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Hip2 与 Smac/DIABLO 相互作用并使其不稳定。

Hip2 interacts with and destabilizes Smac/DIABLO.

机构信息

Graduate School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.

出版信息

Biochem Biophys Res Commun. 2010 Jul 9;397(4):718-23. doi: 10.1016/j.bbrc.2010.06.016. Epub 2010 Jun 9.

DOI:10.1016/j.bbrc.2010.06.016
PMID:20537984
Abstract

Hip2 is a ubiquitin-conjugating enzyme that is involved in the cell cycle and suppression of cell death. To understand its role further, we tried to identify proteins that interact with Hip2. Using the immunoprecipitation technique and one-dimensional gel electrophoresis, we identified Smac/DIABLO, a proapoptotic molecule, as a protein that interacts with Hip2. The interaction of Hip2 and Smac was confirmed through in vivo and in vitro experiments. Hip2 promoted degradation of mature Smac through the ubiquitin proteasome pathway. As a result, Hip2 significantly blocked cell death induced by staurosporine and Smac. This study suggests that Hip2 might be involved in the regulation of Smac-mediated apoptosis.

摘要

Hip2 是一种泛素连接酶,参与细胞周期和细胞死亡的抑制。为了进一步了解其作用,我们试图鉴定与 Hip2 相互作用的蛋白质。使用免疫沉淀技术和一维凝胶电泳,我们鉴定出 Smac/DIABLO,一种促凋亡分子,是与 Hip2 相互作用的蛋白质。Hip2 和 Smac 的相互作用通过体内和体外实验得到证实。Hip2 通过泛素蛋白酶体途径促进成熟 Smac 的降解。结果,Hip2 显著阻断了 staurosporine 和 Smac 诱导的细胞死亡。这项研究表明,Hip2 可能参与了 Smac 介导致凋亡的调节。

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