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

Prolyl isomerase Pin1 in cancer

Zhimin Lu  1 , Tony Hunter  2
Affiliations
Review

Prolyl isomerase Pin1 in cancer

Zhimin Lu et al. Cell Res. 2014 Sep.

Abstract

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.

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Figures

Figure 1
Figure 1
Schematic of the structure of Pin1 showing the regulatory posttranslational modification sites.
See this image and copyright information in PMC

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