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Volumn 17, Issue 5, 1997, Pages 2559-2565

SIP/SHIP inhibits Xenopus oocyte maturation induced by insulin and phosphatidylinositol 3-kinase

Author keywords

[No Author keywords available]

Indexed keywords

INOSITOL POLYPHOSPHATE; INSULIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATASE; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL 3 KINASE;

EID: 0030948401     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.5.2559     Document Type: Article
Times cited : (60)

References (43)
  • 2
    • 0024601010 scopus 로고
    • PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells
    • Auger, K. R., L. A. Serunian, S. P. Soltoff, P. Libby, and L. C. Cantley. 1989. PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells. Cell 57:167-175.
    • (1989) Cell , vol.57 , pp. 167-175
    • Auger, K.R.1    Serunian, L.A.2    Soltoff, S.P.3    Libby, P.4    Cantley, L.C.5
  • 4
    • 0027436135 scopus 로고
    • Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides
    • Bibbins, K. B., H. Boeuf, and H. E. Varmus. 1993. Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides. Mol. Cell. Biol. 13:7278-7287.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7278-7287
    • Bibbins, K.B.1    Boeuf, H.2    Varmus, H.E.3
  • 8
    • 0028172432 scopus 로고
    • Interactive roles of Ras, insulin receptor substrate-1, and proteins with Src homology-2 domains in insulin signaling in Xenopus oocytes
    • Chuang, L. M., S. F. Hausdorff, M. G. Myers, Jr., M. F. White, M. J. Birnbaum, and C. R. Kahn. 1994. Interactive roles of Ras, insulin receptor substrate-1, and proteins with Src homology-2 domains in insulin signaling in Xenopus oocytes. J. Biol. Chem. 269:27645-27649.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27645-27649
    • Chuang, L.M.1    Hausdorff, S.F.2    Myers Jr., M.G.3    White, M.F.4    Birnbaum, M.J.5    Kahn, C.R.6
  • 9
    • 0027379041 scopus 로고
    • Insulin-stimulated oocyte maturation requires insulin receptor substrate 1 and interaction with the SH2 domains of phosphatidylinositol 3-kinase
    • Chuang, L. M., M. G. Myers, Jr., J. M. Backer, S. E. Shoelson, M. F. White, M. J. Birnbaum, and C. R. Kahn. 1993. Insulin-stimulated oocyte maturation requires insulin receptor substrate 1 and interaction with the SH2 domains of phosphatidylinositol 3-kinase. Mol. Cell. Biol. 13:6653-6660.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6653-6660
    • Chuang, L.M.1    Myers Jr., M.G.2    Backer, J.M.3    Shoelson, S.E.4    White, M.F.5    Birnbaum, M.J.6    Kahn, C.R.7
  • 10
    • 0029892833 scopus 로고    scopus 로고
    • A peroxovanadium compound induces Xenopus oocyte maturation: Inhibition by a neutralizing anti-insulin receptor antibody
    • Cummings, C., L. Zhu, A. Sorisky, and X. J. Liu. 1996. A peroxovanadium compound induces Xenopus oocyte maturation: inhibition by a neutralizing anti-insulin receptor antibody. Dev. Biol. 175:338-346.
    • (1996) Dev. Biol. , vol.175 , pp. 338-346
    • Cummings, C.1    Zhu, L.2    Sorisky, A.3    Liu, X.J.4
  • 11
    • 0029978202 scopus 로고    scopus 로고
    • The 145 kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase
    • Damen, J. E., L. Liu, P. Rosten, R. K. Humphries, A. B. Jefferson, P. W. Majerus, and G. Krystal. 1996. The 145 kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase. Proc. Natl. Acad. Sci. USA 93:1689-1693.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1689-1693
    • Damen, J.E.1    Liu, L.2    Rosten, P.3    Humphries, R.K.4    Jefferson, A.B.5    Majerus, P.W.6    Krystal, G.7
  • 12
    • 0015292069 scopus 로고
    • Oogenesis in Xenopus laevis
    • Dumont, J. N. 1971. Oogenesis in Xenopus laevis. J. Morphol. 136:153-188.
