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Updated: Feb 27, 2026

Characterization of Cell Membrane Extensions and Studying Their Roles in Cancer Cell Adhesion Dynamics
08:11

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Published on: March 26, 2018

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Dual Roles of Pin1 in Cancer Development and Progression

Hyeong-Jun Han1, Bu Young Choi2, Young-Joon Surh1

  • 1Tumor Microenvironment Global Core Research Center, College of Pharmacy, Seoul National University, Seoul 08826, Korea.

Current Pharmaceutical Design
|July 4, 2017
PubMed

Insights

Pin1, a peptidyl-prolyl cis/trans isomerase, influences protein conformation and function. While often overexpressed in cancers, its role as a tumor suppressor is also being investigated.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Pin1 (Peptidyl-prolyl cis/trans isomerase) catalyzes cis/trans isomerization of specific phosphorylated motifs (pSer/Thr-Pro) in substrate proteins.
  • This isomerization alters protein conformation, affecting stability, localization, and biological functions.
  • Pin1 overexpression is linked to cancer progression, including proliferation, migration, and invasion.

Purpose of the Study:

  • To systematically dissect the dual roles of Pin1 in cancer.
  • To differentiate between pro-oncogenic and tumor-suppressive functions of Pin1.

Main Methods:

  • The study involves analyzing the biochemical activity of Pin1.
  • Investigating Pin1's interaction with phosphorylated substrate proteins.
  • Assessing the impact of Pin1 on cancer cell behavior and tumor development.

Main Results:

  • Pin1's overexpression is associated with pro-oncogenic activities in malignancies.
  • Emerging evidence suggests Pin1 may also possess tumor-suppressive functions.
  • Further research is required to fully elucidate these contrasting roles.

Conclusions:

  • Pin1 exhibits complex roles in cancer, acting as both an oncogene and potentially a tumor suppressor.
  • A comprehensive understanding of Pin1's functions is crucial for cancer therapy development.
Keywords:
PPIasePin1pSer/Thr-Pro motifphosphorylation-dependent peptidyl-prolyl isomeraseproline isomerizationproline-directed protein kinases

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