FBXO21 mediates the ubiquitylation and proteasomal degradation of EID1.

摘要: Although identification of substrates for ubiquitin ligase (E3) is important understanding its biological functions, detection the interaction between an E3 and has remained challenging. We recently developed a new approach, termed differential proteomics-based ubiquitylation (DiPIUS), discovery given ligase. have now applied this approach to uncharacterized human F-box protein, FBXO21, which serves as substrate-recognition subunit SKP1-CUL1-F-box protein (SCF)-type E3, thereby identifying EID1 (EP300-interacting inhibitor differentiation 1) candidate substrate. The central COOH-terminal portion FBXO21 was found interact with region in transfected cells. Over-expression resulted down-regulation EID1, whereas disruption gene CRISPR/Cas9 system stabilized led accumulation both cytoplasm nucleus. An vitro assay showed that direct substrate SCF(FBXO)(21). Collectively, our results suggest bona fide control abundance by SCF(FBXO)(21) might affect transcriptional repression activity EID1.