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• W4322625660 endingPage "194925" @default.
• W4322625660 startingPage "194925" @default.
• W4322625660 abstract "A moonlighting protein is one, which carries out multiple, often wholly unrelated, functions. The RAD23 protein is a fascinating example of this, where the same polypeptide and the embedded domains function independently in both nucleotide excision repair (NER) and protein degradation via the ubiquitin-proteasome system (UPS). Hence, through direct binding to the central NER component XPC, RAD23 stabilizes XPC and contributes to DNA damage recognition. Conversely, RAD23 also interacts directly with the 26S proteasome and ubiquitylated substrates to mediate proteasomal substrate recognition. In this function, RAD23 activates the proteolytic activity of the proteasome and engages specifically in well-characterized degradation pathways through direct interactions with E3 ubiquitin-protein ligases and other UPS components. Here, we summarize the past 40 years of research into the roles of RAD23 in NER and the UPS." @default.
• W4322625660 created "2023-03-01" @default.
• W4322625660 creator A5008208128 @default.
• W4322625660 creator A5015519563 @default.
• W4322625660 creator A5016385969 @default.
• W4322625660 creator A5072786803 @default.
• W4322625660 date "2023-06-01" @default.
• W4322625660 modified "2023-10-15" @default.
• W4322625660 title "The moonlighting of RAD23 in DNA repair and protein degradation" @default.
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