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First published online January 23, 2008
doi: 10.1242/10.1242/jcs.022459

Journal of Cell Science 121, 249-253 (2008)
Published by The Company of Biologists 2008
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Commentary

The nuclear affairs of PTEN

Sarah M. Planchon1,2, Kristin A. Waite1,2,3 and Charis Eng1,2,3,4,5,*

1 Genomic Medicine Institute, Cleveland Clinic Foundation, Cleveland, OH 44195, USA
2 Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH 44195, USA
3 Taussig Cancer Institute, Cleveland Clinic Foundation, Cleveland, OH 44195, USA
4 Department of Genetics, Case Western Reserve University School of Medicine, Cleveland, OH, USA
5 CASE Comprehensive Cancer Center, Case Western Reserve University School of Medicine, Cleveland, OH, USA

* Author for correspondence (e-mail: engc{at}ccf.org)

Accepted 15 November 2007

PTEN encodes a major tumor-suppressor protein that is a dual-specificity phosphatase. Inactivation of PTEN has been shown to be involved in heritable and sporadic cancers. Mutation or deletion of PTEN, historically the most commonly identified mechanisms of inactivation of tumor suppressors, is found only in the minority of sporadic non-cultured primary cancers, which indicates that there might be other, novel mechanisms of inactivation. Despite the absence of a classic nuclear localization signal, PTEN enters the nucleus by several mechanisms, including simple diffusion, active shuttling, cytoplasmic-localization-signal-dependent export and monoubiquitylation-dependent import. Cytoplasmic PTEN has a well-known role as a negative regulator of the PI3K/AKT pathway; however, it is becoming clear that cytosolic PTEN is not the same as nuclear PTEN. Nuclear PTEN plays a role in chromosome stability, DNA repair, cell cycle arrest and cellular stability. The balance between these functions is an important factor in determining whether a cell remains benign or becomes neoplastic.

Key words: PTEN, Nuclear, Subcellular localization, Cowden, PHTS, Bifurcation




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