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

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• 作者：Joshua D. Dowell ; Shih-Chong Tsai ; Dora C. Dias-Santagata ; Hidehiro Nakajima ; Zhuo Wang ; Wuqiang Zhu ; Loren J. Field
• 关键词：E3 ligase ; BH-3 only ; SV40 T-Antigen
• 刊名：Biochimica et Biophysica Acta (BBA)/Molecular Cell Research
• 出版年：2007
• 出版时间：March 2007
• 年：2007
• 卷：1773
• 期：3
• 页码：358-366
• 全文大小：725 K

文摘

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.