Expression of a mutant p193/CUL7 molecule confers resistance to MG132- and etoposide-induced apoptosis independent of p53 or Parc binding

Joshua D. Dowell, Shih Chong Tsai, Dora C. Dias-Santagata, Hidehiro Nakajima, Zhuo Wang, Wuqiang Zhu, Loren J. Field

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9 Scopus citations


p193/CUL7 is an E3 ubiquitin ligase initially identified as an SV40 Large T Antigen binding protein. Expression of a dominant interfering variant of mouse p193/CUL7 (designated 1152stop) conferred resistance to MG132- and etoposide-induced apoptosis in U2OS cells. Immune precipitation/Western analyses revealed that endogenous p193/CUL7 formed a complex with Parc (a recently identified parkin-like ubiquitin ligase) and p53. Apoptosis resistance did not result from 1152stop-mediated disruption of the endogenous p193/CUL7 binding partners. Moreover, 1152stop molecule did not directly bind to endogenous p193/CUL7, Parc or p53. These data suggested a role for p193/CUL7 in the regulation of apoptosis independently of p53 and Parc activity.

Original languageEnglish (US)
Pages (from-to)358-366
Number of pages9
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Issue number3
StatePublished - Mar 1 2007



  • BH-3 only
  • E3 ligase
  • SV40 T-Antigen

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Biophysics

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