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Literature DB >> 16675164

Regulation of the PTEN phosphatase.

Arne Gericke¹, Mary Munson, Alonzo H Ross.

Abstract

Phosphatase and tensin homologue deleted on chromosome 10 (PTEN) is a phosphatidylinositol phosphate phosphatase and is frequently inactivated in human cancers. The balance between phosphoinositide 3-kinase (PI3K) and PTEN determines PI(3,4,5)P3 levels. PI3K is regulated by a variety of intracellular and extracellular signals, but little is known about the regulation of PTEN. In this article, we review control of PTEN function by phosphorylation as well as by binding of lipid and protein partners.

Entities: Chemical Disease Gene Species

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Year: 2006 PMID： 16675164 DOI： 10.1016/j.gene.2006.02.024

Source DB: PubMed Journal: Gene ISSN： 0378-1119 Impact factor: 3.688

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Cited

80 in total

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10. Haloperidol induces the nuclear translocation of phosphatidylinositol 3'-kinase to disrupt Akt phosphorylation in PC12 cells.

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Regulation of the PTEN phosphatase.

Review 1. PPARgamma as a potential therapeutic target in pulmonary hypertension.

Review 2. Big roles for small GTPases in the control of directed cell movement.

3. PTEN directly activates the actin depolymerization factor cofilin-1 during PGE2-mediated inhibition of phagocytosis of fungi.

4. PTEN and Akt expression during growth of human ovarian follicles.

5. Phosphatase and tensin homolog on chromosome 10 is phosphorylated in primary effusion lymphoma and Kaposi's sarcoma.

6. Glucocorticoid receptor β stimulates Akt1 growth pathway by attenuation of PTEN.

7. Cholesterol stabilizes fluid phosphoinositide domains.

Review 8. Phosphatase and tensin homologue deleted on chromosome 10: extending its PTENtacles.

Review 9. Regulation and modulation of PTEN activity.

10. Haloperidol induces the nuclear translocation of phosphatidylinositol 3'-kinase to disrupt Akt phosphorylation in PC12 cells.