NDLI: The lipid phosphatase activity of PTEN is critical for its tumor supressor function

Content Provider	PubMed Central
Author	Myers, Michael P. Pass, Ian Batty, Ian H. Kaay, Jeroen Van Der Stolarov, Javor P. Hemmings, Brian A. Wigler, Michael H. Downes, C. Peter Tonks, Nicholas K.
Copyright Year	1998
Abstract	Since their discovery, protein tyrosine phosphatases have been speculated to play a role in tumor suppression because of their ability to antagonize the growth-promoting protein tyrosine kinases. Recently, a tumor suppressor from human chromosome 10q23, called PTEN or MMAC1, has been identified that shares homology with the protein tyrosine phosphatase family. Germ-line mutations in PTEN give rise to several related neoplastic disorders, including Cowden disease. A key step in understanding the function of PTEN as a tumor suppressor is to identify its physiological substrates. Here we report that a missense mutation in PTEN, PTEN-G129E, which is observed in two Cowden disease kindreds, specifically ablates the ability of PTEN to recognize inositol phospholipids as a substrate, suggesting that loss of the lipid phosphatase activity is responsible for the etiology of the disease. Furthermore, expression of wild-type or substrate-trapping forms of PTEN in HEK293 cells altered the levels of the phospholipid products of phosphatidylinositol 3-kinase and ectopic expression of the phosphatase in PTEN-deficient tumor cell lines resulted in the inhibition of protein kinase (PK) B/Akt and regulation of cell survival.
Starting Page	13513
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	95
Language	English
Publisher	The National Academy of Sciences
Publisher Date	1998-11-10
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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The lipid phosphatase activity of PTEN is critical for its tumor supressor function.

The lipid phosphatase activity of PTEN is critical for stabilizing intercellular junctions and reverting invasiveness

Motif analysis of the tumor suppressor gene MMAC/PTEN identifies tyrosines critical for tumor suppression and lipid phosphatase activity

PTEN Dual Lipid- and Protein-Phosphatase Function in Tumor Progression

The tumor-suppressor activity of PTEN is regulated by its carboxyl-terminal region

Opening the conformation is a master switch for the dual localization and phosphatase activity of PTEN

The lipid phosphatase activity of PTEN is critical for stabilizing intercellular junctions and reverting invasiveness

Mutational Spectra of PTEN/MMAC1 Gene: a Tumor Suppressor With Lipid Phosphatase Activity

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The lipid phosphatase activity of PTEN is critical for its tumor supressor function

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The lipid phosphatase activity of PTEN is critical for its tumor supressor function.

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