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Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
Author(s) -
Honda Reiko,
Tanaka Hirofumi,
Yasuda Hideyo
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01480-4
Subject(s) - ubiquitin ligase , mdm2 , ubiquitin , suppressor , dna ligase , proteasome , ddb1 , ubiquitin protein ligases , biology , ubiquitin conjugating enzyme , cysteine , microbiology and biotechnology , chemistry , biochemistry , cancer research , enzyme , gene
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.