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Volumn 50, Issue 4, 1996, Pages 864-869

Inhibition by toxin B of inositol phosphate formation induced by G protein-coupled and tyrosine kinase receptors in N1E-115 neuroblastoma cells: Involvement of Rho proteins

Author keywords

[No Author keywords available]

Indexed keywords

BRADYKININ; CALCIUM; CELL RECEPTOR; CLOSTRIDIUM TOXIN; CYTOCHALASIN B; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); INOSITOL PHOSPHATE; LYSOPHOSPHATIDIC ACID; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL 4 PHOSPHATE; PHOSPHATIDYLINOSITOL 4 PHOSPHATE KINASE; PHOSPHOLIPASE C; PLATELET DERIVED GROWTH FACTOR; PLATELET DERIVED GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE KINASE; RHO FACTOR;

EID: 0029912023     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (21)

References (30)
  • 1
    • 0028986998 scopus 로고
    • 2 hydrolysis and regulation of phospholipase C isozymes
    • 2 hydrolysis and regulation of phospholipase C isozymes. Curr. Opin. Cell Biol. 7:183-189 (1995).
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 183-189
    • Lee, S.B.1    Rhee, S.G.2
  • 2
    • 0026659202 scopus 로고
    • Inositol phosphate biochemistry
    • Majerus, P. W. Inositol phosphate biochemistry. Annu. Rev. Biochem. 61: 225-250 (1992).
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 225-250
    • Majerus, P.W.1
  • 5
    • 0024554227 scopus 로고
    • Regulation of brain phosphatidylinositol-4-phosphate kinase by GTP analogues: A potential role for guanine nucleotide regulatory proteins
    • Smith, C. D., and K.-J. Chang. Regulation of brain phosphatidylinositol-4-phosphate kinase by GTP analogues: a potential role for guanine nucleotide regulatory proteins. J. Biol. Chem. 264:3206-3210 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 3206-3210
    • Smith, C.D.1    Chang, K.-J.2
  • 6
    • 0025240993 scopus 로고
    • A small G-protein involved in phosphatidylinositol-4-phosphate kinase activation
    • Urumow, T., and O. H. Wieland. A small G-protein involved in phosphatidylinositol-4-phosphate kinase activation. FEBS Lett. 263:15-17 (1990).
    • (1990) FEBS Lett. , vol.263 , pp. 15-17
    • Urumow, T.1    Wieland, O.H.2
  • 7
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong, L. D., A. Traynor-Kaplan, G. M. Bokoch, and M. A. Schwartz. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 79:507-513 (1994).
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 8
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig, J. H., G. M. Bokoch, C. L. Carpenter, P. A. Janmey, L. A. Taylor, A. Toker, and T. P. Stossel. Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 82:643-653 (1995).
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 9
    • 0027400947 scopus 로고
    • A chimeric toxin to study the role of the 21 kDa GTP binding protein rho in the control of actin microfilament assembly
    • Aullo, P., M. Giry, S. Olsnes, M. R. Popoff, C. Kocks, and P. Boquet. A chimeric toxin to study the role of the 21 kDa GTP binding protein rho in the control of actin microfilament assembly. EMBO J. 12:921-931 (1993).
    • (1993) EMBO J. , vol.12 , pp. 921-931
    • Aullo, P.1    Giry, M.2    Olsnes, S.3    Popoff, M.R.4    Kocks, C.5    Boquet, P.6
  • 10
    • 0024449589 scopus 로고
    • The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells
    • Chardin, P., P. Boquet, P. Madaule, M. R. Popoff, E. J. Rubin, and D. M. Gill. The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells. EMBO J. 8:1087-1092 (1989).
    • (1989) EMBO J. , vol.8 , pp. 1087-1092
    • Chardin, P.1    Boquet, P.2    Madaule, P.3    Popoff, M.R.4    Rubin, E.J.5    Gill, D.M.6
