The moonlighting of RAD23 in DNA repair and protein degradation

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Standard

The moonlighting of RAD23 in DNA repair and protein degradation. / Grønbæk-Thygesen, Martin; Kampmeyer, Caroline; Hofmann, Kay; Hartmann-Petersen, Rasmus.

I: Biochimica et Biophysica Acta - Gene Regulatory Mechanisms, Bind 1866, Nr. 2, 194925, 2023.

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Harvard

Grønbæk-Thygesen, M, Kampmeyer, C, Hofmann, K & Hartmann-Petersen, R 2023, 'The moonlighting of RAD23 in DNA repair and protein degradation', Biochimica et Biophysica Acta - Gene Regulatory Mechanisms, bind 1866, nr. 2, 194925. https://doi.org/10.1016/j.bbagrm.2023.194925

APA

Grønbæk-Thygesen, M., Kampmeyer, C., Hofmann, K., & Hartmann-Petersen, R. (2023). The moonlighting of RAD23 in DNA repair and protein degradation. Biochimica et Biophysica Acta - Gene Regulatory Mechanisms, 1866(2), [194925]. https://doi.org/10.1016/j.bbagrm.2023.194925

Vancouver

Grønbæk-Thygesen M, Kampmeyer C, Hofmann K, Hartmann-Petersen R. The moonlighting of RAD23 in DNA repair and protein degradation. Biochimica et Biophysica Acta - Gene Regulatory Mechanisms. 2023;1866(2). 194925. https://doi.org/10.1016/j.bbagrm.2023.194925

Author

Grønbæk-Thygesen, Martin ; Kampmeyer, Caroline ; Hofmann, Kay ; Hartmann-Petersen, Rasmus. / The moonlighting of RAD23 in DNA repair and protein degradation. I: Biochimica et Biophysica Acta - Gene Regulatory Mechanisms. 2023 ; Bind 1866, Nr. 2.

Bibtex

@article{4a961ef18f7c4997855f875bff7882b9,

title = "The moonlighting of RAD23 in DNA repair and protein degradation",

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.",

keywords = "ERAD, Proteasome, Protein degradation, UBA, Ubiquitin, UBL",

author = "Martin Gr{\o}nb{\ae}k-Thygesen and Caroline Kampmeyer and Kay Hofmann and Rasmus Hartmann-Petersen",

note = "Publisher Copyright: {\textcopyright} 2023",

year = "2023",

doi = "10.1016/j.bbagrm.2023.194925",

language = "English",

volume = "1866",

journal = "BBA Gene Regulatory Mechanisms",

issn = "1874-9399",

publisher = "Elsevier",

number = "2",

}

RIS

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

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

Biologisk Institut