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Related Experiment Videos

CYFIP2, a direct p53 target, is leptomycin-B sensitive.

Roger S Jackson1, Yong-Jig Cho, Susanne Stein

  • 1Vanderbilt-Ingram Comprehensive Cancer Center, Department of Cancer Biology, Vanderbilt University Medical Center, Nashville, Tennessee 37232-6840, USA.

Cell Cycle (Georgetown, Tex.)
|January 25, 2007
PubMed
Summary
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The tumor suppressor p53 induces apoptosis through target genes. Researchers identified Cytoplasmic FMR Interacting Protein 2 (CYFIP2) as a direct p53 target gene involved in this process.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Cancer Research

Background:

  • The tumor suppressor p53 plays a critical role in apoptosis, but its target genes and mechanisms are not fully understood.
  • Identifying novel p53 target genes is crucial for elucidating p53-dependent apoptotic pathways.

Purpose of the Study:

  • To identify novel p53 target genes involved in apoptosis.
  • To investigate the role of Cytoplasmic FMR Interacting Protein 2 (CYFIP2) in p53-mediated apoptosis.

Main Methods:

  • Comprehensive screening for p53 target genes.
  • Analysis of the CYFIP2 promoter for p53-responsive elements.
  • Reporter assays to confirm transcriptional activation.
  • Inducible expression of CYFIP2 to assess apoptosis.

Related Experiment Videos

  • Investigation of CYFIP2 subcellular localization using Leptomycin-B.

    • Main Results:

    • Cytoplasmic FMR Interacting Protein 2 (CYFIP2) was identified as a p53-inducible gene.
    • The CYFIP2 promoter contains a functional p53-responsive element, confirming direct p53 binding and transcriptional activation.
    • Inducible CYFIP2 expression triggers caspase activation and apoptosis.
    • CYFIP2's subcellular localization is sensitive to CRM-1/Exportin inhibition, suggesting nuclear-cytoplasmic shuttling.

    Conclusions:

    • CYFIP2 is a direct transcriptional target of p53.
    • CYFIP2 is implicated as a mediator of p53-dependent apoptosis, potentially within a redundant gene network.
    • CYFIP2's dynamic subcellular localization suggests its functions may involve both cytoplasmic and nuclear compartments.