Activation Mechanisms of Phospholipase C Isozymes

  • Sue Goo Rhee
Chapter
Part of the NATO ASI Series book series (NSSA, volume 246)

Abstract

On binding to their cell surface receptors, many extracellular signaling molecules including hormones, peptide growth factors, neurotransmitters and immunoglobulins, elicit intracellular responses by activating inositol phospholipid-specific phospholipase C (PLC).1 Activated PLC catalyzes the hydrolysis of phosphatidylinositol 4, 5-bisphosphate (PIP2) to generate diacylglycerol and inositol 1, 4, 5-trisphosphate (IP3). Diacylglycerol is the physiological activator of protein kinase C (PKC) and IP3 induces the release of Ca2+ from internal stores.1 This bifurcating pathway constitutes the cornerstone of a transmembrane signal transduction mechanism that is now known to regulate a large array of cellular processes, including metabolism, secretion, contraction, neural activity, and proliferation.

Keywords

Nerve Growth Factor Tyrosine Phosphorylation Mutant Epidermal Growth Factor Receptor Inositol Phosphate Formation Mutant Epidermal Growth Factor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    R.S. Rana and L.E. Hokin, Role of phosphoinositides in transmembrane signaling, Physiol. Rev. 70: 115–164 (1990).PubMedGoogle Scholar
  2. 2.
    S.G. Rhee, P.G. Suh, S.H. Ryu, and S.Y. Lee, Studies of inositol phospholipid-specific phospholipase C, Science 244: 546–550 (1989).PubMedCrossRefGoogle Scholar
  3. 3.
    S.G. Rhee, and K.D. Choi, Multiple forms of phospholipase C isozymes and their activation mechanisms, in: “Advances in Second Messenger and Phosphoprotein Research,” J.W. Putney, Jr., ed., Raven Press, New York, pp. 35–60 (1992)Google Scholar
  4. 4.
    A.C. Koch, D.A. Anderson, M.F. Moran, C. Ellis, and T. Pawson, T., SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins, Science 252: 668–674 (1991).PubMedCrossRefGoogle Scholar
  5. 5.
    S.P. Srivastava, N.Q. Chen, Y.X. Liu, and J.L. Holtzman, Purification and characterization of a new isozyme of thiol: protein-disulfide oxidoreductase from rat hepatic microsomes, J. Biol. Chem. 266: 20337–20344 (1991).PubMedGoogle Scholar
  6. 6.
    M.I. Simon, M.P. Strathmann, and N. Gautam, Diversity of G proteins in signal transduction, Science 252: 802–808 (1991).PubMedCrossRefGoogle Scholar
  7. 7.
    A.V. Smrcka, J.R. Hepler, K.O. Brown, and P.O. Sternweis, Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq, Science 250: 804–807 (1991).CrossRefGoogle Scholar
  8. 8.
    S.J. Taylor, H.Z. Chae, S.G. Rhee, and J.H. Exton, Activation of the ß1 isozyme of phospholipase C by α subunits of the Gq class of G protein, Nature 350: 516–518 (1991).PubMedCrossRefGoogle Scholar
  9. 9.
    J.L. Blank, A.H. Ross, and J.H. Exton, Purification and characterization of two G-proteins that activate the ßl isozyme of phosphoinositide-specific phospholipase C, J. Biol. Chem. 266: 18206–18216 (1991).PubMedGoogle Scholar
  10. 10.
    G. Waldo, J. Boyer, A. Morris, and T.K. Harden, Purification of an A1F4-and G-protein ßγ-subunit-regulated phospholipase C-activating protein, J. Biol. Chem. 266: 14217–14225 (1991).PubMedGoogle Scholar
  11. 11.
    A. Shenker, P. Goldsmith, C.G. Unson, and A.M. Spiegel, The G protein coupled to the thromboxane A2 receptor in human platelets is a member of the novel G family, J. Biol. Chem. 266: 9309–9313 (1991).PubMedGoogle Scholar
  12. 12.
    R.L. Wange, A.V. Smrcka, P.C. Sternweis, and J.H. Exton, Photoaffmity labeling of two rat liver plasma membrane proteins with [32P]γ-azidoanilido GTP in response to vasopressin, J. Biol. Chem. 266: 11409–11412 (1991).PubMedGoogle Scholar
  13. 13.
    S. Gutowski, A. Smrcka, L. Nowak, D. Wu, M. Simon, and P.C. Sternweis, Antibodies to the αq subfamily of guanine nucleotide-binding regulatory protein α subunits attenuate activation of phosphatidylinositol 4, 5-bisphosphate hydrolysis by hormones, J. Biol. Chem. 266: 20519–20524 (1991).PubMedGoogle Scholar
  14. 14.
    S.K.-F. Wong, E.M. Parker, and E.M. Ross, Chimeric muscarinic cholinergic: ß-adrenergic receptors that activate Gs in response to muscarinic agonists, J. Biol. Chem. 265: 6219–6224 (1990).PubMedGoogle Scholar
