Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

被引：1627

作者：

Honda, R ^{[1
]}

Tanaka, H ^{[1
]}

Yasuda, H ^{[1
]}

机构：

[1] Tokyo Univ Pharm & Life Sci, Sch Life Sci, Tokyo 19203, Japan

来源：

FEBS LETTERS | 1997年 / 420卷 / 01期

关键词：

MDM2; p53; ubiquitin ligase; E6AP; HECT domain;

D O I：

10.1016/S0014-5793(97)01480-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The tumor suppressor p53 is degraded by the ubiquitin-proteasome system. p53 was polyubiquitinated in the presence of E1, UbcH5 as E2 and MDM2 oncoprotein, A ubiquitin molecule bound MDM2 through sulfhydroxy bond which is characteristic of ubiquitin ligase (E3)-ubiquitin binding, The cysteine residue in the carboxyl terminus of MDM2 was essential for the activity, These data suggest that the MDM2 protein, which is induced by p53, functions as a ubiquitin ligase, E3, in human papillomavirus-uninfected cells which do not have E6 protein, (C) 1997 Federation of European Biochemical Societies.

引用

页码：25 / 27

页数：3

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