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

Research output: Contribution to journalArticlepeer-review

23 Scopus citations


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 languageEnglish
Article number102860
JournalDNA Repair
StatePublished - Oct 2020

Bibliographical 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:
© 2020 Elsevier B.V.


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


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