Expression of a mutant p193/CUL7 molecule confers resistance to MG132- and etoposide-induced apoptosis independent of p53 or Parc binding
| Autor: | Dora Dias-Santagata, Zhuo Wang, Shih Chong Tsai, Loren J. Field, Joshua D. Dowell, Hidehiro Nakajima, Wuqiang Zhu |
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| Rok vydání: | 2007 |
| Předmět: |
DNA Topoisomerase IV
Cytoplasm Proteasome Endopeptidase Complex Leupeptins Mutant Drug Resistance Gene Expression Apoptosis Plasma protein binding Article Cell Line Mice chemistry.chemical_compound Enzyme activator BH-3 only MG132 Gene expression Animals Humans Molecular Biology E3 ligase Etoposide biology Binding protein Antibodies Monoclonal Cell Biology Cullin Proteins Molecular biology Ubiquitin ligase Enzyme Activation chemistry Mutation SV40 T-Antigen biology.protein Tumor Suppressor Protein p53 Proteasome Inhibitors Protein Binding |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1773:358-366 |
| ISSN: | 0167-4889 |
| DOI: | 10.1016/j.bbamcr.2006.11.020 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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