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Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen.

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Phosphorylation of prostate-associated gene 4 (PAGE4) alters its structure, impacting its interaction with c-Jun and influencing prostate cancer cell growth and survival.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Prostate-associated gene 4 (PAGE4) is a cancer/testis antigen upregulated in prostate cancer.
  • PAGE4's expression level influences prostate cancer cell survival and proliferation.
  • Phosphorylation at Thr-51 is crucial for PAGE4's function in c-Jun transactivation.

Purpose of the Study:

  • To investigate the structural consequences of PAGE4 phosphorylation at Thr-51.
  • To elucidate how phosphorylation affects PAGE4's interaction with c-Jun.
  • To understand the functional implications of these structural changes in prostate cancer.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was used to analyze PAGE4 structure.
  • Site-specific phosphorylation at Thr-51 was introduced to study its effects.
  • In vitro binding assays were performed to assess PAGE4-c-Jun interactions.

Main Results:

  • Phosphorylation at Thr-51 induces conformational changes in PAGE4, increasing transient turn-like structures.
  • Phosphorylated PAGE4 becomes more compact and negatively charged in its central region.
  • Phosphorylation attenuates PAGE4 binding to c-Jun, likely due to altered conformation.

Conclusions:

  • PAGE4 phosphorylation triggers conformational shifts in its dynamic ensemble.
  • These structural changes have significant functional consequences for prostate cancer cell biology.
  • PAGE4's post-translational modifications illustrate principles of conformational switching in intrinsically disordered proteins.