Oxygen-dependent asparagine hydroxylation of the ubiquitin-associated (UBA) domain in Cezanne regulates ubiquitin binding
Deubiquitinases (DUBs) are vital for the regulation of ubiquitin signals, and both catalytic
activity of and target recruitment by DUBs need to be tightly controlled. Here, we identify
asparagine hydroxylation as a novel posttranslational modification involved in the regulation
of Cezanne (also known as OTU domain–containing protein 7B (OTUD7B)), a DUB that
controls key cellular functions and signaling pathways. We demonstrate that Cezanne is a
substrate for factor inhibiting HIF1 (FIH1)-and oxygen-dependent asparagine hydroxylation …
activity of and target recruitment by DUBs need to be tightly controlled. Here, we identify
asparagine hydroxylation as a novel posttranslational modification involved in the regulation
of Cezanne (also known as OTU domain–containing protein 7B (OTUD7B)), a DUB that
controls key cellular functions and signaling pathways. We demonstrate that Cezanne is a
substrate for factor inhibiting HIF1 (FIH1)-and oxygen-dependent asparagine hydroxylation …
