IndraLab

Statements

USP44 deubiquitinates DDB2. 7 / 7
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"USP44 Deubiquitinates and Prevents the Premature Degradation of DDB2."
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"Ubiquitination of DDB2 was reversed by the inclusion of wild-type USP44 but not the catalytically inactive USP44C281A."
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"These data lead us to conclude that USP44 deubiquitinates DDB2 following UV exposure and prevents its premature degradation."
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"One possibility is that USP44 de-ubiquitinates DDB2 once it has been released, allowing it to be recycled back onto persisting CPDs."
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"This indicates that USP44 may regulate the GG-NER pathway by deubiquitylating DDB2 to prevent DDB2-proteasomal degradation and promote the recruitment of XPC [81]."
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"Here we show that the tumor suppressor USP44 directly deubiquitinates DDB2 to prevent its premature degradation and is selectively required for CPD repair."
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"Consistent with the selective CPD repair defect in Usp44 null cells, we find that USP44 deubiquitinates the recognition protein DDB2 to facilitate its accumulation on DNA lesions and facilitate the subsequent recruitment of XPC."
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