Differential effects of SUMO1 and SUMO2 on circadian protein PER2 stability and function.

ABSTRACT: Posttranslational modification (PTM) of core circadian clock proteins, including Period2 (PER2), is required for proper circadian regulation. PER2 function is regulated by casein kinase 1 (CK1)-mediated phosphorylation and ubiquitination but little is known about other PER2 PTMs or their interaction with PER2 phosphorylation. We found that PER2 can be SUMOylated by both SUMO1 and SUMO2; however, SUMO1 versus SUMO2 conjugation had different effects on PER2 turnover and transcriptional suppressor function. SUMO2 conjugation facilitated PER2 interaction with β-TrCP leading to PER2 proteasomal degradation. In contrast, SUMO1 conjugation, mediated by E3 SUMO-protein ligase RanBP2, enhanced CK1-mediated PER2^S662 phosphorylation, inhibited PER2 degradation and increased PER2 transcript

SUBMITTER: Chen LC 

PROVIDER: S-EPMC8277905 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature