The moonlighting of RAD23 in DNA repair and protein degradation
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The moonlighting of RAD23 in DNA repair and protein degradation. / Grønbæk-Thygesen, Martin; Kampmeyer, Caroline; Hofmann, Kay; Hartmann-Petersen, Rasmus.
In: Biochimica et Biophysica Acta - Gene Regulatory Mechanisms, Vol. 1866, No. 2, 194925, 2023.Research output: Contribution to journal › Review › Research › peer-review
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TY - JOUR
T1 - The moonlighting of RAD23 in DNA repair and protein degradation
AU - Grønbæk-Thygesen, Martin
AU - Kampmeyer, Caroline
AU - Hofmann, Kay
AU - Hartmann-Petersen, Rasmus
N1 - Publisher Copyright: © 2023
PY - 2023
Y1 - 2023
N2 - 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.
AB - 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.
KW - ERAD
KW - Proteasome
KW - Protein degradation
KW - UBA
KW - Ubiquitin
KW - UBL
U2 - 10.1016/j.bbagrm.2023.194925
DO - 10.1016/j.bbagrm.2023.194925
M3 - Review
C2 - 36863450
AN - SCOPUS:85149270966
VL - 1866
JO - BBA Gene Regulatory Mechanisms
JF - BBA Gene Regulatory Mechanisms
SN - 1874-9399
IS - 2
M1 - 194925
ER -
ID: 338981771