  • 12
    • 0027374497 scopus 로고
    • Activation of platelet phosphatidylinositide 3-kinase requires the small GTP-binding protein Rho
    • Zhang, J., W. G. King, S. Dillon, A. Hall, L. Feig, and S. E. Rittenhouse. Activation of platelet phosphatidylinositide 3-kinase requires the small GTP-binding protein Rho. J. Biol. Chem. 268:22251-22254 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 22251-22254
    • Zhang, J.1    King, W.G.2    Dillon, S.3    Hall, A.4    Feig, L.5    Rittenhouse, S.E.6
  • 13
    • 0030063978 scopus 로고    scopus 로고
    • Inhibition of receptor signaling to phospholipase D by Clostridium difficile toxin B. Role of Rho proteins
    • Schmidt, M., U. Rümenapp, C. Bienek, J. Keller, C. von Eichel-Streiber, and K. H. Jakobs. Inhibition of receptor signaling to phospholipase D by Clostridium difficile toxin B. Role of Rho proteins. J. Biol. Chem. 271: 2422-2426 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 2422-2426
    • Schmidt, M.1    Rümenapp, U.2    Bienek, C.3    Keller, J.4    Von Eichel-Streiber, C.5    Jakobs, K.H.6
  • 16
    • 0023656574 scopus 로고
    • ADP-ribosylation of a 21-24 kDa eukaryotic protein(s) by C3, a novel botulinum ADP-ribosyltransferase, is regulated by guanine nucleotide
    • Aktories, K., and J. Frevert. ADP-ribosylation of a 21-24 kDa eukaryotic protein(s) by C3, a novel botulinum ADP-ribosyltransferase, is regulated by guanine nucleotide. Biochem. J. 247:363-368 (1987).
    • (1987) Biochem. J. , vol.247 , pp. 363-368
    • Aktories, K.1    Frevert, J.2
  • 17
    • 0023175490 scopus 로고
    • Purification of two high molecular weight toxins of Clostridium difficile which are antigenically related
    • von Eichel-Streiber, C., U. Harperath, U. Bosse, and U. Hadding. Purification of two high molecular weight toxins of Clostridium difficile which are antigenically related. Microb. Pathog. 2:307-318 (1987).
    • (1987) Microb. Pathog. , vol.2 , pp. 307-318
    • Von Eichel-Streiber, C.1    Harperath, U.2    Bosse, U.3    Hadding, U.4
  • 18
    • 0028073780 scopus 로고
    • Mechanisms of phospholipase D stimulation by m3 muscarinic acetylcholine receptors: Evidence for involvement of tyrosine phosphorylation
    • Schmidt, M., S. M. Hüwe, B. Fasselt, D. Homann, U. Rümenapp, J. Sandmann, and K. H. Jakobs. Mechanisms of phospholipase D stimulation by m3 muscarinic acetylcholine receptors: evidence for involvement of tyrosine phosphorylation. Eur. J. Biochem. 225:667-675 (1994).
    • (1994) Eur. J. Biochem. , vol.225 , pp. 667-675
    • Schmidt, M.1    Hüwe, S.M.2    Fasselt, B.3    Homann, D.4    Rümenapp, U.5    Sandmann, J.6    Jakobs, K.H.7
  • 19
    • 0029121436 scopus 로고
    • Rapid and persistent desensitjzation of m3 muscarinic acetylcholine receptor-stimulated phospholipase D: Concomitant sensitization of phospholipase C
    • Schmidt, M., B. Fasselt, U. Rümenapp, C. Bienek, T. Wieland, C. J. van Koppen, and K. H. Jakobs. Rapid and persistent desensitjzation of m3 muscarinic acetylcholine receptor-stimulated phospholipase D: concomitant sensitization of phospholipase C. J. Biol. Chem. 270:19949-19956 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 19949-19956
    • Schmidt, M.1    Fasselt, B.2    Rümenapp, U.3    Bienek, C.4    Wieland, T.5    Van Koppen, C.J.6    Jakobs, K.H.7
  • 20
    • 0025103818 scopus 로고
    • Guanosine 5′-[γ-thio]triphosphate-stimulated hydrolysis of phosphatidylinositol 4,5-bisphosphate in HL-60 granulocytes: Evidence that the guanine nucleotide acts by relieving phospholipase C from an inhibitory constraint
