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Pin1 and JNK1 cooperatively modulate TAp63γ.

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  • 1Center of Growth, Metabolism and Aging, Key Laboratory of Biological Resources and Ecological Environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu, China.

FEBS Open Bio
|February 6, 2021
PubMed
Summary

The peptidyl-prolyl isomerase (PPI) Pin1 protein binds to the TAp63γ transcription factor, enhancing its activity. This interaction, dependent on JNK1 phosphorylation, reveals a novel regulatory mechanism for TAp63γ transactivity.

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Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Protein Interactions

Background:

  • The p63 gene produces multiple isoforms, including TAp63γ, a key transcription factor.
  • Previous work identified Pin1 binding to TAp63γ and the importance of serine 12 (S12) for its transcriptional regulation.

Purpose of the Study:

  • To investigate the role of Pin1 and JNK1 in modulating TAp63γ transcriptional and pro-apoptotic activities.
  • To elucidate the novel mechanism regulating TAp63γ transactivity.

Main Methods:

  • Investigated the interaction between Pin1, TAp63γ, and JNK1.
  • Analyzed the effect of S12 phosphorylation and Pin1 binding on TAp63γ activity.

Main Results:

  • Pin1 significantly stimulates the transcriptional and pro-apoptotic functions of TAp63γ.
  • JNK1-mediated phosphorylation of S12 is crucial for Pin1-dependent TAp63γ activation.
  • A novel regulatory model: unphosphorylated S12 leads to moderate activity, pS12 causes hypoactivity, and Pin1 binding to pS12-P13 results in hyperactivity.

Conclusions:

  • Pin1 acts as a critical positive regulator of TAp63γ activity through a phosphorylation-dependent mechanism.
  • This study uncovers a new pathway for controlling TAp63γ function, impacting gene regulation and apoptosis.