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Pin1 and JNK1 cooperatively modulate TAp63γ.

Xueying Fan1, Wei He2, Ke Hu1

  • 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.

Keywords:
JNK1Pin1TAp63γtransactivity

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