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The same tyrosine-based inhibition motif, in the intracytoplasmic domain of Fc gamma RIIB, regulates negatively BCR-, TCR-, and FcR-dependent cell activation
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Daeron M, Latour S, Malbec O, Espinosa E, Pina P, Pasmans S, Fridman WH. The same tyrosine-based inhibition motif, in the intracytoplasmic domain of Fc gamma RIIB, regulates negatively BCR-, TCR-, and FcR-dependent cell activation. Immunity. 3:1995;635-646.
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Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by Fc gamma RIIB1
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D'Ambrosio D, Hippen KL, Minskoff SA, Mellman I, Pani G, Siminovitch KA, Cambier JC. Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by Fc gamma RIIB1. Science. 268:1995;293-297.
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Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions
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Black DS, Bliska JB. Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions. EMBO J. 16:1997;2730-2744.
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Negative signaling in B-lymphocytes induces tyrosine phosphorylation of the 145kDa inositol polyphosphate 5-phosphatase, SHIP
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of outstanding interest. These experiments first established that p150 SH2 domain-containing inositol 5-phosphatase (SHIP) is exclusive tyrosine phosphorylated and associated with Shc, the adapter protein involved in stimulation of the Ras pathway, upon co-crosslinking surface immunoglobulin and Immunoglobulin Fcγ receptor (Fcγ) Rllb. SHIP did not undergo tyrosine phoshorylation nor did it interact with Shc under positive signaling conditions (triggering of surface immunoglobulin alone). These events regarding SHIP were completely reversed by costimulation of B cells under negative signaling conditions with a blocking anti-FcγRIIb antibody, thus indicating the intimate involvement of FcγRIIb in promoting SHIP phosphorylation and in its interaction with Shc.
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Chacko GW, Tridandapani S, Damen J, Liu L, Krystal G, Coggeshall KM. Negative signaling in B-lymphocytes induces tyrosine phosphorylation of the 145kDa inositol polyphosphate 5-phosphatase, SHIP. of outstanding interest J Immunol. 157:1996;2234-2238 These experiments first established that p150 SH2 domain-containing inositol 5-phosphatase (SHIP) is exclusive tyrosine phosphorylated and associated with Shc, the adapter protein involved in stimulation of the Ras pathway, upon co-crosslinking surface immunoglobulin and Immunoglobulin Fcγ receptor (Fcγ) Rllb. SHIP did not undergo tyrosine phoshorylation nor did it interact with Shc under positive signaling conditions (triggering of surface immunoglobulin alone). These events regarding SHIP were completely reversed by costimulation of B cells under negative signaling conditions with a blocking anti-FcγRIIb antibody, thus indicating the intimate involvement of FcγRIIb in promoting SHIP phosphorylation and in its interaction with Shc.
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Chacko, G.W.1
Tridandapani, S.2
Damen, J.3
Liu, L.4
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Coggeshall, K.M.6
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21
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0029835940
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Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor Fc(gamma)RIIB
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of special interest. of outstanding interest. Reported at approximately the same time as Chacko et al., 1996 [20], these studies employed immunoreceptor tyrosine-based inhibitory motif (ITIM) synthetic phosphopeptide as described earlier by D'Ambrosio et al., 1995 [18], and determined the primary sequence of the p150 protein, which proved to be SHIP. The authors further showed that SHIP co-immunoprecipitated with FcγRIIb in B cells and mast cells during negative signaling conditions.
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of special interest Ono M, Bolland S, Tempst P, Ravetch JV. Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor Fc(gamma)RIIB. of outstanding interest Nature. 383:1996;263-266 Reported at approximately the same time as Chacko et al., 1996 [20], these studies employed immunoreceptor tyrosine-based inhibitory motif (ITIM) synthetic phosphopeptide as described earlier by D'Ambrosio et al., 1995 [18], and determined the primary sequence of the p150 protein, which proved to be SHIP. The authors further showed that SHIP co-immunoprecipitated with FcγRIIb in B cells and mast cells during negative signaling conditions.
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Nature
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Ono, M.1
Bolland, S.2
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Ravetch, J.V.4
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22
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0029978202
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The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase
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of special interest. These authors were the first of three groups (see Kavanaugh et al., 1996 [23] and Lioubin et al., 1996 [24]) to identify cDNA encoding the SHIP protein and to establish its enzymatic activity and specificity for 3-phosphorylated inositols and phosphoinositides.
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Damen JE, Liu L, Rosten P, Humphries RK, Jefferson AB, Majerus PW, Krystal G. The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase. of special interest Proc Natl Acad Sci USA. 93:1996;1689-1693 These authors were the first of three groups (see Kavanaugh et al., 1996 [23] and Lioubin et al., 1996 [24]) to identify cDNA encoding the SHIP protein and to establish its enzymatic activity and specificity for 3-phosphorylated inositols and phosphoinositides.
