Large-scale characterization of HeLa cell nuclear phosphoproteins.

ABSTRACT: Determining the site of a regulatory phosphorylation event is often essential for elucidating specific kinase-substrate relationships, providing a handle for understanding essential signaling pathways and ultimately allowing insights into numerous disease pathologies. Despite intense research efforts to elucidate mechanisms of protein phosphorylation regulation, efficient, large-scale identification and characterization of phosphorylation sites remains an unsolved problem. In this report we describe an application of existing technology for the isolation and identification of phosphorylation sites. By using a strategy based on strong cation exchange chromatography, phosphopeptides were enriched from the nuclear fraction of HeLa cell lysate. From 967 proteins, 2,002 phosphorylation sites we

SUBMITTER: Beausoleil SA 

PROVIDER: S-EPMC514446 | biostudies-literature | 2004 Aug

REPOSITORIES: biostudies-literature