Prolyl isomerase Pin1 in cancer

Cell Res. 2014 Sep;24(9):1033-49. doi: 10.1038/cr.2014.109. Epub 2014 Aug 15.


Proline-directed phosphorylation is a posttranslational modification that is instrumental in regulating signaling from the plasma membrane to the nucleus, and its dysregulation contributes to cancer development. Protein interacting with never in mitosis A1 (Pin1), which is overexpressed in many types of cancer, isomerizes specific phosphorylated Ser/Thr-Pro bonds in many substrate proteins, including glycolytic enzyme, protein kinases, protein phosphatases, methyltransferase, lipid kinase, ubiquitin E3 ligase, DNA endonuclease, RNA polymerase, and transcription activators and regulators. This Pin1-mediated isomerization alters the structures and activities of these proteins, thereby regulating cell metabolism, cell mobility, cell cycle progression, cell proliferation, cell survival, apoptosis and tumor development.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Apoptosis
  • Cell Cycle
  • Glycolysis
  • Humans
  • NIMA-Interacting Peptidylprolyl Isomerase
  • Neoplasms / enzymology*
  • Neoplasms / genetics
  • Neoplasms / pathology
  • Neoplasms / therapy
  • Peptidylprolyl Isomerase / genetics
  • Peptidylprolyl Isomerase / metabolism*
  • Transcription Factors / metabolism


  • NIMA-Interacting Peptidylprolyl Isomerase
  • Transcription Factors
  • PIN1 protein, human
  • Peptidylprolyl Isomerase