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Proc Natl Acad Sci USA
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Damen, J.E.1
Liu, L.2
Rosten, P.3
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Jefferson, A.B.5
Majerus, P.W.6
Krystal, G.7
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23
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0030113662
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Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2
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Kavanaugh WM, Pot DA, Chin SM, Deuter-Reinhard M, Jefferson AB, Norris FA, Masiarz FR, Cousens LS, Majerus PW, Williams LT. Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2. Curr Biol. 6:1996;438-445.
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Kavanaugh, W.M.1
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Masiarz, F.R.7
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Majerus, P.W.9
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24
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0029665083
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P150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity
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Lioubin MN, Algate PA, S.T, Carlberg K, Aebersold R, Rohrschneider LR. p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. Genes Dev. 10:1996;1084-1095.
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Lioubin, M.N.1
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Rohrschneider, L.R.5
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25
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0030566667
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The SHIP phosphatase becomes associated with Fc gammaRIIB1 and is tyrosine phosphorylated during 'negative' signaling
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D'Ambrosio D, Fong DC, Cambier JC. The SHIP phosphatase becomes associated with Fc gammaRIIB1 and is tyrosine phosphorylated during 'negative' signaling. Immunol Lett. 54:1996;77-82.
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D'Ambrosio, D.1
Fong, D.C.2
Cambier, J.C.3
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26
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0031033886
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Co-ligation of the antigen and Fc receptors gives rise to the selective modulation of intracellular signaling in B cells. Regulation of the association of phosphatidylinositol 3-kinase and inositol 5′-phosphatase with the antigen receptor complex
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Kiener PA, Lioubin MN, Rohrschneider LR, Ledbetter JA, Nadler SG, Diegel ML. Co-ligation of the antigen and Fc receptors gives rise to the selective modulation of intracellular signaling in B cells. Regulation of the association of phosphatidylinositol 3-kinase and inositol 5′-phosphatase with the antigen receptor complex. J Biol Chem. 272:1997;3838-3844.
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Kiener, P.A.1
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Rohrschneider, L.R.3
Ledbetter, J.A.4
Nadler, S.G.5
Diegel, M.L.6
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27
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0030854757
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Recruitment and phosphorylation of SHIP and Shc to the B cell Fcgamma ITIM peptide motif
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of outstanding interest. These experiments addressed the mechanism through which SH2 domain-containing inositol 5-phosphatase (SHIP) was exclusively phosphorylated under negative signaling conditions. Using synthetic phosphopeptides, the authors demonstrated that the SH2 domain of SHIP directly bound the phosphorylated immunoglobulin Fcγ receptor (Fcγ)RIIb immunoreceptor tyrosine-based inhibitory motif (ITIM) motif and related peptides, but not immuno-receptor tyrosine-based activation motif (ITAM)-like sequences. Experiments using FcγRIIb-deficient cell lines revealed that FcγRIIb expression was essential for tyrosine phosphorylation of SHIP and its subsequent interaction with Shc. These findings established a model in which FcγRIIb becomes tyrosine phosphorylated and associates with SHIP prior to, and essential for, SHIP tyrosine phosphorylation.
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Tridandapani S, Kelley T, Pradhan M, Cooney D, Justement LB, Coggeshall KM. Recruitment and phosphorylation of SHIP and Shc to the B cell Fcgamma ITIM peptide motif. of outstanding interest Mol Cell Biol. 17:1997;4305-4311 These experiments addressed the mechanism through which SH2 domain-containing inositol 5-phosphatase (SHIP) was exclusively phosphorylated under negative signaling conditions. Using synthetic phosphopeptides, the authors demonstrated that the SH2 domain of SHIP directly bound the phosphorylated immunoglobulin Fcγ receptor (Fcγ)RIIb immunoreceptor tyrosine-based inhibitory motif (ITIM) motif and related peptides, but not immuno-receptor tyrosine-based activation motif (ITAM)-like sequences. Experiments using FcγRIIb-deficient cell lines revealed that FcγRIIb expression was essential for tyrosine phosphorylation of SHIP and its subsequent interaction with Shc. These findings established a model in which FcγRIIb becomes tyrosine phosphorylated and associates with SHIP prior to, and essential for, SHIP tyrosine phosphorylation.
