Abstract
Deubiquitination via deubiquitinating enzymes (DUBs) has been emerged as one of the important post-translational modifications, resulting in the regulation of numerous target proteins. In this study, we screened new protein biomarkers for adipogenesis, and related studies showed that ubiquitin specific protease 19 (USP19) as a DUB is gradually decreased during adipogenesis and it regulates coronin 2A (CORO2A) as one of the components for the nuclear receptor co-repressor (NCoR) complex in some studies. The regulation of CORO2A through the deubiquitinating activity of USP19 affected the transcriptional repression activity of the retinoic acid receptor (RAR), suggesting that USP19 may be involved in the regulation of RAR-mediated adipogenesis.
Highlights
Deubiquitination is the opposite process of ubiquitination and is mediated by deubiquitinating enzymes (DUBs) [1]
The results suggest that ubiquitin specific protease 19 (USP19) may be associated with the transcriptional regulation of retinoic acid receptor (RAR) via coronin 2A (CORO2A) as one of the components for the nuclear receptor co-repressor (NCoR) complex during the adipogenesis
These findings suggest that the transcription levels of USP19, USP42, and USP54 were changed during adipogenesis
Summary
Deubiquitination is the opposite process of ubiquitination and is mediated by deubiquitinating enzymes (DUBs) [1]. DUBs have the ability to detach ubiquitin molecules from ubiquitinated substrates, changing the fate of these substrates, including their activity or stabilization. DUBs have been thought to be pivotal mediators in diverse cellular systems including signal transduction, cell cycle regulation, cell proliferation, and cell death [2]. Several studies have suggested that USP19 has diverse roles in cellular processes, including cell cycle regulation, the response to hypoxia, and muscle atrophy [3,4,5]. USP19 was shown to be involved in the unfolded protein response (UPR) and in the ER-associated degradation (ERAD) pathway [7]. These results indicate that USP19 can mediate a variety of mechanisms within cells
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