    • (1971) J. Morphol. , vol.136 , pp. 153-188
    • Dumont, J.N.1
  • 13
    • 0031039024 scopus 로고    scopus 로고
    • Direct Regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • Franke, T. F., D. R. Kaplan, L. C. Cantley, and A. Toker. 1997. Direct Regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science 275:665.
    • (1997) Science , vol.275 , pp. 665
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 14
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • Franke, T. F., S. I. Yang, T. O. Chan, K. Datta, A. Kazlauskas, D. K. Morrison, D. R. Kaplan, and P. N. Tsichlis. 1995. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 81:727-736.
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.I.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.K.6    Kaplan, D.R.7    Tsichlis, P.N.8
  • 15
    • 0001192771 scopus 로고
    • High efficiency gene transfer into mammalian cells
    • D. M. Glover (ed.), IRL Press, Oxford, England
    • German, C. 1985. High efficiency gene transfer into mammalian cells, p. 143-190. In D. M. Glover (ed.), DNA cloning, a practical approach, vol. 2. IRL Press, Oxford, England.
    • (1985) DNA Cloning, a Practical Approach , vol.2 , pp. 143-190
    • German, C.1
  • 16
    • 0028004098 scopus 로고
    • Evidence for a role of phosphatidylinositol 3-kinase in the regulation of glucose transport in Xenopus oocytes
    • Gould, G. W., T. J. Jess, G. C. Andrews, J. J. Herbst, R. J. Plevin, and E. M. Gibbs. 1994. Evidence for a role of phosphatidylinositol 3-kinase in the regulation of glucose transport in Xenopus oocytes. J. Biol. Chem. 269: 26622-26625.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26622-26625
    • Gould, G.W.1    Jess, T.J.2    Andrews, G.C.3    Herbst, J.J.4    Plevin, R.J.5    Gibbs, E.M.6
  • 17
    • 0026654026 scopus 로고
    • Platelet-derived growth factor stimulates synthesis of PtdIns(3,4,5)P3 by activating a PtdIns(4,5)P2 3-OH kinase
    • Hawkins, P. T., T. R. Jackson, and L. R. Stephens. 1992. Platelet-derived growth factor stimulates synthesis of PtdIns(3,4,5)P3 by activating a PtdIns(4,5)P2 3-OH kinase. Nature 358:157-159.
    • (1992) Nature , vol.358 , pp. 157-159
    • Hawkins, P.T.1    Jackson, T.R.2    Stephens, L.R.3
  • 18
    • 0028918408 scopus 로고
    • Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase
    • Hu, Q., A. Klippel, A. J. Muslin, W. J. Fantl, and L. T. Williams. 1995. Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase. Science 268:100-102.
    • (1995) Science , vol.268 , pp. 100-102
    • Hu, Q.1    Klippel, A.2    Muslin, A.J.3    Fantl, W.J.4    Williams, L.T.5
  • 19
    • 0029152796 scopus 로고
    • Phosphatidylinositol 3,4,5-trisphosphate is a substrate for the 75 kDa inositol polyphosphate 5-phosphatase and a novel 5-phosphatase which forms a complex with the p85/p110 form of phosphoinositide 3-kinase
    • Jackson, S. P., S. M. Schoenwaelder, M. Matzaris, S. Brown, and C. A. Mitchell. 1995. Phosphatidylinositol 3,4,5-trisphosphate is a substrate for the 75 kDa inositol polyphosphate 5-phosphatase and a novel 5-phosphatase which forms a complex with the p85/p110 form of phosphoinositide 3-kinase. EMBO J. 14:4490-4500.
    • (1995) EMBO J. , vol.14 , pp. 4490-4500
    • Jackson, S.P.1    Schoenwaelder, S.M.2    Matzaris, M.3    Brown, S.4    Mitchell, C.A.5
  • 20
    • 0029982454 scopus 로고    scopus 로고
    • Mutation of the conserved domains of two inositol polyphosphate 5-phosphatases
    • Jefferson, A. B., and P. W. Majerus. 1996. Mutation of the conserved domains of two inositol polyphosphate 5-phosphatases. Biochemistry 35:7890-7894.
    • (1996) Biochemistry , vol.35 , pp. 7890-7894
    • Jefferson, A.B.1    Majerus, P.W.2
  • 21
    • 0028961785 scopus 로고
    • Properties of type II inositol polyphosphate 5-phosphatase
    • Jefferson, A. B., and P. W. Majerus. 1995. Properties of type II inositol polyphosphate 5-phosphatase. J. Biol. Chem. 270:9370-9377.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9370-9377
    • Jefferson, A.B.1    Majerus, P.W.2
  • 22
    • 0028486018 scopus 로고
    • Phosphatidylinositol 3-kinase
    • Kapeller, R., and L. C. Cantley. 1994. Phosphatidylinositol 3-kinase. Bioessays 16:565-576.
    • (1994) Bioessays , vol.16 , pp. 565-576
    • Kapeller, R.1    Cantley, L.C.2
  • 23
    • 0027219681 scopus 로고
    • Single point mutations in the SH2 domain impair the transforming potential of vav and fail to activate proto-vav
    • Katzav, S. 1993. Single point mutations in the SH2 domain impair the transforming potential of vav and fail to activate proto-vav. Oncogene 8:1757-1763.
    • (1993) Oncogene , vol.8 , pp. 1757-1763
    • Katzav, S.1
  • 24
    • 0026742317 scopus 로고
    • Modification of the 85-kilodalton subunit of phosphatidylinositol-3 kinase in platelet-derived growth factor-stimulated cells
    • Kavanaugh, W. M., A. Klippel, J. A. Escobedo, and L. T. Williams. 1992. Modification of the 85-kilodalton subunit of phosphatidylinositol-3 kinase in platelet-derived growth factor-stimulated cells. Mol. Cell. Biol. 12:3415-3424.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3415-3424
    • Kavanaugh, W.M.1    Klippel, A.2    Escobedo, J.A.3    Williams, L.T.4
  • 26
    • 0028198330 scopus 로고
    • The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity
    • Klippel, A., J. A. Escobedo, M. Hirano, and L. T. Williams. 1994. The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity. Mol. Cell. Biol. 14:2675-2685.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2675-2685
    • Klippel, A.1    Escobedo, J.A.2    Hirano, M.3    Williams, L.T.4
  • 27
    • 0031015986 scopus 로고    scopus 로고
    • A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain
    • Klippel, A., W. M. Kavanaugh, D. Pot, and L. T. Williams. 1997. A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain. Mol. Cell. Biol. 17:338-344.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 338-344
    • Klippel, A.1    Kavanaugh, W.M.2    Pot, D.3    Williams, L.T.4
  • 28
    • 0029943605 scopus 로고    scopus 로고
    • Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways
    • Klippel, A., C. Reinhard, W. M. Kavanaugh, G. Apell, M.-A. Escobedo, and L. T. Williams. 1996. Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways. Mol. Cell. Biol. 16:4117-4127.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4117-4127
    • Klippel, A.1    Reinhard, C.2    Kavanaugh, W.M.3    Apell, G.4    Escobedo, M.-A.5    Williams, L.T.6
  • 29
    • 0029665083 scopus 로고    scopus 로고
    • P150ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity
    • Lioubin, M. N., P. A. Algate, S. Tsai, K. Carlberg, R. Aebersold, and L. R. Rohrschneider. 1996. p150ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. Genes Dev. 10:1084-1095.
