2
Views
49
CrossRef citations to date
0
Altmetric
Research Article

SIP/SHIP Inhibits Xenopus Oocyte Maturation Induced by Insulin and Phosphatidylinositol 3-Kinase

, , , , &
Pages 2559-2565 | Received 12 Dec 1996, Accepted 11 Feb 1997, Published online: 29 Mar 2023

REFERENCES

  • Amigorena, S., C. Bonnerot, J. R. Drake, D. Choquet, W. Hunziker, J. G. Guillet, P. Webster, C. Sautes, I. Mellman, and W. H. Fridman. 1992. Cytoplasmic domain heterogeneity and functions of IgG Fc receptors in B lymphocytes. Science 256:1808–1812.
  • 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.
  • Backer, J. M., M. G. Myers, Jr., S. E. Shoelson, D. J. Chin, X. J. Sun, M. Miralpeix, P. Hu, B. Margolis, E. Y. Skolnik, J. Schlessinger, and M. F. White. 1992. Phosphatidylinositol 3′-kinase is activated by association with IRS-1 during insulin stimulation. EMBO J. 11:3469–3479.
  • 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.
  • Cantley, L. C., K. R. Auger, C. Carpenter, B. Duckworth, A. Graziani, R. Kapeller, and S. Soltoff. 1991. Oncogenes and signal transduction. Cell 64:281–302.
  • Carpenter, C. L., K. R. Auger, M. Chanudhuri, M. Yoakim, B. Schaffhausen, S. Shoelson, and L. C. Cantley. 1993. Phosphoinositide 3-kinase is activated by phosphopeptides that bind to the SH2 domains of the 85-kDa subunit. J. Biol. Chem. 268:9478–9483.
  • Carpenter, C. L., K. R. Auger, B. C. Duckworth, W. M. Huo, B. Schaff-hausen, and L. C. Cantley. 1993. A tightly associated serine/threonine protein kinase regulates phosphoinositide 3-kinase activity. Mol. Cell. Biol. 13:1657–1665.
  • 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.
  • 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.
  • 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.
  • 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 phosphati-dylinositol 3,4,5-trisphosphate 5-phosphatase. Proc. Natl. Acad. Sci. USA 93:1689–1693.
  • Dumont, J. N. 1971. Oogenesis in Xenopus laevis. J. Morphol. 136:153–180.
  • 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.
  • 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 phos-phatidylinositol 3-kinase. Cell 81:727–736.
  • Gorman, 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.
  • 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.
  • 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.
  • Hu, Q., A. Klippel, A. J. Muslin, W. J. Fantl, and L. T. Williams. 1995. Ras-dependent induction of cellular responses by constitutively active phos-phatidylinositol-3 kinase. Science 268:100–102.
  • 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.
  • Jefferson, A. B., and P. W. Majerus. 1996. Mutation of the conserved domains of two inositol polyphosphate 5-phosphatases. Biochemistry 35:7890–7894.
  • Jefferson, A. B., and P. W. Majerus. 1995. Properties of type II inositol polyphosphate 5-phosphatase. J. Biol. Chem. 270:9370–9377.
  • Kapeller, R., and L. C. Cantley. 1994. Phosphatidylinositol 3-kinase. Bioes-says 16:565–576.
  • 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.
  • 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.
  • Kavanaugh, W. M., D. A. Pot, S. M. Chin, M. Deuter-Reinhard, A. B. Jefferson, F. A. Norris, F. R. Masiarz, L. S. Cousens, P. W. Majerus, and L. T. Williams. 1996. Multiple forms of an inositol polyphosphate 5-phos-phatase form signaling complexes with SHC and GRB2. Curr. Biol. 6:438–445.
  • 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.
  • 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.
  • Klippel, A., C. Reinhard, W. M. Kavanaugh, G. Apell, M.-A. Escobedo, and L. T. Williams. 1996. Membrane localization of phosphatidylinositol 3-ki-nase is sufficient to activate multiple signal-transducing kinase pathways. Mol. Cell. Biol. 16:4117–4127.
  • 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.
  • 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-phospha-tase associates with the interleukin-3 receptor. J. Biol. Chem. 271:29729–29733.
  • 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 phos-phatidylinositol 3-kinase in insulin-induced Xenopus oocyte maturation. Mol. Cell. Biol. 15:3563–3570.
  • 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.
  • 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.
  • 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.)
  • 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.
  • 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 Fc7RIIB. Nature 383:263–266.
  • 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.
  • 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.
  • 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 phospho-protein is mediated by the lipid products of phosphoinositide 3-kinase. J. Biol. Chem. 270:29525–29531.
  • Toker, A., M. Meyer, K. K. Reddy, J. R. Falck, R. Aneja, S. Aneja, A. Parra, D. J. Burns, L. M. Ballas, and L. C. Cantley. 1994. Activation of protein kinase C family members by the novel polyphosphoinositides PtdIns-3,4-P2 and PtdIns-3,4,5-P3. J. Biol. Chem. 269:32358–32367.
  • 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.
  • Wu, M., and J. Gerhart. 1991. Raising Xenopus in the laboratory. Methods Cell Biol. 36:1–18.
  • 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.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.