USP2a protein deubiquitinates and stabilizes the circadian protein CRY1 in response to inflammatory signals.

ABSTRACT: The mammalian circadian clock coordinates various physiological activities with environmental cues to achieve optimal adaptation. The clock manifests oscillations of key clock proteins, which are under dynamic control at multiple post-translational levels. As a major post-translational regulator, the ubiquitination-dependent proteasome degradation system is counterbalanced by a large group of deubiquitin proteases with distinct substrate preference. Until now, whether deubiquitination by ubiquitin-specific proteases can regulate the clock protein stability and circadian pathways remains largely unclear. The mammalian clock protein, cryptochrome 1 (CRY1), is degraded via the FBXL3-mediated ubiquitination pathway, suggesting that it is also likely to be targeted by the deubiquitination pathw

SUBMITTER: Tong X 

PROVIDER: S-EPMC3408137 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature