[Pin1: a multi-talented peptidyl prolyl cis-trans isomerase and a promising therapeutic target for human cancers].

Abstract

Post-translational modifications are critical to modulate protein function. A post-translational mechanism, peptidyl prolyl cis-trans isomerisation, plays a key role in protein regulation. Pin1 is a ubiquitous peptidyl prolyl cis-trans isomerase conserved from Archae to Human. This enzyme binds and isomerizes phospho-serine/threonine-proline motifs. This process can induce conformational change in protein targets and modulates their activity, cellular localization, phosphorylation state, stability and/or protein-protein interactions. Pin1 activity regulates proteins involved in cell proliferation, pluripotency or cellular invasion. Pin1 is overexpressed in several human cancers and contributes to tumorigenesis. Its inactivation constitutes a promising therapeutic strategy.

• Authors: Justine Marsolier, Jonathan B Weitzman
• Journal: Medecine sciences : M/S (Med Sci (Paris)) 2014 Aug-Sep Vol. 30 Issue 8-9 Pg. 772-8 ISSN: 0767-0974 [Print] France
• Vernacular Title: Pin1: une peptidyl-prolyl cis-trans isomérase multifonctionnelle et une cible anticancéreuse prometteuse.
• PMID: 25174754 (Publication Type: Journal Article, Review)
• Copyright: © 2014 médecine/sciences – Inserm.

Chemical References

• Enzyme Inhibitors
• NIMA-Interacting Peptidylprolyl Isomerase
• PIN1 protein, human
• Peptidylprolyl Isomerase

Topics

• Animals
• Cell Proliferation
• Cell Transformation, Neoplastic (genetics, metabolism)
• Enzyme Inhibitors (therapeutic use)
• Humans
• Molecular Targeted Therapy (methods, trends)
• NIMA-Interacting Peptidylprolyl Isomerase
• Neoplasms (drug therapy, enzymology)
• Peptidylprolyl Isomerase (antagonists & inhibitors, metabolism)