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Mol Cell Biol
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Tridandapani, S.1
Kelley, T.2
Pradhan, M.3
Cooney, D.4
Justement, L.B.5
Coggeshall, K.M.6
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28
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0030923454
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Activation-induced bi-dentate SHIP and Shc interaction in B lymphocytes
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of outstanding interest. Using recombinant interaction domains from SH2 domain-containing inositol 5-phosphatase (SHIP) and Shc and synthetic phosphopeptides corresponding to known phosphorylation sites of the two proteins, the authors disclosed that SHIP-Shc interaction requires SHIP but not Shc tyrosine phosphorylation and is bidentate. Thus the phosphotyrosine-binding domain of Shc bound phosphoSHIP at Y931 (using single-letter code for amino acids) and/or Y1035. The SH2 domain of SHIP engaged phosphoShc at Y317 and doubly phosphorylated Y239/240, identical to those phosphorylated residues of Shc engaged by the SH2 domain of Grb2. The SH2 domain of Shc was not involved in the interaction. Results reported by Liu et al., 1997 [29] but not by Lamkin et al., 1997 [30] are consistent with these conclusions.
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Pradhan M, Coggeshall KM. Activation-induced bi-dentate SHIP and Shc interaction in B lymphocytes. of outstanding interest J Cell Biochem. 67:1997;32-42 Using recombinant interaction domains from SH2 domain-containing inositol 5-phosphatase (SHIP) and Shc and synthetic phosphopeptides corresponding to known phosphorylation sites of the two proteins, the authors disclosed that SHIP-Shc interaction requires SHIP but not Shc tyrosine phosphorylation and is bidentate. Thus the phosphotyrosine-binding domain of Shc bound phosphoSHIP at Y931 (using single-letter code for amino acids) and/or Y1035. The SH2 domain of SHIP engaged phosphoShc at Y317 and doubly phosphorylated Y239/240, identical to those phosphorylated residues of Shc engaged by the SH2 domain of Grb2. The SH2 domain of Shc was not involved in the interaction. Results reported by Liu et al., 1997 [29] but not by Lamkin et al., 1997 [30] are consistent with these conclusions.
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(1997)
J Cell Biochem
, vol.67
, pp. 32-42
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Pradhan, M.1
Coggeshall, K.M.2
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29
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0030975468
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The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with Shc and its induction of apoptosis
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Liu L, Damen JE, Hughes MR, Babic I, Jirik FR, Krystal G. The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with Shc and its induction of apoptosis. J Biol Chem. 272:1997;8983-8988.
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J Biol Chem
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Liu, L.1
Damen, J.E.2
Hughes, M.R.3
Babic, I.4
Jirik, F.R.5
Krystal, G.6
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30
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0030610802
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Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP
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Lamkin TD, Walk SF, Liu L, Damen JE, Krystal G, Ravichandran KS. Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP. J Biol Chem. 272:1997;10396-10401.
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Lamkin, T.D.1
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Liu, L.3
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Krystal, G.5
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Negative signaling via FcgammallB1 in B cells blocks phospholipase Cgamma2 phosphorylation but not Syk or Lyn activation
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Sarkar S, Schlottmann K, Cooney D, Coggeshall KM. Negative signaling via FcgammallB1 in B cells blocks phospholipase Cgamma2 phosphorylation but not Syk or Lyn activation. J Biol Chem. 271:1996;20182-20186.
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Activation of B lymphocytes: Integrating signals from CD19, CD22 and Fc gamma Rllb1
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Doody GM, Dempsey PW, Fearon DT. Activation of B lymphocytes: integrating signals from CD19, CD22 and Fc gamma Rllb1. Curr Opin Immunol. 8:1996;378-382.
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Doody, G.M.1
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Fearon, D.T.3
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34
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0343307005
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Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling
-
note
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2+ influx was restored to levels seen under positive signaling in B cells lacking SHIP but not SHP-1. In contrast, B cells expressing the killer cell inhibitory receptor required a functional SHP-1 but not SHIP gene product. Together, the data indicated that SHP-1 was not required for B cell negative signaling by immunoglobulin Fcγ receptor (FcγR)IIb and that SHIP was essential. Additional experiments indicated that SHIP-deficient B cells undergo greater activation-induced cell death upon triggering of surface immunoglobulin than normal B cells, suggesting that SHIP protects cellsfrom apoptosis upon its recruitment to FcγRIIb.
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Cell
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Ono, M.1
Okada, H.2
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Yanagi, S.4
Kurosaki, T.5
Ravetch, J.V.6
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Protein tyrosine phosphatase SHP-1 is dispensible for FcgammaRIIB-mediated inhibition of B cell antigen receptor activation
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Nadler MJS, Chen B, Anderson JS, Wortis HH, Neel BG. Protein tyrosine phosphatase SHP-1 is dispensible for FcgammaRIIB-mediated inhibition of B cell antigen receptor activation. J Biol Chem. 272:1997;20038-20043.
