Direct identification of PTEN phosphorylation sites (Q28203697)

2

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David C Seldin

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William S Lane

4

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Benjamin G Neel

New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway

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publication date

25 September 2002

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language of work or name

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528

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issue

1-3

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page(s)

145-53

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cites work

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Allelic imbalance, including deletion of PTEN/MMACI, at the Cowden disease locus on 10q22-23, in hamartomas from patients with Cowden syndrome and germline PTEN mutation

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Mutation spectrum and genotype-phenotype analyses in Cowden disease and Bannayan-Zonana syndrome, two hamartoma syndromes with germline PTEN mutation

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Pten is essential for embryonic development and tumour suppression

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High cancer susceptibility and embryonic lethality associated with mutation of the PTEN tumor suppressor gene in mice

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Mutation of Pten/Mmac1 in mice causes neoplasia in multiple organ systems

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

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

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Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutation of the tumor suppressor PTEN/MMAC

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Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN

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PTEN modulates cell cycle progression and cell survival by regulating phosphatidylinositol 3,4,5,-trisphosphate and Akt/protein kinase B signaling pathway

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PTEN and myotubularin: novel phosphoinositide phosphatases

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Transformation of chicken cells by the gene encoding the catalytic subunit of PI 3-kinase

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The PTEN/MMAC1 tumor suppressor phosphatase functions as a negative regulator of the phosphoinositide 3-kinase/Akt pathway

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Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2

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Phosphorylation of the PTEN tail regulates protein stability and function

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The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation

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

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Phosphorylation of the PTEN Tail Acts as an Inhibitory Switch by Preventing Its Recruitment into a Protein Complex

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