Two-dimensional electrophoresis-based characterization of post-translational modifications of mammalian 20S proteasome complexes.

ABSTRACT: PTMs serve as key regulatory mechanisms for 20S proteasome functions. Alterations in 20S PTMs have been previously observed with changes in modified protein degradation patterns and altered cellular phenotypes. Despite decades of investigation, our knowledge pertaining to the various PTMs of 20S complexes and their biological significance remain limited. In this investigation, we show that 2-DE offers an analytical tool with high resolution and reproducibility. Accordingly, it has been applied for the characterization of PTMs including glycosylation, phosphorylation, oxidation, and nitrosylation. The PTMs of murine cardiac 20S proteasomes and their associating proteins were examined. Our 2-DE analyses displayed over 25 spots for the 20S complexes (17 subunits), indicating multiply modified

SUBMITTER: Zong C 

PROVIDER: S-EPMC2674022 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature