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Peptidyl-prolyl Isomerases in Human Pathologies

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Front. Pharmacol. | doi: 10.3389/fphar.2018.01477

A Guide to PIN1 Function and Mutations Across Cancers

 Maguie El Boustani1,  Lucia De Stefano1, Isabella Caligiuri1, Nayla Mouawad1, Carlotta Granchi2, Vincenzo Canzonieri1, Tiziano Tuccinardi2,  Antonio Giordano3 and  Flavio Rizzolio4*
  • 1Translational Medicine, Centro di Riferimento Oncologico di Aviano (IRCCS), Italy
  • 2Pharmacy, University of Pisa, Italy
  • 3Biology, Temple University, United States
  • 4Università Ca' Foscari, Italy

PIN1 is a member of a family of peptidylprolyl isomerases that bind phosphoproteins and catalyze the rapid cis-trans isomerization of proline peptidyl bonds, resulting in an alteration of protein structure, function and stability. PIN1 is overexpressed in human cancers, suggesting it promotes tumorigenesis, but depending on the cellular context, it also acts as a tumor suppressor. Here, we review the role of PIN1 in cancer and the regulation of PIN1 expression, and catalog the single nucleotide polymorphisms and mutations in PIN1 gene associated with cancer. In addition, we provide a 3D model of the protein to localize the mutated residues.

Keywords: Pin1, Cancer, mutations, SNP, 3D modeling

Received: 30 Oct 2018; Accepted: 03 Dec 2018.

Edited by:

Filippo Caraci, Università degli Studi di Catania, Italy

Reviewed by:

Simone Carradori, Dipartimento di Farmacia, Università "G. d'Annunzio" di Chieti-Pescara, Italy
Fabrizio Carta, Università degli Studi di Firenze, Italy  

Copyright: © 2018 El Boustani, De Stefano, Caligiuri, Mouawad, Granchi, Canzonieri, Tuccinardi, Giordano and Rizzolio. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

* Correspondence: Dr. Flavio Rizzolio, Università Ca' Foscari, Venice, Italy, flavio.rizzolio@unive.it