    • (1996) Genes Dev. , vol.10 , pp. 1084-1095
    • Lioubin, M.N.1    Algate, P.A.2    Tsai, S.3    Carlberg, K.4    Aebersold, R.5    Rohrschneider, L.R.6
  • 30
    • 0029959174 scopus 로고    scopus 로고
    • A novel phosphatidylinositol 3,4,5 trisphosphate 5-phosphatase associates with the interleukin-3 receptor
    • Liu, L., A. B. Jefferson, X. Zhang, F. A. Norris, P. W. Majerus, and G. Krystal. 1996. A novel phosphatidylinositol 3,4,5 trisphosphate 5-phosphatase associates with the interleukin-3 receptor. J. Biol. Chem. 271:29729-29733.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29729-29733
    • Liu, L.1    Jefferson, A.B.2    Zhang, X.3    Norris, F.A.4    Majerus, P.W.5    Krystal, G.6
  • 31
    • 0029067502 scopus 로고
    • Molecular cloning of an amphibian insulin receptor substrate 1-like cDNA and involvement of phosphatidylinositol 3-kinase in insulin-induced Xenopus oocyte maturation
    • Liu, X. J., A. Sorisky, L. Zhu, and T. Pawson. 1995. Molecular cloning of an amphibian insulin receptor substrate 1-like cDNA and involvement of phosphatidylinositol 3-kinase in insulin-induced Xenopus oocyte maturation. Mol. Cell. Biol. 15:3563-3570.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3563-3570
    • Liu, X.J.1    Sorisky, A.2    Zhu, L.3    Pawson, T.4
  • 32
    • 0026453585 scopus 로고
    • Identification of residues in GTPase-activating protein Src homology 2 domains that control binding to tyrosine phosphorylated growth factor receptors and p62
    • Marengere, L. E., and T. Pawson. 1992. Identification of residues in GTPase-activating protein Src homology 2 domains that control binding to tyrosine phosphorylated growth factor receptors and p62. J. Biol. Chem. 267:22779-22786.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22779-22786
    • Marengere, L.E.1    Pawson, T.2
  • 33
    • 0027190850 scopus 로고
    • Raf-1 protein kinase is important for progesterone-induced Xenopus oocyte maturation and acts downstream of mos
    • Muslin, A. J., A. M. MacNicol, and L. T. Williams. 1993. Raf-1 protein kinase is important for progesterone-induced Xenopus oocyte maturation and acts downstream of mos. Mol. Cell. Biol. 13:4197-4202.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4197-4202
    • Muslin, A.J.1    MacNicol, A.M.2    Williams, L.T.3
  • 34
    • 0028347321 scopus 로고
    • A 13-amino-acid motif in the cytoplasmic domain of Fc gamma RIIB modulates B-cell receptor signalling
    • Erratum, 369:340
    • Muta, T., T. Kurosaki, Z. Misulovin, M. Sanchez, M. C. Nussenzweig, and J. V. Ravetch. 1994. A 13-amino-acid motif in the cytoplasmic domain of Fc gamma RIIB modulates B-cell receptor signalling. Nature 368:70-73. (Erratum, 369:340.)
    • (1994) Nature , vol.368 , pp. 70-73
    • Muta, T.1    Kurosaki, T.2    Misulovin, Z.3    Sanchez, M.4    Nussenzweig, M.C.5    Ravetch, J.V.6
  • 35
    • 0027535742 scopus 로고
    • Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-triphosphate
    • Nakanishi, H., K. A. Brewer, and J. H. Exton. 1993. Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-triphosphate. J. Biol. Chem. 268:6-13.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6-13
    • Nakanishi, H.1    Brewer, K.A.2    Exton, J.H.3
  • 36
    • 0029835940 scopus 로고    scopus 로고
    • Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor FcγRIIB
    • Ono, M., S. Bolland, P. Tempst, and J. V. Ravetch. 1996. Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor FcγRIIB. Nature 383:263-266.
