Role of GTP-Binding Proteins in FcεRI Signaling

  • Anna Koffer
Part of the Molecular Biology Intelligence Unit book series (MBIU)

Abstract

Direct evidence for the involvement of specific GTPases in the response of mast cells or the related rat basophilic leukemia (RBL-2H3) cells to FcεRI activation is limited. However, several lines of circumstantial evidence point to the crucial role of GTP-binding proteins in the response of mast or RBL-2H3 cells to FcεRI activation. These include the effects of GTP depletion, of inhibition of the isoprenoid pathway and of various inhibitors and stimulators of GTP-binding proteins. Such experiments will be described in the first section of this chapter. Due to my interest in the mechanism of exocytosis, this and the last section are biased towards the secretory responses to activation of FcεRI and of GTP-binding proteins.

Keywords

Lipase Histamine Dexamethasone Integrin Nucleoside 

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References

  1. 1.
    Park DJ, Min HK, Rhee SG. IgE-induced tyrosine phosphorylation of phospholipase C-gammal in rat basophilic leukemia cells. J Biol Chem 1991; 266: 24237–40.PubMedGoogle Scholar
  2. 2.
    Deanin GG, Martinez AM, Pfeiffer JR et al. Tyrosine kinase-dependent phosphatidylinostiol turnover and functional responses in the FceRl signaling pathway. Biochem Biophys Res Commun 1991; 179: 551–7.PubMedCrossRefGoogle Scholar
  3. 3.
    Beaven MA, Metzger H. Signal transduction by Fc receptors: the FceRI case. Immunol Today 1993; 14: 222–6.PubMedCrossRefGoogle Scholar
  4. 4.
    DeFranco AL. Transmembrane signaling by antigen receptors of B and T lymphocytes. Current Biology 1995; 7: 163–75.Google Scholar
  5. 5.
    Wilson BS, Deanin GG, Standefer JC et al. Depletion of guanine nucleotides with mycophenolic acid suppresses IgE receptor-mediated degranulation in rat basophilic leukemia cells. J Immunol 1989; 143: 259–65.PubMedGoogle Scholar
  6. 6.
    Casey PJ. Lipid modification of G proteins. Curr Opin Cell Biol 1994; 6: 219–25.PubMedCrossRefGoogle Scholar
  7. 7.
    Deanin GG, Cutts JL, Pfeiffer JR et al. Role of isoprenoid metabolism in IgE receptor-mediated signal transduction. J Immunol 1991; 146: 3528–35.PubMedGoogle Scholar
  8. 8.
    Shakarjian MP, Eiseman E, Penhallow RC et al. 3-Hydroxy-3-methylglutaryl-coenzyme A reductase inhibition in a rat mast cell line. Impairment of tyrosine kinase-dependent signal transduction and the subsequent degranulation response. J Biol Chem 1993; 268: 15252–9.PubMedGoogle Scholar
  9. 9.
    Saito H, Okajima F, Molski TFP et al. Effects of ADP-ribosylation of GTP-binding protein by pertussis toxin on immunoglobulin E-dependent and -independent histamine release from mast cells and basophils. J Immunol 1987; 138: 3927–34.PubMedGoogle Scholar
  10. 10.
    Warner JA, Yancey KB, MacGlashan DW. The effect of pertussis toxin on mediator release from human basophils. J Immunol 1987; 139: 161–5.PubMedGoogle Scholar
  11. 11.
    Ali H, Cunho-Melo JR, Beaven MA. Activation of phospholipase C via adenosine receptors provides synergistic signals for secretion in antigen stimulated RBL-2H3 cells. Evidence for a novel adenosine receptor. J Biol Chem 1990; 265: 745–53.PubMedGoogle Scholar
  12. 12.
    McCloskey MA. Cholera toxin potentiates IgE-coupled inositol phospholipid hydrolysis and mediator secretion by RBL-2H3 cells. Proc Natl Acad Sci USA 1988; 85: 7260–4.PubMedCrossRefGoogle Scholar
  13. 13.
    Narasimhan V, Holowka D, Fewtrell C et al. Cholera toxin increases the rate of antigen-stimulated calcium influx in rat basophilic leukemia cells. J Biol Chem 1988; 263: 19626–32X.PubMedGoogle Scholar
  14. 14.
    Hide M, Ali H, Price SR et al. GTP-binding protein GE(aZ): Its down-regulation by dexamethasone and its credentials as a mediator of antigen-induced responses in RBL-2H3 cells. Mol Pharmacol 1991; 40: 473–9.PubMedGoogle Scholar
  15. 15.
    Aridor M, Rajmilevich G, Beaven MA et al. Activation of exocytosis by the heterotrimeric G protein Gi3. Science 1993; 262: 1569–72.PubMedCrossRefGoogle Scholar
  16. 16.
    Gomperts BD. Involvement of guanine nucleotide-binding proteins in the gating of Caz+ by receptors. Nature 1983; 306: 64–6.PubMedCrossRefGoogle Scholar
  17. 17.
    Fernandez JM, Neher E, Gomperts BD. Capacitance measurements reveal stepwise fusion events in degranulating mast cells. Nature 1984; 312: 453–5.PubMedCrossRefGoogle Scholar
  18. 18.
    Cockcroft S, Howell TW, Gomperts BD. Two G proteins act in series to control stimulus-secretion coupling in mast cells: Use of neomycin to distinguish between G proteins controlling polyphosphoinositide phosphodiesterase and exocytosis. J Cell Biol 1987; 105: 2745–50.PubMedCrossRefGoogle Scholar
  19. 19.
