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The deubiquitinating protein USP24 interacts with DDB2 and regulates DDB2 stability

29 Nov 2012

Abstract excerpt

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...

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PMID: 23159851
DOI: 10.4161/cc.22688

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The deubiquitinating protein USP24 interacts with DDB2 and regulates DDB2 stabilityPMID 23159851Read ↗

DDB2, the xeroderma pigmentosum group E gene product, is directly ubiquitylated by Cullin 4A-based ubiquitin ligase complex.Semantic proximity Read ↗

The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites.Semantic proximity Read ↗

DDB2 association with PCNA is required for its degradation after UV-induced DNA damage.Semantic proximity Read ↗

DDB2 complex-mediated ubiquitylation around DNA damage is oppositely regulated by XPC and Ku and contributes to the recruitment of XPA.Semantic proximity Read ↗

The xeroderma pigmentosum group E gene product DDB2 is a specific target of cullin 4A in mammalian cells.Semantic proximity Read ↗

DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound lesions in DNA.Semantic proximity Read ↗

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Emerging Roles of DDB2 in CancerSemantic proximity Read ↗

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