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36
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0030860518
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Negative signaling pathways of the killer cell inhibitory receptor and Fc gamma RIIb1 require distinct phosphatases
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Gupta N, Scharenberg AM, Burshtyn DN, Wagtmann N, Lioubin MN, Rohrschneider LR, Kinet JP, Long EO. Negative signaling pathways of the killer cell inhibitory receptor and Fc gamma RIIb1 require distinct phosphatases. J Exp Med. 186:1997;473-478.
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Gupta, N.1
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Lioubin, M.N.5
Rohrschneider, L.R.6
Kinet, J.P.7
Long, E.O.8
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37
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Tridandapani S, Kelley T, Cooney D, Pradhan M, Coggeshall KM. Negative signaling in B cells: SHIP Grbs Shc. Immunol Today. 18:1997;424-427.
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38
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Negative signaling in B cells causes reduced Ras activity by reducing Shc-Grb2 interactions
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Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha
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of special interest. This report and that of Stokoe et al., 1997 [63] identified and described some properties of PDK1, a PtdIns-3,4,5P3-responsive kinase that acts immediately upstream of Akt. The authors suggest a model in which PtdIns-3 kinase induces the formation of PtdIns-3,4,5P3, stimulating PDK1 which phosphorylates and activates Akt to promote cell survival.
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Alessi DR, James SR, Downes CP, Holmes AB, Gaffney PR, Reese CB, Cohen P. Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha. of special interest Curr Biol. 7:1997;261-269 This report and that of Stokoe et al., 1997 [63] identified and described some properties of PDK1, a PtdIns-3,4,5P3-responsive kinase that acts immediately upstream of Akt. The authors suggest a model in which PtdIns-3 kinase induces the formation of PtdIns-3,4,5P3, stimulating PDK1 which phosphorylates and activates Akt to promote cell survival.
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Cohen, P.7
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63
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Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein Kinase B
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of special interest. This report and that of Alessi et al., 1997 [62] identified and described some properties of PDK1, a PtdIns-3,4,5P3-responsive kinase that acts immediately upstream of Akt. The authors suggest a model in which PtdIns-3 kinase induces the formation of PtdIns-3,4,5P3, stimulating PDK1 which phosphorylates and activates Akt to promote cell survival.
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Stokoe D, Stephens LR, Copeland T, Gaffney PRJ, Reese CB, Painter GF, Holmes AB, McCormick F, Hawkins PT. Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein Kinase B. of special interest Science. 277:1997;567-570 This report and that of Alessi et al., 1997 [62] identified and described some properties of PDK1, a PtdIns-3,4,5P3-responsive kinase that acts immediately upstream of Akt. The authors suggest a model in which PtdIns-3 kinase induces the formation of PtdIns-3,4,5P3, stimulating PDK1 which phosphorylates and activates Akt to promote cell survival.
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Science
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Stokoe, D.1
Stephens, L.R.2
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Painter, G.F.6
Holmes, A.B.7
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note
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Scharenberg AM, El-Hillal O, Fruman DA, Beitz LO, Li Z, Lin S, Gout I, Cantley LC, Rawlings DJ, Kinet J-P. Phosphatidylinositol-3,4,5-triphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathways: a target for SHIP-mediated inhibitory signals. of special interest EMBO J. 17:1998;1961-1972 These authors demonstrated that over-expression of PtdIns-3 kinase catalytic subunit together with Bruton's tyrosine kinase (Btk) enhanced calcium signaling in B cells. Negative signaling conditions blocked PtdIns-3,4,5P3 accumulation mediated by surface immunoglobulin, phospholipase C (PLC)-γ2 tyrosine phosphorylation, induction of Btk activation and reduced calcium influx. Expression of a wild-type or catalytic-deficient forms of SH2-domain-containing inositol 5-phosphatase (SHIP) in NIH 3T3 fibroblasts blocked or promoted activation of Btk induced by PtdIns-3 kinase. These findings were consistent with those of Sarkar et al., 1996 [31], who observed reduced PLCγ2 tyrosine phosphorylation under negative signaling conditions. The authors interpreted the results to indicate that generation of PtdIns-3,4,5P3 mediated by PtdIns-3 kinase acts proximal to Btk and PLCγ2 tyrosine phosphorylation in the generation of calcium signals and that SHIP, through hydrolysis of PtdIns-3,4,5P3 prevents these events during negative signaling in B cells.
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Lin, S.6
Gout, I.7
Cantley, L.C.8
Rawlings, D.J.9
Kinet J-P10
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