    • Camps, M., C. Hou, K. H. Jakobs, and P. Gierschik. Guanosine 5′-[γ-thio]triphosphate-stimulated hydrolysis of phosphatidylinositol 4,5-bisphosphate in HL-60 granulocytes: evidence that the guanine nucleotide acts by relieving phospholipase C from an inhibitory constraint. Biochem. J. 271:743-748 (1990).
    • (1990) Biochem. J. , vol.271 , pp. 743-748
    • Camps, M.1    Hou, C.2    Jakobs, K.H.3    Gierschik, P.4
  • 21
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias, K. F., L. C. Cantley, and C. L. Carpenter. Rho family GTPases bind to phosphoinositide kinases. J. Biol. Chem. 270:17656-17659 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.C.2    Carpenter, C.L.3
  • 22
    • 0028274104 scopus 로고
    • Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly
    • Janmey, P. A. Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu. Rev. Physiol. 56:169-191 (1994).
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 169-191
    • Janmey, P.A.1
  • 24
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J., and A. Hall. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389-399 (1992).
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 25
    • 0029089504 scopus 로고
    • A small GTP-binding protein, Rho, associates with the platelet-derived growth factor type-β receptor upon ligand binding
    • Zubiaur, M., J. Sancho, C. Terhorst, and D. V. Faller. A small GTP-binding protein, Rho, associates with the platelet-derived growth factor type-β receptor upon ligand binding. J. Biol. Chem. 270:17221-17228 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 17221-17228
    • Zubiaur, M.1    Sancho, J.2    Terhorst, C.3    Faller, D.V.4
  • 26
    • 0028589148 scopus 로고
    • Platelet-derived growth factor receptor signals
    • Claesson-Welsh, L. Platelet-derived growth factor receptor signals. J. Biol. Chem. 269:32023-32026 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 32023-32026
    • Claesson-Welsh, L.1
  • 27
    • 0025784055 scopus 로고
    • Dissociation of platelet-derived growth factor (PDGF) receptor autophosphorylation from other PDGF-mediated second messenger events
    • Quinones, M. A., L. J. Mundschau, J. Rakes, and D. V. Faller. Dissociation of platelet-derived growth factor (PDGF) receptor autophosphorylation from other PDGF-mediated second messenger events. J. Biol. Chem. 266: 14055-14063 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 14055-14063
    • Quinones, M.A.1    Mundschau, L.J.2    Rakes, J.3    Faller, D.V.4
  • 28
    • 0027211693 scopus 로고
    • Phospholipase C-γ1 and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal
    • Valius, M., and A. Kazlauskas. Phospholipase C-γ1 and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal. Cell 73:321-334 (1993).
    • (1993) Cell , vol.73 , pp. 321-334
    • Valius, M.1    Kazlauskas, A.2
  • 29
    • 0028021882 scopus 로고
    • Plekstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan, J. E., P. J. Hajduk, H. S. Yoon, and S. W. Fesik. Plekstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature (Lond.) 371:168-170 (1994).
    • (1994) Nature (Lond.) , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 30
    • 0027965240 scopus 로고
    • Novel function of phosphatidylinositol 4,5-bisphosphate as a cofactor for brain membrane phospholipase D
    • Liscovitch, M., V. Chalifa, P. Pertile, C.-S. Chen, and L. C. Cantley. Novel function of phosphatidylinositol 4,5-bisphosphate as a cofactor for brain membrane phospholipase D. J. Biol. Chem. 269:21403-21406 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 21403-21406
    • Liscovitch, M.1    Chalifa, V.2    Pertile, P.3    Chen, C.-S.4    Cantley, L.C.5


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