The moonlighting of RAD23 in DNA repair and protein degradation

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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.
TidsskriftBiochimica et Biophysica Acta - Gene Regulatory Mechanisms
Udgave nummer2
Antal sider16
StatusUdgivet - 2023

Bibliografisk note

Funding Information:
We are supported by grants from Novo Nordisk Foundation ( ) challenge programme PRISM ( NNF18OC0033950 ), REPIN ( NNF18OC0033926 ), and NNF21OC0071057 , the Independent Research Fund Denmark ( Natur og Univers, Det Frie Forskningsråd ) ( ) 10.46540/2032-00007B , and the Villum Foundation ( ) 40526 . The funders had no role in the preparation of the manuscript or decision to publish.

Publisher Copyright:
© 2023

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