MDM2 interacts with MDMX through their RING finger domains

Shyu Tanimura, Satoshi Ohtsuka, Kaoru Mitsui, Kazuo Shirouzu, Akihiko Yoshimura, Motoaki Ohtsubo

Research output: Contribution to journalArticlepeer-review

271 Citations (Scopus)


The N-terminus of MDM2 proto-oncoprotein interacts with p53 and down modulates p53 activity by inhibiting transcriptional activity and promoting p53 degradation. MDMX is structurally related to MDM2 and also binds to p53. However, the function of MDMX has not been clarified yet. We found that MDM2 hetero-oligomerized with MDMX through their C-terminal RING finger domains. Yeast two-hybrid analysis revealed that the hetero-oligomerization between MDMX and MDM2 was more stable than the homo-oligomerization of each protein. MDM2 has been shown to be degraded by the ubiquitin-proteasome pathway, while MDMX was a stable protein. Interaction of MDMX with MDM2 through the C-terminal RING finger domains resulted in inhibiting degradation of MDM2. These data indicate that MDMX functions as a regulator of MDM2. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)5-9
Number of pages5
JournalFEBS Letters
Issue number1
Publication statusPublished - 1999 Mar 19
Externally publishedYes


  • MDM2
  • MDMX
  • RING finger
  • p53

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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