PTEN and myotubularin phosphatases: from 3-phosphoinositide dephosphorylation to disease (Q28218655)

Synthesis and function of 3-phosphorylated inositol lipids

Europe PubMed Central

title

PTEN and myotubularin phosphatases: from 3-phosphoinositide dephosphorylation to disease (English)

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2

Jack E Dixon

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author name string

Matthew J Wishart

series ordinal

1

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language of work or name

English

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publication date

December 2002

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published in

Trends in Cell Biology

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volume

12

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issue

12

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page(s)

579-85

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cites work

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PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer

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The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate

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PTEN and myotubularin: novel phosphoinositide phosphatases

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Pten is essential for embryonic development and tumour suppression

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The PTEN tumor suppressor homolog in Caenorhabditis elegans regulates longevity and dauer formation in an insulin receptor-like signaling pathway

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Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis

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Characterization of an adapter subunit to a phosphatidylinositol (3)P 3-phosphatase: identification of a myotubularin-related protein lacking catalytic activity

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Functional redundancy in the myotubularin family

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