome phosphoproteome: a combined CID and electron transfer dissociation approach.

ABSTRACT: The 20 S proteasomes play a critical role in intracellular homeostasis and stress response. Their function is tuned by covalent modifications, such as phosphorylation. In this study, we performed a comprehensive characterization of the phosphoproteome for the 20 S proteasome complexes in both the murine heart and liver. A platform combining parallel approaches in differential sample fractionation (SDS-PAGE, IEF, and two-dimensional electrophoresis), enzymatic digestion (trypsin and chymotrypsin), phosphopeptide enrichment (TiO(2)), and peptide fragmentation (CID and electron transfer dissociation (ETD)) has proven to be essential for identifying low abundance phosphopeptides. As a result, a total of 52 phosphorylation identifications were made in mammalian tissues; 44 of them were novel. T

SUBMITTER: Lu H 

PROVIDER: S-EPMC2577207 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature