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Related Experiment Videos

p8 and prothymosin alpha: unity is strength.

Cédric Malicet1, Jean Charles Dagorn, José Luis Neira

  • 1INSERM U.624, Stress Cellulaire, Marseille, France.

Cell Cycle (Georgetown, Tex.)
|April 22, 2006
PubMed
Summary

The p8/ProTalpha protein complex, not individual proteins, inhibits apoptosis. This finding reveals that the function of natively unfolded proteins may reside in multi-protein complexes.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Protein Biochemistry

Background:

  • p8 and prothymosin alpha are natively unstructured proteins.
  • Both proteins are individually associated with anti-apoptotic activity.

Purpose of the Study:

  • To investigate the functional role of the p8/ProTalpha heterodimer in apoptosis.
  • To determine if the anti-apoptotic activity resides in individual proteins or their complex.

Main Methods:

  • In vitro analysis of p8 and prothymosin alpha interaction.
  • Formation of a stable one-to-one heterodimer complex.
  • Modulation of protein concentrations via vector overexpression and siRNA inhibition.
  • Monitoring apoptosis in response to altered protein levels.

Main Results:

  • The p8/ProTalpha complex forms a stable heterodimer.
  • Apoptosis inhibition correlated with the concentration of the limiting protein in the complex.
  • Individual p8 or prothymosin alpha proteins were found to be inactive in isolation.
  • The anti-apoptotic function is attributed to the p8/ProTalpha complex.

Conclusions:

  • The anti-apoptotic activity previously ascribed to p8 and prothymosin alpha individually is actually mediated by their heterodimer complex.
  • Natively unfolded proteins may exert function through multi-protein complexes rather than as individual entities.

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