Expanding molecular roles of UV-DDB: Shining light on genome stability and cancer

Maria Beecher; Namrata Kumar; Sunbok Jang; Vesna Rapić-Otrin; Bennett Van Houten

doi:10.1016/j.dnarep.2020.102860

Expanding molecular roles of UV-DDB: Shining light on genome stability and cancer

Maria Beecher, Namrata Kumar, Sunbok Jang, Vesna Rapić-Otrin, Bennett Van Houten

Department of Pharmaceutical Sciences

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

Abstract

UV-damaged DNA binding protein (UV-DDB) is a heterodimeric complex, composed of DDB1 and DDB2, and is involved in global genome nucleotide excision repair. Mutations in DDB2 are associated with xeroderma pigmentosum complementation group E. UV-DDB forms a ubiquitin E3 ligase complex with cullin-4A and RBX that helps to relax chromatin around UV-induced photoproducts through the ubiquitination of histone H2A. After providing a brief historical perspective on UV-DDB, we review our current knowledge of the structure and function of this intriguing repair protein. Finally, this article discusses emerging data suggesting that UV-DDB may have other non-canonical roles in base excision repair and the etiology of cancer.

Original language	English
Article number	102860
Journal	DNA Repair
Volume	94
DOIs	https://doi.org/10.1016/j.dnarep.2020.102860
State	Published - Oct 2020

Bibliographical note

Publisher Copyright:
© 2020 Elsevier B.V.

Keywords

Nucleotide excision repair
Single molecule
Structure-function
UV-DDB
XP-E
Xeroderma pigmentosum

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.dnarep.2020.102860

Cite this

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title = "Expanding molecular roles of UV-DDB: Shining light on genome stability and cancer",

abstract = "UV-damaged DNA binding protein (UV-DDB) is a heterodimeric complex, composed of DDB1 and DDB2, and is involved in global genome nucleotide excision repair. Mutations in DDB2 are associated with xeroderma pigmentosum complementation group E. UV-DDB forms a ubiquitin E3 ligase complex with cullin-4A and RBX that helps to relax chromatin around UV-induced photoproducts through the ubiquitination of histone H2A. After providing a brief historical perspective on UV-DDB, we review our current knowledge of the structure and function of this intriguing repair protein. Finally, this article discusses emerging data suggesting that UV-DDB may have other non-canonical roles in base excision repair and the etiology of cancer.",

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T2 - Shining light on genome stability and cancer

AU - Beecher, Maria

AU - Kumar, Namrata

AU - Jang, Sunbok

AU - Rapić-Otrin, Vesna

AU - Van Houten, Bennett

PY - 2020/10

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AB - UV-damaged DNA binding protein (UV-DDB) is a heterodimeric complex, composed of DDB1 and DDB2, and is involved in global genome nucleotide excision repair. Mutations in DDB2 are associated with xeroderma pigmentosum complementation group E. UV-DDB forms a ubiquitin E3 ligase complex with cullin-4A and RBX that helps to relax chromatin around UV-induced photoproducts through the ubiquitination of histone H2A. After providing a brief historical perspective on UV-DDB, we review our current knowledge of the structure and function of this intriguing repair protein. Finally, this article discusses emerging data suggesting that UV-DDB may have other non-canonical roles in base excision repair and the etiology of cancer.

KW - Nucleotide excision repair

KW - Single molecule

KW - Structure-function

KW - UV-DDB

KW - XP-E

KW - Xeroderma pigmentosum

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Expanding molecular roles of UV-DDB: Shining light on genome stability and cancer

Abstract

Bibliographical note

Keywords

UN SDGs

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