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Deubiquitylase USP7 regulates human terminal erythroid differentiation by stabilizing GATA1.


ABSTRACT: Ubiquitination is an enzymatic post-translational modification that affects protein fate. The ubiquitin-proteasome system (UPS) was first discovered in reticulocytes where it plays important roles in reticulocyte maturation. Recent studies have revealed that ubiquitination is a dynamic and reversible process and that deubiquitylases are capable of removing ubiquitin from their protein substrates. Given the fact that the UPS is highly active in reticulocytes, it is speculated that deubiquitylases may play important roles in erythropoiesis. Yet, the role of deubiquitylases in erythropoiesis remains largely unexplored. In the present study, we found that the expression of deubiquitylase USP7 is significantly increased during human terminal erythroid differentiation. We further showed that int

SUBMITTER: Liang L 

PROVIDER: S-EPMC6821630 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

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