Expression of a mutant p193/CUL7 molecule confers resistance to MG132- and etoposide-induced apoptosis independent of p53 or Parc binding.
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.
Mesh Terms:
Animals, Antibodies, Monoclonal, Apoptosis, Cell Line, Cullin Proteins, Cytoplasm, DNA Topoisomerase IV, Drug Resistance, Enzyme Activation, Etoposide, Gene Expression, Humans, Leupeptins, Mice, Mutation, Proteasome Endopeptidase Complex, Protein Binding, Tumor Suppressor Protein p53
Animals, Antibodies, Monoclonal, Apoptosis, Cell Line, Cullin Proteins, Cytoplasm, DNA Topoisomerase IV, Drug Resistance, Enzyme Activation, Etoposide, Gene Expression, Humans, Leupeptins, Mice, Mutation, Proteasome Endopeptidase Complex, Protein Binding, Tumor Suppressor Protein p53
Biochim. Biophys. Acta
Date: Mar. 01, 2007
PubMed ID: 17229476
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