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Int J Biochem Cell Biol. 2009 Apr;41(4):757-61. doi: 10.1016/j.biocel.2008.09.022. Epub 2008 Oct 2.

Phosphatase and tensin homologue deleted on chromosome 10: extending its PTENtacles.

Author information

1
Pharmacology and Pharmaceutical Sciences, USC School of Pharmacy, Los Angeles, CA 90089, United States. bstiles@usc.edu

Abstract

Since its discovery in 1997, phosphatase and tensin homologue deleted on chromosome 10 (PTEN) has become one of the most important molecules in tumor biology. Mutations, deletions or dysregulation of PTEN is found in many human tumors. Recent studies have extended the reach of PTEN to include diabetes and neurological diseases such as Parkinson's and autism. In this review, we summarize the traditionally characterized function of PTEN as the lipid phosphatase that dephosphorylates PI-3,4,5-P(3), and several other newly discovered functions. The inhibition of the phosphatidylinositol-3-kinase (PI3K)/AKT signaling pathway may account for most of PTEN's tumor suppressing function. However, other growth inhibiting functions of PTEN may not involve this pathway. PTEN can also inhibit growth through its protein phosphatase activity and in ways not related to its enzymatic activity at all. We survey the many functions and biochemical interactions of PTEN in cytoplasm, the nucleus and throughout the cell in this paper.

PMID:
18950730
PMCID:
PMC2940266
DOI:
10.1016/j.biocel.2008.09.022
[Indexed for MEDLINE]
Free PMC Article

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