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

Pharmaceutical Sciences

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

17 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

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

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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.",

keywords = "Nucleotide excision repair, Single molecule, Structure-function, UV-DDB, XP-E, Xeroderma pigmentosum",

author = "Maria Beecher and Namrata Kumar and Sunbok Jang and Vesna Rapi{\'c}-Otrin and {Van Houten}, Bennett",

note = "Funding Information: We thank Dr. Emily Beckwitt for creating movie 1. We apologize in advance for any work which, due to page limitations, was not directly cited here. This work was supported by NIH grants R01ES019566 (BVH), and R01ES028686 (BVH), and 2P30CA047904 to UPMC Hillman Cancer Center. Publisher Copyright: {\textcopyright} 2020 Elsevier B.V.",

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doi = "10.1016/j.dnarep.2020.102860",

language = "English",

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AU - Beecher, Maria

AU - Kumar, Namrata

AU - Jang, Sunbok

AU - Rapić-Otrin, Vesna

AU - Van Houten, Bennett

N1 - Funding Information: We thank Dr. Emily Beckwitt for creating movie 1. We apologize in advance for any work which, due to page limitations, was not directly cited here. This work was supported by NIH grants R01ES019566 (BVH), and R01ES028686 (BVH), and 2P30CA047904 to UPMC Hillman Cancer Center. Publisher Copyright: © 2020 Elsevier B.V.

PY - 2020/10

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N2 - 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.

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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JO - DNA Repair

JF - DNA Repair

M1 - 102860

ER -

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

Abstract

Keywords

UN SDGs

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