Protein kinase g positively regulates proteasome-mediated degradation of misfolded proteins.

ABSTRACT:

Background

Proteasome functional insufficiency is implicated in a large subset of cardiovascular diseases and may play an important role in their pathogenesis. The regulation of proteasome function is poorly understood, hindering the development of effective strategies to improve proteasome function.

Methods and results

Protein kinase G (PKG) was manipulated genetically and pharmacologically in cultured cardiomyocytes. Activation of PKG increased proteasome peptidase activities, facilitated proteasome-mediated degradation of surrogate (enhanced green fluorescence protein modified by carboxyl fusion of degron CL1) and bona fide (CryAB(R120G)) misfolded proteins, and attenuated CryAB(R120G) overexpression-induced accumulation of ubiquitinated proteins and cellular injury. PKG

SUBMITTER: Ranek MJ 

PROVIDER: S-EPMC3761383 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature