QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online November 21, 2007
doi: 10.1242/10.1242/jcs.015230

This Article Figures Only Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tamguney, T. Articles by Stokoe, D. Search for Related Content PubMed PubMed Citation Articles by Tamguney, T. Articles by Stokoe, D. Social Bookmarking                         What's this?

New insights into PTEN

UCSF Cancer Research Institute, 2340 Sutter Street, San Francisco, CA 94115, USA

e-mails: tmeyer{at}cc.ucsf.edu; Stokoe.david{at}gene.com

Accepted 16 October 2007

The functions ascribed to PTEN have become more diverse since its discovery as a putative phosphatase mutated in many human tumors. Although it can dephosphorylate lipids and proteins, it also has functions independent of phosphatase activity in normal and pathological states. In addition, control of PTEN function is very complex. It is positively and negatively regulated at the transcriptional level, as well as post-translationally by phosphorylation, ubiquitylation, oxidation and acetylation. Although most of its tumor suppressor activity is likely to be caused by lipid dephosphorylation at the plasma membrane, PTEN also resides in the cytoplasm and nucleus, and its subcellular distribution is under strict control. Deregulation of PTEN function is implicated in other human diseases in addition to cancer, including diabetes and autism.

Key words: PI3-kinase activity, PTEN, Phosphatase, Cancer, Diabetes

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				S. Mosessian, N. K. Avliyakulov, D. J. Mulholland, P. Boontheung, J. A. Loo, and H. Wu Analysis of PTEN Complex Assembly and Identification of Heterogeneous Nuclear Ribonucleoprotein C as a Component of the PTEN-associated Complex J. Biol. Chem., October 30, 2009; 284(44): 30159 - 30166. [Abstract] [Full Text] [PDF]

				L. Ressel, F. Millanta, E. Caleri, V. M. Innocenti, and A. Poli Reduced PTEN Protein Expression and Its Prognostic Implications in Canine and Feline Mammary Tumors Vet. Pathol., September 1, 2009; 46(5): 860 - 868. [Abstract] [Full Text] [PDF]

				M. Niedermeier, B. T. Hennessy, Z. A. Knight, M. Henneberg, J. Hu, A. V. Kurtova, W. G. Wierda, M. J. Keating, K. M. Shokat, and J. A. Burger Isoform-selective phosphoinositide 3'-kinase inhibitors inhibit CXCR4 signaling and overcome stromal cell-mediated drug resistance in chronic lymphocytic leukemia: a novel therapeutic approach Blood, May 28, 2009; 113(22): 5549 - 5557. [Abstract] [Full Text] [PDF]

				K. Sakamoto, K. Iwasaki, H. Sugiyama, and Y. Tsuji Role of the Tumor Suppressor PTEN in Antioxidant Responsive Element-mediated Transcription and Associated Histone Modifications Mol. Biol. Cell, March 15, 2009; 20(6): 1606 - 1617. [Abstract] [Full Text] [PDF]