    Howell TW, Cockcroft S, Gomperts BD. Essential synergy between Caz’ and guanine nucleotides in exocytotic secretion from permeabilized mast cells. J Cell Biol 1987; 105: 191–7.PubMedCrossRefGoogle Scholar
  20. 20.
    Ali H, Collado-Escobar DM, Beaven MA. The rise in concentration of free Caz’ and of pH provides sequential, synergistic signals for secretion in antigen-stimulated RBL- 2H3 cells. J Immunol 1989; 143: 2626–33.PubMedGoogle Scholar
  21. 21.
    Luini A, De Matteis MA. Evidence that receptor-linked G protein inhibits exocytosis by a post-second-messenger mechanism in AtT-20 cells. J Neurochem 1990; 54: 30–8.PubMedCrossRefGoogle Scholar
  22. 22.
    Buccione R, Di Tullio G, Caretta M et al. Analysis of protein kinase C requirement for exocytosis in permeabilized RBL-2H3 cells: a GTP-binding protein(s) as a potential target for protein kinase C. Biochem J 1994; 298: 149–56.PubMedGoogle Scholar
  23. 23.
    Ishizaka T. Role of GTP-binding protein in histamine release from mast cells. Clin Immunol Immunopathol 1989; 50: 20–9.PubMedCrossRefGoogle Scholar
  24. 24.
    Ali H, Cunha-Melo JR, Beaven MA. Receptor-mediated release of inositol 1,4,5trisphosphate and inositol 1,4-bisphosphate in rat basophilic leukemia RBL-2H3 cells permeabilized with streptolysin O. Biochim Biophys Acta 1989; 1010: 88–99.PubMedCrossRefGoogle Scholar
  25. 25.
    Aridor M, Traub LM, Sagi-Eisenberg R. Exocytosis in mast cells by basic secretagogues: Evidence for direct activation of GTP-binding proteins. J Cell Biol 1990; 111: 909–17.PubMedCrossRefGoogle Scholar
  26. 26.
    Churcher Y, Allan D, Gomperts BD. Relationship between arachidonate generation and exocytosis in permeabilized mast cells. Biochem J 1990; 266: 157–63.PubMedGoogle Scholar
  27. 27.
    Okano Y, Yamada K, Yano K et al. Guanosine 5’-(gamma-thio)triphosphate stimulates arachidonic acid liberation in permeabilized rat peritoneal mast cells. Biochem Biophys Res Commun 1987; 145: 1267–75.PubMedCrossRefGoogle Scholar
  28. 28.
    Truett AP, Snyderman R, Murray JJ. Stimulation of phosphorylcholine turnover and diacylglycerol production in human polymorphonuclear leukocytes. Novel assay for phosphorylcholine. Biochem J 1989; 260: 909–13.PubMedGoogle Scholar
  29. 29.
    Hirasawa N, Santini F, Beaven MA. Activation of the mitogen-activated protein kinase/cytosolic PLA2 pathway in a rat mast cell line. J Immunol 1995; 154: 5391–402.PubMedGoogle Scholar
  30. 30.
    Fasolato C, Hoth M, Penner R. A GTPdependent step in the activation mechanism of capacitative calcium influx. J Biol Chem 1993; 268: 20737–40.PubMedGoogle Scholar
  31. 31.
    Qian YX, McCloskey MA. Activation of mast cell K’ channels through multiple G protein-linked receptors. Proc Natl Acad Sci USA 1993; 90: 7844–8.PubMedCrossRefGoogle Scholar
  32. 32.
    Norman JC, Price LS, Ridley AJ et al. Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins. J Cell Biol 1994; 126 (4): 1005–15.PubMedCrossRefGoogle Scholar
  33. 33.
    Borovikov YS, Norman JC, Price LS et al. Secretion from permeabilized mast cells is enhanced by addition of gelsolin: contrasting effects of endogenous gelsolin. J Cell Sci 1995; 108: 657–66.PubMedGoogle Scholar
  34. 34.
    Tatham PER, Gomperts BD. In: Siddle K et al, eds. Peptide Hormones-A Practical Approach. Oxford: IRL Press, 1990: 257–69.Google Scholar
  35. 35.
    Koffer A, Gomperts BD. Soluble proteins as modulators of the exocytotic reaction of permeabilized rat mast cells. J Cell Sci 1989; 94: 585–91.PubMedGoogle Scholar
  36. 36.
    Churcher Y, Gomperts BD. ATP dependent and ATP independent pathways of exocytosis revealed by interchanging glutamate and chloride as the major anion in permeabilized mast cells. Cell Regul 1990; 1: 337–46.PubMedGoogle Scholar
  37. 37.
    Koffer A. Calcium-induced secretion from permeabilized rat mast cells: requirements for guanine nucleotides. Biochim Biophys Acta 1993; 1176: 236–44.Google Scholar
  38. 38.
    Koffer A, Churcher Y. Calcium and GTPgamma-S as single effectors of secretion from permeabilized rat mast cells: requirements for ATP. Biochim Biophys Acta 1993; 1176: 222–30.PubMedCrossRefGoogle Scholar
  39. 39.
    Lillie THW, Gomperts BD. Guanine nucleotide is essential, Cat’ is a modulator, in the exocytotic reaction of permeabilized rat mast cells. Biochem J 1992; 288: 181–7.PubMedGoogle Scholar
  40. 40.