    • (1996) Nature , vol.383 , pp. 263-266
    • Ono, M.1    Bolland, S.2    Tempst, P.3    Ravetch, J.V.4
  • 37
    • 0028892253 scopus 로고
    • Phosphatidylinositol (3,4,5)P3 interacts with SH2 domains and modulates PI 3-kinase association with tyrosine-phosphorylated proteins
    • Rameh, L. E., C.-S. Chen, and L. C. Cantley. 1995. Phosphatidylinositol (3,4,5)P3 interacts with SH2 domains and modulates PI 3-kinase association with tyrosine-phosphorylated proteins. Cell 83:821-830.
    • (1995) Cell , vol.83 , pp. 821-830
    • Rameh, L.E.1    Chen, C.-S.2    Cantley, L.C.3
  • 38
    • 0027366440 scopus 로고
    • Agonist-stimulated synthesis of phosphatidylinositol(3,4,5)-trisphosphate: A new intracellular signalling system? Biochim
    • Stephens, L. R., T. R Jackson, and P. T. Hawkins. 1993. Agonist-stimulated synthesis of phosphatidylinositol(3,4,5)-trisphosphate: a new intracellular signalling system? Biochim. Biophys. Acta 1179:27-75.
    • (1993) Biophys. Acta , vol.1179 , pp. 27-75
    • Stephens, L.R.1    Jackson, T.R.2    Hawkins, P.T.3
  • 39
    • 0028788181 scopus 로고
    • Phosphorylation of the platelet p47 phosphoprotein is mediated by the lipid products of phosphoinositide 3-kinase
    • Toker, A., C. Bachelot, C. S. Chen, J. R. Falck, J. H. Hartwig, L. C. Cantley, and T. J. Kovacsovics. 1995. Phosphorylation of the platelet p47 phosphoprotein is mediated by the lipid products of phosphoinositide 3-kinase. J. Biol. Chem. 270:29525-29531.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29525-29531
    • Toker, A.1    Bachelot, C.2    Chen, C.S.3    Falck, J.R.4    Hartwig, J.H.5    Cantley, L.C.6    Kovacsovics, T.J.7
  • 41
    • 0029859565 scopus 로고    scopus 로고
    • Cloning and characterization of human SHIP, the 145 kDa inositol 5-phosphatase that associates with SHC after cytokine stimulation
    • Ware, M. D., P. Rosten, J. E. Damen, L. Liu, R. K. Humphries, and G. Krystal. 1996. Cloning and characterization of human SHIP, the 145 kDa inositol 5-phosphatase that associates with SHC after cytokine stimulation. Blood 88:2833-2840.
    • (1996) Blood , vol.88 , pp. 2833-2840
    • Ware, M.D.1    Rosten, P.2    Damen, J.E.3    Liu, L.4    Humphries, R.K.5    Krystal, G.6
  • 42
    • 0026267136 scopus 로고
    • Raising Xenopus in the laboratory
    • Wu, M., and J. Gerhart. 1991. Raising Xenopus in the laboratory. Methods Cell Biol. 36:1-18.
    • (1991) Methods Cell Biol. , vol.36 , pp. 1-18
    • Wu, M.1    Gerhart, J.2
  • 43
    • 0029084949 scopus 로고
    • Phosphatidylinositol (3,4,5)-trisphosphate stimulates phosphorylation of pleckstrin in human platelets
    • Zhang, J., J. R. Falck, K. K. Reddy, C. S. Abrams, W. Zhao, and S. E. Rittenhouse. 1995. Phosphatidylinositol (3,4,5)-trisphosphate stimulates phosphorylation of pleckstrin in human platelets. J. Biol. Chem. 270:22807-22810.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22807-22810
    • Zhang, J.1    Falck, J.R.2    Reddy, K.K.3    Abrams, C.S.4    Zhao, W.5    Rittenhouse, S.E.6


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