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0030837555
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P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase
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Myers M.P., Stolarov J.P., Eng C., Li J., Wang S.I., Wigler M.H., Parsons R., Tonks N.K. P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase. Proc Natl Acad Sci USA. 94:1997;9052-9057.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 9052-9057
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Myers, M.P.1
Stolarov, J.P.2
Eng, C.3
Li, J.4
Wang, S.I.5
Wigler, M.H.6
Parsons, R.7
Tonks, N.K.8
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48
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0032577699
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The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
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3production.
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3production.
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(1998)
J Biol Chem
, vol.273
, pp. 13375-13378
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Maehama, T.1
Dixon, J.E.2
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49
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0032506011
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The lipid phosphatase activity of PTEN is critical for its tumor supressor function
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3but not poly-Glu-phospho-Tyr. In addition, overexpression of wild-type or 'substrate trapping' forms of PTEN is shown to affect 3-phosphoinositide levels and Akt phosphorylation.
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3but not poly-Glu-phospho-Tyr. In addition, overexpression of wild-type or 'substrate trapping' forms of PTEN is shown to affect 3-phosphoinositide levels and Akt phosphorylation.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 13513-13518
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Myers, M.P.1
Pass, I.2
Batty, I.H.3
Van Der Kaay, J.4
Stolarov, J.P.5
Hemmings, B.A.6
Wigler, M.H.7
Downes, C.P.8
Tonks, N.K.9
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50
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0032475861
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Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN
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This paper describes the phenotypes of PTEN knockout mice and fibro- blasts. PTEN knockout mice die in utero by day 9.5 of development and display abnormal patterning and regions of increased proliferation. In contrast, PTEN mutant mouse embryonic fibroblasts show no proliferation defects, but have decreased sensitivity to various apoptotic stimuli and have elevated Akt activity.
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Stambolic V., Suzuki A., de la Pompa J.L., Brothers G.M., Mirtsos C., Sasaki T., Ruland J., Penninger J.M., Siderovski D.P., Mak T.W. Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN. Cell. 95:1998;29-39. This paper describes the phenotypes of PTEN knockout mice and fibro- blasts. PTEN knockout mice die in utero by day 9.5 of development and display abnormal patterning and regions of increased proliferation. In contrast, PTEN mutant mouse embryonic fibroblasts show no proliferation defects, but have decreased sensitivity to various apoptotic stimuli and have elevated Akt activity.
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(1998)
Cell
, vol.95
, pp. 29-39
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Stambolic, V.1
Suzuki, A.2
De La Pompa, J.L.3
Brothers, G.M.4
Mirtsos, C.5
Sasaki, T.6
Ruland, J.7
Penninger, J.M.8
Siderovski, D.P.9
Mak, T.W.10
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51
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0032558822
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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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Haas-Kogan D., Shalev N., Wong M., Mills G., Yount G., Stokoe D. Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutation of the tumor suppressor PTEN/MMAC. Curr Biol. 8:1998;1195-1198.
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(1998)
Curr Biol
, vol.8
, pp. 1195-1198
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Haas-Kogan, D.1
Shalev, N.2
Wong, M.3
Mills, G.4
Yount, G.5
Stokoe, D.6
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53
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0032530384
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Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast
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note
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3-binding PH domains and co-expressing PI3K. A variety of PH domains was tested and their in vivo lipid binding-specificity in yeast was shown to reflect well their in vitro lipid binding-specificity. TOPIS was then used to identify several new PH domain-containing proteins that bind 3-phosphoinositides.
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(1998)
EMBO J
, vol.17
, pp. 5374-5387
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Isakoff, S.J.1
Cardozo, T.2
Andreev, J.3
Li, Z.4
Ferguson, K.M.5
Abagyan, R.6
Lemmon, M.A.7
Aronheim, A.8
Skolnik, E.Y.9
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54
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0032500730
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Bifurcation of lipid and protein kinase signals of PI3Kγ to the protein kinases PKB and MAPK
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In vitro, many PI3Ks possess protein kinase activity towards themselves or their associated adaptor subunits. In this report, mutants of the G-protein-linked PI3K p110γ were created which had lost their lipid kinase activity but had retained in vitro protein kinase activity. In a co-expression system, these 'protein kinase only' mutants no longer activate Akt (a 3-phosphoinositide-dependent phenomenon) but do activate the mitogen-activated protein kinase ERK2. Although the physiological relevance of these observations is not entirely clear, these findings do demonstrate that the protein kinase activity of PI3Ks can have an impact on intracellular signal transduction.
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Bondeva T., Pirola L., Bulgarelli-Leva G., Rubio I., Wetzker R., Wymann M.P. Bifurcation of lipid and protein kinase signals of PI3Kγ to the protein kinases PKB and MAPK. Science. 282:1998;293-296. In vitro, many PI3Ks possess protein kinase activity towards themselves or their associated adaptor subunits. In this report, mutants of the G-protein-linked PI3K p110γ were created which had lost their lipid kinase activity but had retained in vitro protein kinase activity. In a co-expression system, these 'protein kinase only' mutants no longer activate Akt (a 3-phosphoinositide-dependent phenomenon) but do activate the mitogen-activated protein kinase ERK2. Although the physiological relevance of these observations is not entirely clear, these findings do demonstrate that the protein kinase activity of PI3Ks can have an impact on intracellular signal transduction.
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(1998)
Science
, vol.282
, pp. 293-296
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Bondeva, T.1
Pirola, L.2
Bulgarelli-Leva, G.3
Rubio, I.4
Wetzker, R.5
Wymann, M.P.6
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