    Price LS, Norman JC, Ridley AJ et al. Small GTPases, rac and rho, as regulators of secretion in mast cells. Current Biology 1995; 5 (1): 68–73.PubMedCrossRefGoogle Scholar
  41. 41.
    Liao F, Shin HS, Rhee SG. Tyrosine phosphorylation of phospholipase C-gammal induced by crosslinking of the high affinity or low-affinity Fc receptor for IgG in U937 cells. Proc Nat Acad Sci USA 1992; 89: 3659–63.PubMedCrossRefGoogle Scholar
  42. 42.
    Lee SB, Rhee SG. Significance of PIP2 hydrolysis and regulation of phospholipase C isozymes. Curr Opin Cell Biol 1995; 7: 183–9.PubMedCrossRefGoogle Scholar
  43. 43.
    Takai Y, Kaibuchi K, Kikuchi A et al. Small GTP-binding proteins. Int Rev Cytol 1992; 133: 187–230.PubMedCrossRefGoogle Scholar
  44. 44.
    Hall A. Ras-related proteins. Curr Opin Cell Biol 1993; 5: 265–8.PubMedCrossRefGoogle Scholar
  45. 45.
    Kahn RA, der CJ, Bokoch GM. The ras superfamily of GTP-binding proteins: guidelines on nomenclature [news]. FASEB J 1992; 6: 2512–3.PubMedGoogle Scholar
  46. 46.
    Boguski MS, McCormick F. Proteins regulating ras and its relatives. Nature 1993; 366: 643–53.PubMedCrossRefGoogle Scholar
  47. 47.
    Mayer BJ, Baltimore D. Signalling through SH2 and SH3 domains. Trends in Cell Biol 1993; 3: 8–13.CrossRefGoogle Scholar
  48. 48.
    Harlan JE, Hajduk PJ, Yoon HS et al. Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature 1994; 371: 168–70.PubMedCrossRefGoogle Scholar
  49. 49.
    Quilliam LA, Khosravi FR, Huff SY et al. Guanine nucleotide exchange factors: activators of the Ras superfamily of proteins. Bio Essays 1995; 17: 395–404.Google Scholar
  50. 50.
    McCormick F. How receptors turn ras on. Nature 1993; 363: 15–7.PubMedCrossRefGoogle Scholar
  51. 51.
    Rozakis AM, Fernley R, Wade J et al. The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos. Nature 1993; 363: 83–5.CrossRefGoogle Scholar
  52. 52.
    Gale NW, Kaplan S, Lowenstein EJ et al. Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras. Nature 1993; 363: 88–92.PubMedCrossRefGoogle Scholar
  53. 53.
    Li N, Batzer A, Daly R et al. Guaninenucleotide-releasing factor hSosl binds to Grb2 and links receptor tyrosine kinases to Ras signalling. Nature 1993; 363: 85–8.PubMedCrossRefGoogle Scholar
  54. 54.
    Smit L, de Vries Smits AM, Bos JL et al. B cell antigen receptor stimulation induces formation of a Shc-Grb2 complex containing multiple tyrosine-phosphorylated proteins. J Biol Chem 1994; 269: 20209–12.PubMedGoogle Scholar
  55. 55.
    Saxton TM, van Oostveen I, Bowtell D et al. B cell antigen receptor crosslinking induces phosphorylation of the p2lras oncoprotein activators SHC and mSOS1 as well as assembly of complexes containing SHC, GRB-2, mSOS1, and a 145 kDa tyrosine-phosphorylated protein. J Immunol 1994; 153: 623–36.PubMedGoogle Scholar
  56. 56.
    Ravichandran KS, Lee KK, Songyang Z et al. Interaction of Shc with the zeta chain of the T cell receptor upon T cell activation. Science 1993; 262: 902–5.PubMedCrossRefGoogle Scholar
  57. 57.
    Buday L, Egan SE, Rodriguez Viciana P et al. A complex of Grb2 adaptor protein, Sos exchange factor, and a 36 kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells. J Biol Chem 1994; 269: 9019–23.PubMedGoogle Scholar
  58. 58.
    Sieh M, Batzer A, Schlessinger J et al. GRB2 and phospholipase C-gamma 1 associate with a 36- to 38-kilodalton phosphotyrosine protein after T cell receptor stimulation. Mol Cell Biol 1994; 14: 4435–42.PubMedGoogle Scholar
  59. 59.
    Reif K, Buday L, Downward J et al. SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: the guanine nucleotide exchange protein Sos and a 75 kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases. J Biol Chem 1994; 269: 14081–7.PubMedGoogle Scholar
  60. 60.
    Downward J, Graves JD, Warne PH et al. Stimulation of p2lras upon T cell activation. Nature 1990; 346: 719–23.PubMedCrossRefGoogle Scholar
  61. 61.
    Izquierdo M, Downward J, Graves JD et al. Role of protein kinase C in T cell antigen receptor regulation of p2lras: evidence that two p2lras regulatory pathways coexist in T cells. Mol Cell Biol 1992; 12: 3305–12.PubMedGoogle Scholar
  62. 62.
    Turner H, Reif K, Rivera J et al. Regulation of the adapter molecule Grb2 by the FceR1 in the mast cell line RBL-2H3. J Biol Chem 1995; 270: 9500–6.PubMedCrossRefGoogle Scholar
  63. 63.
    Bar-Sagi D, Gomperts BD. Stimulation of exocytotic degranulation by microinjection of the ras oncogenic protein into rat mast cells. Oncogene 1988; 3: 463–9.PubMedGoogle Scholar
  64. 64.
    Margolis B, Hu P, Katzav S et al. Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs. Nature 1992; 356: 71–4.PubMedCrossRefGoogle Scholar
  65. 65.
    Katzav S, Martin ZD, Barbacid M. vav, a novel human oncogene derived from a locus ubiquitously expressed in hematopoietic cells. EMBO J 1989; 8: 2283–90.PubMedGoogle Scholar
  66. 66.
    Adams JM, Houston H, Allen J et al. The hematopoietically expressed vav protooncogene shares homology with the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene (CDC24) involved in cytoskeletal organization. Oncogene 1992; 7: 611–8.PubMedGoogle Scholar
  67. 67.
    Puil L, Pawson T. Vagaries of Vay. Current Biology 1992; 2 (5): 275–7.PubMedCrossRefGoogle Scholar
  68. 68.
    Bustelo XR, Ledbetter JA, Barbacid M. Product of vav proto-oncogene defines a new class of tyrosine protein kinase substrates. Nature 1992; 356: 68–71.PubMedCrossRefGoogle Scholar
  69. 69.
    Hirasawa N, Scharenberg A, Yamamura H et al. A requirement for Syk in the activation of the microtubule-associated protein kinase/phospholipase A2 pathway by FceRI is not shared by a G protein-coupled receptor. J Biol Chem 1995; 270: 10960–7.PubMedCrossRefGoogle Scholar
  70. 70.
    Gulbins E, Coggeshall KM, Baier G et al. Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation. Science 1993; 260: 822–5.PubMedCrossRefGoogle Scholar
  71. 71.
    Gulbins E, Langlet C, Baier G et al. Tyrosine phosphorylation and activation of Vav GTP/GDP exchange activity in antigen receptor-triggered B cells. J Immunol 1994; 152: 2123–9.PubMedGoogle Scholar
  72. 72.
    Gulbins E, Coggeshall KM, Baier G et al. Direct stimulation of Vav guanine nucleotide exchange activity for Ras by phorbol esters and diglycerides. Mol Cell Biol 1994; 14: 4749–58.PubMedGoogle Scholar
  73. 73.
    Bustelo XR, Suen KL, Leftheris K et al. Vav cooperates with Ras to transform rodent fibroblasts but is not a Ras GDP/GTP exchange factor. Oncogene 1994; 9: 2405–13.PubMedGoogle Scholar
  74. 74.
    Khosravi FR, Chrzanowska WM, Solski PA et al. Dbl and Vav mediate transformation via mitogen-activated protein kinase pathways that are distinct from those activated by oncogenic Ras. Mol Cell Biol 1994; 14: 6848–57.Google Scholar
  75. 75.
    Kazanietz MG, Bustelo XR, Barbacid M et al. Zinc finger domains and phorbol ester pharmacophore. Analysis of binding to mutated form of protein kinase C zeta and the vav and c-raf proto-oncogene products. J Biol Chem 1994; 269: 11590–4.PubMedGoogle Scholar
  76. 76.
    Ramos MF, Druker BJ, Fischer S. Vav binds to several SH2/SH3 containing proteins in activated lymphocytes. Oncogene 1994; 9: 1917–23.Google Scholar
  77. 77.
    Avruch J, Zhang XF, Kyriakis JM. Raf meets Ras: completing the framework of a signal transduction pathway. Trends Biochem Sci 1994; 19: 279–83.PubMedCrossRefGoogle Scholar
  78. 78.
    Leevers SJ, Paterson HF, Marshall CJ. Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature 1994; 369: 411–4.PubMedCrossRefGoogle Scholar
  79. 79.
    Tordai A, Franklin RA, Patel H et al. Crosslinking of surface IgM stimulates the Ras/Raf-1/MEK/MAPK cascade in human B lymphocytes. J Biol Chem 1994; 269: 7538–43.PubMedGoogle Scholar
  80. 80.
    Franklin RA, Tordai A, Patel H et al. Ligation of the T cell receptor complex results in activation of the Ras/Raf-1/MEK/ MAPK cascade in human T lymphocytes. J Clin Invest 1994; 93: 2134–40.PubMedCrossRefGoogle Scholar
  81. 81.
    Woodrow M, Clipstone NA, Cantrell D. p2lras and calcineurin synergize to regulate the nuclear factor of activated T cells. J Exp Med 1993; 178: 1517–22.PubMedCrossRefGoogle Scholar
  82. 82.
    Santini F, Beaven MA. Tyrosine phosphorylation of a mitogen-activated protein kinase-like protein occurs at a late step in exocytosis. Studies with tyrosine phosphatase inhibitors and various secretagogues in rat RBL-2H3 cells. J Biol Chem 1993; 268: 22716–22.PubMedGoogle Scholar
  83. 83.
    Offermanns S, Jones SV, Bombien E et al. Stimulation of mitogen-activated protein kinase activity by different secretory stimuli in rat basophilic leukemia cells. J Immunol 1994; 152: 250–61.PubMedGoogle Scholar
  84. 84.
    Fruman DA, Bierer BE, Benes JE et al. The complex of FK506-binding protein 12 and FK506 inhibits calcineurin phosphatase activity and IgE activation-induced cytokine transcripts, but not exocytosis, in mouse mast cells. J Immunol 1995; 154: 1846–51.PubMedGoogle Scholar
  85. 85.
    Franklin RA, Tordai A, Patel H et al. Ligation of the T cell receptor complex results in activation of the Ras/Raf-1/MEK/MAPK cascade in human T lymphocytes. J Clin Invest 1994; 93: 2134–40.PubMedCrossRefGoogle Scholar
  86. 86.
    Siegel JN, June CH, Yamada H et al. Rapid activation of C-Raf-1 after stimulation of the T cell receptor or the muscarinic receptor type 1 in resting T cells. J Immunol 1993; 151: 4116–27.PubMedGoogle Scholar
  87. 87.
    Burgering BM, Bos JL. Regulation of Ras-mediated signalling: more than one way to skin a cat. Trends Biochem Sci 1995; 20: 18–22.PubMedCrossRefGoogle Scholar
  88. 88.
    Crespo P, Xu N, Simonds WF, Gutkind JS. Ras-dependent activation of MAP kinase pathway mediated by G protein beta gamma subunits. Nature 1994; 369: 418–20.PubMedCrossRefGoogle Scholar
  89. 89.
    Egan SE, Weinberg RA. The pathway to signal achievement. Nature 1993; 365: 781–3.PubMedCrossRefGoogle Scholar
  90. 90.
    Tanaka S, Morishita T, Hashimoto Y et al. C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins. Proc Natl Acad Sci USA 1994; 91: 3443–7.PubMedCrossRefGoogle Scholar
  91. 91.
    Miki H, Miura K, Matuoka K et al. Association of Ash/Grb-2 with dynamin through the Src homology 3 domain. J Biol Chem 1994; 269: 5489–92.PubMedGoogle Scholar
  92. 92.
    Schlaepfer DD, Hanks SK, Hunter T et al. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 1994; 372: 786–91.PubMedGoogle Scholar
  93. 93.
    Moran M, Polakis P, McCormick F et al. Protein-tyrosine kinases regulate the phosphorylation, protein interactions, subcellular distribution and activity of p21 ras GTPase-activating protein. Mol Cell Biol 1991; 11: 1804–12.PubMedGoogle Scholar
  94. 94.
    Serth J, Weber W, Frech M et al. Binding of the H-ras p21 GTPase activating protein by the activated epidermal growth factor receptor leads to inhibition of the p21 GTPase activity in vitro. Biochemistry 1992; 31: 6361–5.PubMedCrossRefGoogle Scholar
  95. 95.
    Settleman J, Albright CF, Foster LC et al. Association between GTPase activators for Rho and Ras families. Nature 1992; 359: 153–4.PubMedCrossRefGoogle Scholar
  96. 96.
    Ridley AJ, Self AJ, Kasmi F et al. Rho family GTPase activating proteins p190, bcr and rhoGAP show distinct specificities in vitro and in vivo. EMBO J 1993; 12: 5151–60.PubMedGoogle Scholar
  97. 97.
    McGlade J, Brunkhorst B, Anderson D et al. The N-terminal region of GAP regulates cytoskeletal structure and cell adhesion. EMBO J 1993; 12: 3073–81.PubMedGoogle Scholar
  98. 98.
    Lazarus AH, Kawauchi K, Rapoport MJ et al. Antigen-induced B lymphocyte activation involves the p2lras and ras GAP signaling pathway. J Exp Med 1993; 178: 1765–9.PubMedCrossRefGoogle Scholar
  99. 99.
    Gold MR, Crowley MT, Martin GA et al. Targets of B lymphocyte antigen receptor signal transduction include the p21 ras GAP and two GAP-associated proteins. J Immunol 1993; 150: 377–86.PubMedGoogle Scholar
  100. 100.
    Gold MR, Crowley MT, Martin GA et al. Targets of B lymphocyte antigen receptor signal transduction include the p2lras GTPase-activating protein (GAP) and two GAP-associated proteins. J Immunol 1993; 150: 377–86.PubMedGoogle Scholar
  101. 101.
    Rodriguez-Viciana P, Warne PH, Dhand R et al. Phosphatidylinositol-3-OH kinase as a direct target of Ras. Nature 1994; 370: 527–32.PubMedCrossRefGoogle Scholar
  102. 102.
    Stephens L, Jackson T, Hawkins PT. Synthesis of phosphatidylinositol 3,4,5trisphosphate in permeabilized neutrophils regulated by receptors and G proteins. J Biol Chem 1993; 268: 17162–72.PubMedGoogle Scholar
  103. 103.
    Gold MR, Chan VW, Turck CW et al. Membrane Ig crosslinking regulates phosphatidylinositol 3-kinase in B lymphocytes. J Immunol 1992; 148: 2012–22.PubMedGoogle Scholar
  104. 104.
    Cantrell DA, Izquierdo M, Reif K et al. Regulation of Ptdlns-3-kinase and the guanine nucleotide binding proteins p2lras during signal transduction by the T cell antigen receptor and the interleukin-2 receptor. Semin Immunol 1993; 5: 319–26.PubMedCrossRefGoogle Scholar
  105. 105.
    Yano H, Nakanishi S, Kimura K et al. Inhibition of histamine secretion by wortmannin through the blockade of phosphatidylinositol 3-kinase in RBL-2H3 cells. J Biol Chem 1993; 268: 25846–56.PubMedGoogle Scholar
  106. 106.
    Barker SA, Caldwell KK, Hall A et al. Wortmannin blocks lipid and protein kinase activities associated with PI 3-kinase and inhibits a subset of responses induced by FccR1 receptor crosslinking. Mol Biol Cell 1995; 6: 1145–58.PubMedGoogle Scholar
  107. 107.
    McGlade CJ, Ellis C, Reedijk M et al. SH2 domains of the p85 alpha subunit of phosphatidylinositol 3-kinase regulate binding to growth factor receptors. Mol Cell Biol 1992; 12: 991–7.PubMedGoogle Scholar
  108. 108.
    Van Horn DJ, Myers Jr MG, Backer JM. Direct activation of the phosphatidylinositol 3’-kinase by the insulin receptor. J Biol Chem 1994; 269: 29–32.PubMedGoogle Scholar
  109. 109.
    Reif K, Gout I, Waterfield MD et al. Divergent regulation of phosphatidylinositol 3-kinase P85 alpha and P85 beta isoforms upon T cell activation. J Biol Chem 1993; 268: 10780–8.PubMedGoogle Scholar
  110. 110.
    Weng WK, Jarvis L, LeBien TW. Signaling through CD19 activates Vav/mitogen-activated protein kinase pathway and induces formation of a CD19/Vav/phosphatidylinositol 3-kinase complex in human B cell precursors. J Biol Chem 1994; 269: 32514–21.PubMedGoogle Scholar
  111. 111.
    Zhang J, King WG, Dillons S et al. Activation of platelet phosphatidylinositide 3-kinase requires the small GTP-binding protein rho. J Biol Chem 1993; 268: 22251–4.PubMedGoogle Scholar
  112. 112.
    Zheng Y, Bagrodia S, Cerione RA. Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85. J Biol Chem 1994; 269: 18727–30.PubMedGoogle Scholar
  113. 113.
    Wennstrom S, Hawkins P, Cooke F et al. Activation of phosphoinositide 3-kinase is required for PDGF-stimulated membrane ruffling. Current Biol 1994; 4: 385–93.CrossRefGoogle Scholar
  114. 114.
    Kumagai N, Morii N, Fujisawa K et al. ADP-ribosylation of rho p21 inhibits lysophosphatidic acid-induced protein tyrosine phosphorylation and phosphatidylinositol 3-kinase activation in cultured Swiss 3T3 cells. J Biol Chem 1993; 268: 24535–8.PubMedGoogle Scholar
  115. 115.
    Hawkins PT, Eguinoa A, Qui R et al. PDGF stimulates an increase in GTP-Rac via the activation of phosphoinositide 3OH kinase. Current Biol 1995; 5: 393–400.CrossRefGoogle Scholar
  116. 116.
    Stephens L, Smrcka A, Cooke FT et al. A novel phosphoinositide 3 kinase activity in myeloid-deprived cells is activated by G protein gamma subunits. Cell 1994; 77: 83–93.PubMedCrossRefGoogle Scholar
  117. 117.
    Spaargaren M, Bischoff JR. Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap. Proc Natl Acad Sci USA 1994; 91: 12609–13.PubMedCrossRefGoogle Scholar
  118. 118.
    Hofer F, Fields S, Schneider C et al. Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator. Proc Natl Acad Sci USA 1994; 91: 11089–93.PubMedCrossRefGoogle Scholar
  119. 119.
    Russel M, Lange Carter CA, Johnson GL. Direct interaction between Ras and the kinase domain of Mitogen-Activated Protein Kinase Kinase Kinase (MEKK1). J Biol Chem 1995; 270: 11757–60.CrossRefGoogle Scholar
  120. 120.
    Nassar N, Horn G, Herrmann C et al. The 2.2 A crystal structure of the Ras-binding domain of the ser/threo kinase c-Rafl in complex with RaplA and a GTP analogue. Nature 1995; 375: 554–60.PubMedCrossRefGoogle Scholar
  121. 121.
    Higashijima T, Uzu S, Nakajima T et al. A peptide toxin from wasp venom mimics receptors by activating GTP-regulatory proteins (G proteins). J Biol Chem 1988; 263: 6491–4.PubMedGoogle Scholar
  122. 122.
    Mousli M, Bronner C, Landry Y et al. Direct activation of GTP-binding regulatory proteins (G proteins) by substance P and compound 48/80. FEBS Lett 1990; 259: 260–2.PubMedCrossRefGoogle Scholar
  123. 123.
    Swieter M, Midura RJ, Nishikata H et al. Mouse 3T3 fibroblasts induce rat basophilic leukemia (RBL-2H3) cells to acquire responsiveness to compound 48/80. J Immunol 1993; 150: 617–24.PubMedGoogle Scholar
  124. 124.
    Balch WE. Small GTP-binding proteins in vesicular transport. Trends in Biochem Sci 1990; 15: 473–7.CrossRefGoogle Scholar
  125. 125.
    Oberhauser AF, Balan V, Fernandez Badilla CL et al. RT-PCR cloning of Raba isoforms expressed in peritoneal mast cells. FEBS Lett 1994; 339: 171–4.PubMedCrossRefGoogle Scholar
  126. 126.
    Izushi K, Shirasaka T, Chokki M et al. Phosphorylation of smg p21B in rat peritoneal mast cells in association with histamine release inhibition by dibutyryl-cAMP. FEBS Lett 1992; 314: 241–5.PubMedCrossRefGoogle Scholar
  127. 127.
    Oberhauser AF, Monck JR, Balch WE et al. Exocytotic fusion is activated by Rab3a peptides. Nature 1992; 360: 270–3.PubMedCrossRefGoogle Scholar
  128. 128.
    MacLean CM, Law GJ, Edwardson JM. Stimulation of exocytotic membrane fusion by modified peptides of the rab3 effector domain: Re-evaluation of the role of rab3 in regulated exocytosis. Biochem J 1993; 294: 325–8.PubMedGoogle Scholar
  129. 129.
    Law GN, AJ, Mason WT. Mastoparan like effects of rab3al peptide. FEBS Lett 1994; 333: 56–60.CrossRefGoogle Scholar
  130. 130.
    Ludger J, Lledo P, Roa M et al. The GTPase rab3A negatively controls calcium-dependent exocytosis in neuroendocrine cells. EMBO J 1994; 13: 2029–37.Google Scholar
  131. 131.
    Holz RW, Brondyk WH, Senter RA et al. Evidence for the involvement of rab3A in Ca2’-dependent exocytosis from adrenal chromaffin cells. J Biol Chem 1994; 269: 10229–34.PubMedGoogle Scholar
  132. 132.
    Fujita Y, Sasaki T, Araki K et al. GDP/ GTP exchange reaction-stimulating activity of Rabphilin-3A for Rab3A small GTPbinding protein. FEBS Lett 1994; 353: 67–70.PubMedCrossRefGoogle Scholar
  133. 133.
    Yamaguchi T, Shirataki H, Kishida S et al. Two functionally different domains of rabphilin-3A, Rab3A p25/smg p25A-binding and phospholipid-and Ca(2’)-binding domains. J Biol Chem 1993; 268: 27164–70.PubMedGoogle Scholar
  134. 134.
    Kato M, Sasaki T, Imazumi K et al. Phosphorylation of Rabphilin-3A by calmodulindependent protein kinase II. Biochem Biophys Res Commun 1994; 205: 1776–84.PubMedCrossRefGoogle Scholar
  135. 135.
    Numata S, Shirataki H, Hagi S et al. Phosphorylation of Rabphilin-3A, a putative target protein for Rab3A, by cyclic AMP-dependent protein kinase. Biochem Biophys Res Commun 1994; 203: 1927–34.PubMedCrossRefGoogle Scholar
  136. 136.
    Fykse EM, Li C, Sudhof TC. Phosphorylation of rabphilin-3A by Cat’/calmodulinand cAMP-dependent protein kinases in vitro. J Neurosci 1995; 15: 2385–95.PubMedGoogle Scholar
  137. 137.
    Takai Y, Sasaki T, Tanaka K et al. Rho as a regulator of the cytoskeleton. TIBS 1995; 20: 227–231.PubMedGoogle Scholar
  138. 138.
    Ridley AJ, Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 1992; 70: 389–99.PubMedCrossRefGoogle Scholar
  139. 139.
    Ridley AJ, Paterson HF, Johnston CL et al. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 1992; 70: 401–10.PubMedCrossRefGoogle Scholar
  140. 140.
    Nobes CD, Hall A. Rho, Rac and Cdc42 regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia and filopodia. Cell 1995; 81: 53–62.PubMedCrossRefGoogle Scholar
  141. 141.
    Chong LD, Traynor KA, Bokoch GM et al. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 1994; 79: 507–13.PubMedCrossRefGoogle Scholar
  142. 142.
    Bowman EP, Uhlinger DJ, Lambeth JD. Neutrophil phospholipase D is activated by a membrane–associated rho family small molecular weight GTP–binding protein. J Biol Chem 1993; 268:21509–215–12.Google Scholar
  143. 143.
    Malcolm CK, Ross AH, Qiu RG et al. Activation of rat liver phospholipase D by the small GTP-binding protein RhoA. J Biol Chem 1994; 269 (42): 25951–4.PubMedGoogle Scholar
  144. 144.
    Lassing I, Lindberg U. Evidence that the phosphatidylinositol cycle is linked to cell motility. Exp Cell Res 1988; 174: 1–15.PubMedCrossRefGoogle Scholar
  145. 145.
    Peppelenbosch MP, Qiu RG, de Vries Smits AM et al. Rac mediates growth factor-induced arachidonic acid release. Cell 1995; 81: 849–56.PubMedCrossRefGoogle Scholar
  146. 146.
    Ridley AJ, Hall A. Signal transduction pathways regulating Rho-mediated stress fibre formation: requirement for a tyrosine kinase. EMBO J 1994; 13: 2600–10.PubMedGoogle Scholar
  147. 147.
    Morel F, Doussiere J, Vignais PV. The superoxide-generating oxidase of phagocytic cells. Physiological, molecular and pathological aspects. Eur J Biochem 1991; 201: 523–46.PubMedCrossRefGoogle Scholar
  148. 148.
    Seckl MJ, Morii N, Narumiya S et al. Guanosine 5’-3–0-(thio)triphosphate stimulates tyrosine phosphorylation of p125FAK and paxillin in permeabilized Swiss 3T3 cells. Role of p2lrho. J Biol Chem 1995; 270: 6984–90.PubMedCrossRefGoogle Scholar
  149. 149.
    Richardson A, Parsons JT. Signal transduction through integrins: a central role for focal adhesion kinase? Bio Essays 1995; 17 (3): 229–236.Google Scholar
  150. 150.
    Hamawy MM, Swaim WD, Minoguchi K et al. The aggregation of the high affinity IgE receptor induces tyrosine phosphorylation of paxillin, a focal adhesion protein. J Immunol 1994; 153: 4655–62.PubMedGoogle Scholar
  151. 151.
    Minoguchi K, Kihara H, Nishikata H et al. Src family tyrosine kinase Lyn binds several proteins including paxillin in rat basophilic leukemia cells. Mol Immunol 1994; 31: 519–29.PubMedCrossRefGoogle Scholar
  152. 152.
    Thomas SM, Soriano P, Imamoto A. Specific and redundant roles of Src and Fyn in organizing the cytoskeleton. Nature 1995; 376: 267–271.PubMedCrossRefGoogle Scholar
  153. 153.
    Rankin S, Morii N, Narumiya Set al. Botulinum C3 exoenzyme blocks the tyrosine phosphorylation of p125FAK and paxillin induced by bombesin and endothelin. FEBS Lett 1994; 354: 315–9.PubMedCrossRefGoogle Scholar
  154. 154.
    Turner CE, Miller JT. Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125F“K-binding region. J Cell Sci 1994; 107: 1583–91.PubMedGoogle Scholar
  155. 155.
    Abo A, Boyhan A, West I et al. Reconstitution of neutrophil NADPH oxidase activity in the cell free system by four components: p67-phox, p47-phox, p21-racl and cytochrome b245. J Biol Chem 1992; 267: 16767–70.PubMedGoogle Scholar
  156. 156.
    Rotrosen D, Yeung CL, Leto TL et al. Cytochrome b558: the flavin-binding component of the phagocyte NADPH oxidase. Science 1992; 256: 1459–62.PubMedCrossRefGoogle Scholar
  157. 157.
    Bokoch-GM. Regulation of the phagocyte respiratory burst by small GTP-binding proteins. Trends Cell Biol 1995; 5: 109–13.PubMedCrossRefGoogle Scholar
  158. 158.
    Heyworth PG, Bohl BP, Bokoch GM et al. Rac translocates independently of the neutrophil NADPH oxidase components p47phox and p67phox. Evidence for its interaction with flavocytochrome b558. J Biol Chem 1994; 269: 30749–52.PubMedGoogle Scholar
  159. 159.
    Diekmann D, Abo A, Johnston C et al. Interaction of Rac with p67phox and regulation of phagocytic NADPH oxidase activity. Science 1994; 265: 531–3.PubMedCrossRefGoogle Scholar
  160. 160.
    Manser E, Leung T, Salihuddin H et al. A brain serine/threonine protein kinase activated by cdc42 and racl. Nature 1994; 367: 40–6.PubMedCrossRefGoogle Scholar
  161. 161.
    Kishi K, Sasaki T, Kuroda S et al. Regulation of cytoplasmic division of Xenopus embryo by rhop2l and its inhibitory GDP/ GTP exchange protein (rho GDI). J Cell Biol 1993; 120: 1187–95.PubMedCrossRefGoogle Scholar
  162. 162.
    Hirata K, Kikuchi A, Sasaki T et al. Involvement of rho p21 in the GTP enhancement of calcium sensitivity in smooth muscle contraction. J Biol Chem 1992; 267: 8719–22.PubMedGoogle Scholar
  163. 163.
    Jalink K, van Corven EJ, Hengeveld T et al. Inhibition of lysophosphatidate-and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho. J Cell Biol 1994; 126: 801–10.PubMedCrossRefGoogle Scholar
  164. 164.
    Vojtek AB, Cooper JA. Rho family members: Activators of MAP kinase cascades. Cell 1995; 82: 527–9.PubMedCrossRefGoogle Scholar
  165. 165.
    Price LS. Ph.D. Thesis 1995, University College London.Google Scholar
  166. 166.
    Koffer A, Tatham PER, Gomperts BD. Changes in the state of actin during the exocytotic reaction of permeabilized rat mast cells. J Cell Biol 1990; 111: 919–27.PubMedCrossRefGoogle Scholar
  167. 167.
    Janmey PA, Iida K, Yin HL et al. Polyphosphoinositide micelles and polyphosphoinositide-containing vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin. J Biol Chem 1987; 262: 12228–36.PubMedGoogle Scholar
  168. 168.
    Pfeiffer JR, Seagrave JC, Davis BH et al. Membrane and cytoskeletal changes associated with IgE-mediated serotonin release from rat basophilic leukemia cells. J Cell Biol 1985; 101: 2145–55.PubMedCrossRefGoogle Scholar
  169. 169.
    Apgar J. Regulation of the antigen-induced F-actin response in rat basophilic leukemia cells by protein kinase C. J Cell Biol 1991; 112: 1157–63.PubMedCrossRefGoogle Scholar
  170. 170.
    Apgar JR. Polymerization of actin in RBL-2H3 cells can be triggered through either the IgE receptor or the adenosine receptor but different signaling pathways are used. Mol Biol Cell 1994; 5: 313–22.PubMedGoogle Scholar
  171. 171.
    Apgar JR. Association of the crosslinked IgE receptor with the membrane skeleton is independent of the known signaling mechanisms in rat basophilic leukemia cells. Cell Regul 1991; 2: 181–91.PubMedGoogle Scholar
  172. 172.
    Pfeiffer JR, Oliver JM. Tyrosine kinase-dependent assembly of actin plaques linking FceR 1 -crosslinking to increased cell substrate adhesion in RBL-2H3 tumor mast cells. J Immunol 1994; 152 (1): 270–9.PubMedGoogle Scholar
  173. 173.
    Oliver JM, Burg DL, Wilson BS et al. Inhibition of mast cell Fc epsilon R1-mediated signaling and effector function by the Syk-selective inhibitor, piceatannol. J Biol Chem 1994; 269: 29697–703.PubMedGoogle Scholar

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© Springer-Verlag Berlin Heidelberg 1997

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  • Anna Koffer

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