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DCAF7 is required for maintaining the cellular levels of ERCC1-XPF and nucleotide excision repair

Kawara, Hiroaki ; Akahori, Ryo ; Wakasugi, Mitsuo ; Sancar, Aziz ; Matsunaga, Tsukasa

Biochemical and biophysical research communications, 2019-10, Vol.519 (1), p.204-210 [Periódico revisado por pares]

United States: Elsevier Inc

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  • Título:
    DCAF7 is required for maintaining the cellular levels of ERCC1-XPF and nucleotide excision repair
  • Autor: Kawara, Hiroaki ; Akahori, Ryo ; Wakasugi, Mitsuo ; Sancar, Aziz ; Matsunaga, Tsukasa
  • Assuntos: Adaptor Proteins, Signal Transducing - metabolism ; Cell Line ; DCAF7/WDR68/HAN11 ; DNA Repair ; DNA-Binding Proteins - metabolism ; Down-Regulation ; Endonucleases - metabolism ; ERCC1-XPF ; Humans ; Nucleotide excision repair ; Proteasome Endopeptidase Complex - metabolism ; Protein Binding ; Protein Multimerization ; TRiC/CCT
  • É parte de: Biochemical and biophysical research communications, 2019-10, Vol.519 (1), p.204-210
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
  • Descrição: The ERCC1-XPF heterodimer is a structure-specific endonuclease and plays multiple roles in various DNA repair pathways including nucleotide excision repair and also telomere maintenance. The dimer formation, which is mediated by their C-terminal helix-hairpin-helix regions, is essential for their endonuclease activity as well as the stability of each protein. However, the detailed mechanism of how a cellular level of ERCC1-XPF is regulated still remains elusive. Here, we report the identification of DDB1- and CUL4-associated factor 7 (DCAF7, also known as WDR68/HAN11) as a novel interacting protein of ERCC1-XPF by mass spectrometry after tandem purification. Immunoprecipitation experiments confirmed their interaction and suggested dominant association of DCAF7 with XPF but not ERCC1. Interestingly, siRNA-mediated knockdown of DCAF7, but not DDB1, attenuated the cellular level of ERCC1-XPF, which is partly dependent on proteasome. The depletion of TCP1α, one of components of the molecular chaperon TRiC/CCT known to interact with DCAF7 and promote its folding, also reduced ERCC1-XPF level. Finally, we show that the depletion of DCAF7 causes inefficient repair of UV-induced (6–4) photoproducts, which can be rescued by ectopic overexpression of XPF or ERCC1-XPF. Altogether, our results strongly suggest that DCAF7 is a novel regulator of ERCC1-XPF protein level and cellular nucleotide excision repair activity. [Display omitted] •DCAF7 was identified as a novel ERCC1-XPF interactor by proteomic analysis.•DCAF7 interacts with ERCC1-XPF heterodimer via its association with XPF.•DCAF7 depletion by siRNA downregulates the cellular level of ERCC1-XPF, which is partly dependent on proteasome.•Knockdown of TCP1α, a component of TRiC/CCT, also reduces cellular ERCC1-XPF level.•DCAF7-depleted cells show impaired nucleotide excision repair ability.
  • Editor: United States: Elsevier Inc
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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