  15. 15.
    D. Wu, C.H. Lee, S.G. Rhee, and M.I. Simon, Activation of phospholipase C by the α subunits of the Gq and G11 proteins in transfected Cos-7 cells, J. Biol. Chem. 267: 1811–1817 (1992).PubMedGoogle Scholar
  16. 16.
    D. Park, D.-Y. Jhon, R. Kriz, J. Knopf, and S.G. Rhee, Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-ß2, J. Biol. Chem., in press (1992).Google Scholar
  17. 17.
    C.H. Lee, D. Park, D. Wu, S.G. Rhee, and M.I. Simon, Members of the Gq α subunit gene family activate phospholipase C-ß isozymes, J. Biol. Chem., in press (1992).Google Scholar
  18. 18.
    G. Berstein, J.L. Blank, D.-Y. Jhon, J.H. Exton, S.G. Rhee, and E.M. Ross, Phospholipase C-ßl is a GTPase activating protein (GAP) for Gq/11, its physiologic regulator, Cell, in press (1992).Google Scholar
  19. 19.
    D. Rotin, B. Margolis, M. Mohammadi, R. Daly, G. Daum, N. Li, W. Burgess, E.H. Fischer, A. Ullrich, and J. Schlessinger, SH2 domains prevent tyrosine dephosphorylation of the EGF receptor: Identification of Tyr992 as the high-affinity binding site for SH2 domains of phospholipase C-γ, EMBO J. 11: 559–567 (1992).PubMedGoogle Scholar
  20. 20.
    M. Mohammadi, A.M. Honegger, D. Rotin, R. Fischer, F. Bellot, W. Li, C.A. Dionne, M. Jaye, M. Rubinstein, and J. Schlessinger, A tyrosinephosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Fig) is a binding site for the SH2 domain of phospholipase C-γ1, Mol. Cell. Biol. 11: 5068–5078 (1991).PubMedGoogle Scholar
  21. 21.
    H.K. Kim, J.W. Kim, A. Zilberstein, B. Margolis, C.K. Kim, J. Schlessinger, and S.G. Rhee, PDGF stimulation of inositol phospholipid hydrolysis requires PLC-γ1 phosphorylation on tyrosine residues 783 and 1254, Cell 65: 435–441 (1991).PubMedCrossRefGoogle Scholar
  22. 22.
    D. Rotin, A.M. Honegger, B.L. Margolis, A. Ullrich, and J. Schlessinger, Presence of SH2 domains of phospholipase Cγ1 enhances substrate phosphorylation by increasing the affinity towards the EGF-receptor, J. Biol Chem., in press (1992).Google Scholar
  23. 23.
    Q.C. Vega, C. Cochet, O. Filhol, C.P. Chang, S.G. Rhee, and G.N. Gill, A site of tyrosine phosphorylation in the C terminus of the epidermal growth factor receptor is required to activate phospholipase C, Mol. Cell. Biol. 12: 128–135 (1992).PubMedGoogle Scholar
  24. 24.
    M.I. Wahl, G.A. Jones, S. Nishibe, S.G. Rhee, and G. Carpenter, Growth factor stimulation of phospholipase C-γ1 activity: Comparative properties of control and activated enzymes, J. Biol Ghem., in press (1992).Google Scholar
  25. 25.
    P.J. Goldschmidt-Clermont, J.W. Kim, L.M. Machesky, S.G. Rhee, and T.D. Pollard, Regulation of phospholipase C-γ1 by profilin and tyrosine phosphorylation, Science 251: 1231–1233 (1991).PubMedCrossRefGoogle Scholar
  26. 26.
    D.G. Drubin, J. Mulholland, Z. Zhu, and D. Botstein, Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I, Nature 343: 288–290 (1990).PubMedCrossRefGoogle Scholar
  27. 27.
    G. Todderud, M.I. Wahl, S.G. Rhee, and G. Carpenter, Stimulation of phospholipase C-γ1 membrane association by epidermal growth factor, Science 249: 296–299 (1990).PubMedCrossRefGoogle Scholar
  28. 28.
    S.G. Rhee, D.J. Park, and D. Park, Regulation of phospholipase C isozymes, in “Cellular and Molecular Mechanisms of Inflammation: Signal Transduction,” C.G. Cochrane and M.A. Gimbrone, eds., Academic Press, New York, in press (1992).Google Scholar
  29. 29.
    D.J. Park, H.W. Rho, and S.G. Rhee, CD3 stimulation causes phosphorylation of phospholipase C-γ1 on serine and threonine residues in a human T-cell line, Troc. Natl. Acad. Sci. U.S.A. 88: 5453–5456 (1991).CrossRefGoogle Scholar
  30. 30.
    F. Liao, H.S. Shin, and S.G. Rhee, Tyrosine phosphorylation of phospholipase C-γ1 induced by cross-linking of the high-affinity or low-affinity Fc receptor for IgG in U937 cells, Proc. Natl. Acad. Sci. U.S.A., in press (1992).Google Scholar

Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Sue Goo Rhee
    • 1
  1. 1.Laboratory of Biochemistry National Heart, Lung and Blood InstituteNational Institutes of HealthBethesdaUSA

Personalised recommendations