RNF34 is a cold-regulated E3 ubiquitin ligase for PGC-1α and modulates brown fat cell metabolism.

ABSTRACT: The transcriptional coactivator PGC-1α is a master regulator of energy metabolism and adaptive thermogenesis in the brown fat cell. PGC-1α is a short-lived protein, and the molecular components that control PGC-1α turnover and their functional importance in energy metabolism are largely unknown. Here we performed a luciferase-based overexpression screen and identified a Ring-finger-containing protein, RNF34, as a specific E3 ubiquitin ligase for PGC-1α. RNF34 is a nuclear protein that interacts with and ubiquitinates PGC-1α to promote its turnover. Interestingly, RNF34 binds to the C-terminal half of PGC-1α and targets it for degradation independently of the previously identified N-terminal phosphodegron motif. In brown fat cells, knockdown of RNF34 increases the endogenous PGC-1α protein

SUBMITTER: Wei P 

PROVIDER: S-EPMC3255768 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature