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Related Experiment Videos

MDM2 suppresses p73 function without promoting p73 degradation.

X Zeng1, L Chen, C A Jost

  • 1Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, Oregon 97201, USA.

Molecular and Cellular Biology
|April 17, 1999
PubMed
Summary
This summary is machine-generated.

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The tumor suppressor p73 protein interacts with MDM2, which inhibits p73

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Cellular Biology

Background:

  • The p53 tumor suppressor protein is regulated by MDM2 through a feedback loop.
  • The p53 homolog p73 shares functional similarities with p53, including transcriptional activation.
  • The relationship between p73 and MDM2 in autoregulation is not fully understood.

Purpose of the Study:

  • To investigate if p73, similar to p53, engages in an autoregulatory feedback loop with MDM2.
  • To elucidate the mechanism by which MDM2 might regulate p73 function.

Main Methods:

  • In vivo and in vitro binding assays to assess p73-MDM2 interaction.
  • Transient-transfection and chloramphenicol acetyltransferase (CAT) assays to measure transcriptional activity.
  • Apoptosis assays in p53-null cells to evaluate functional consequences.

Related Experiment Videos

  • Co-immunoprecipitation assays to study protein-protein interactions with p300/CBP.

    • Main Results:

    • p73 directly binds to MDM2.
    • Wild-type MDM2 inhibits p73-dependent transcription and p73-induced apoptosis.
    • MDM2 disrupts the interaction of p73 with p300/CBP by binding to the N terminus of p300/CBP.
    • MDM2 does not promote p73 degradation.
    • Both p73alpha and p73beta stimulate endogenous MDM2 expression.

    Conclusions:

    • MDM2 negatively regulates p73 transcriptional activity and function through a mechanism distinct from p53 inactivation.
    • p73 activates MDM2 transcription, establishing a feedback loop where MDM2 inhibits p73 function.
    • This regulatory mechanism highlights a novel pathway for controlling p73 activity in cancer.