The deubiquitinating protein USP24 interacts with DDB2 and regulates DDB2 stability

Ling Zhang, Abigail Lubin, Hua Chen, Zhongyi Sun, Feng Gong

Research output: Contribution to journalArticlepeer-review

34 Scopus citations


Damage-specific DNA-binding protein 2 (DDB2) was first isolated as a subunit of the UV-DDB heterodimeric complex that is involved in DNA damage recognition in the nucleotide excision repair pathway (NER). DDB2 is required for efficient repair of CPDs in chromatin and is a component of the CRL4 DDB2 E3 ligase that targets XPC, histones and DDB2 itself for ubiquitination. In this study, a yeast two-hybrid screening of a human cDNA library was performed to identify potential DDB2 cellular partners. We identified a deubiquitinating enzyme, USP24, as a likely DDB2-interacting partner. Interaction between DDB2 and USP24 was confirmed by co-precipitation. Importantly, knockdown of USP24 in two human cell lines decreased the steady-state levels of DDB2, indicating that USP24-mediated DDB2 deubiquitination prevents DDB2 degradation. In addition, we demonstrated that USP24 can cleave an ubiquitinated form of DDB2 in vitro. Taken together, our results suggest that the ubiquitin-specific protease USP24 is a novel regulator of DDB2 stability.

Original languageEnglish (US)
Pages (from-to)4378-4384
Number of pages7
JournalCell Cycle
Issue number23
StatePublished - Dec 1 2012


  • DDB2
  • Deubiquitinase
  • Deubiquitination
  • Nucleotide excision repair
  • USP24
  • UV-DDB
  • XPE
  • Yeast two-hybrid

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Developmental Biology


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