| Literature DB >> 17229476 |
Joshua D Dowell1, Shih-Chong Tsai, Dora C Dias-Santagata, Hidehiro Nakajima, Zhuo Wang, Wuqiang Zhu, Loren J Field.
Abstract
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.Entities:
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Year: 2006 PMID: 17229476 PMCID: PMC1876763 DOI: 10.1016/j.bbamcr.2006.11.020
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002