Non-canonical Function of Prolyl Hydroxylase Domain 2 in Breast Cancer Cell Growth and Progression: Role of Peptidyl-prolyl Cis-trans Isomerase NIMA-interacting 1

Yanymee N. Guillen Quispe(Seoul National University), Su‐Jung Kim(Seoul National University), Soma Saeidi(Seoul National University), Gyo-Jin Choi(Seoul National University), Chaithanya Chelakkot(Seoul National University), Tianchi Zhou(Institute of Genetics and Cancer), Sang-Beom Bang(Seoul National University), Tae-Won Kim(Seoul National University), Young Kee Shin(Seoul National University), Young‐Joon Surh(Seoul National University)
Journal of Cancer Prevention
December 30, 2024
10.15430/jcp.24.031
Cited by 1Open Access
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Abstract

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) targets proteins with phosphorylated serine/threonine-proline (pSer/Thr-Pro) motifs. As PHD2 contains several pSer/Thr-Pro motifs, it may be a potential substrate of Pin1. In the present study, we found Pin1 and PHD2 interactions in human breast cancer MDA-MB-231 cells. The breast cancer tissue array revealed higher levels of PHD2 and Pin1 in tumors compared to adjacent normal tissues. Through liquid chromatography-tandem mass spectrometry spectrometry, three phosphorylation sites (S125, T168, and S174) on PHD2 were identified, with serine 125 as the main site for Pin1 binding. As a new Pin1 binding partner, oncogenic PHD2 could be a potential therapeutic target for breast cancer treatment.

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