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We have identified a novel component of the circadian clock that regulates its sensitivity to light at the evening light to dark transition. USP2 (  U  biquitin   S  pecific   P  rotease   2  ), which de-ubiquitinylates and stabilizes target proteins, is rhythmically expressed in multiple tissues including the SCN. We have developed a knockout model of USP2 and found that exposure to low irradiance light at ZT12 increases phase delays of USP2 −/−  mice compared to wildtype. We additionally show that USP2b is in a complex with several clock components and regulates the stability and turnover of BMAL1, which in turn alters the expression of several CLOCK/BMAL1 controlled genes. Rhythmic expression of USP2 in the SCN and other tissues offers a new level of control of the clock machinery through de-ubiqutinylation and suggests a role for USP2 during circadian adaptation to environmental day length changes.

The De-Ubiquitinylating Enzyme, USP2, Is Associated with the Circadian Clockwork and Regulates Its Sensitivity to Light