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Volumn 243, Issue 1-2, 1997, Pages 10-20

Cell signalling through guanine-nucleotide-binding regulatory proteins (G proteins) and phospholipases

Author keywords

Guanine nucleotide binding regulatory protein; Inositol phospholipids; Phosphatidylcholine; Protein kinase C

Indexed keywords

DIACYLGLYCEROL; GUANINE NUCLEOTIDE BINDING PROTEIN; INOSITOL TRISPHOSPHATE; ISOENZYME; PHOSPHATIDIC ACID; PHOSPHATIDYLCHOLINE; PHOSPHOLIPASE; PHOSPHOLIPASE C; PHOSPHOLIPASE D; PROTEIN TYROSINE KINASE;

EID: 0031026288     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00010.x     Document Type: Review
Times cited : (148)

References (112)
  • 1
    • 0021443856 scopus 로고
    • Inositol trisphosphate and diacylglycerol as second messengers
    • Berridge, M. J. (1984) Inositol trisphosphate and diacylglycerol as second messengers, Biochem. J. 220, 345-360.
    • (1984) Biochem. J. , vol.220 , pp. 345-360
    • Berridge, M.J.1
  • 2
    • 0029936331 scopus 로고    scopus 로고
    • Regulation of phosphoinositide phospholipase by hormones, neurotransmitters and other agonists linked to G-proteins
    • Exton, J. H. (1996) Regulation of phosphoinositide phospholipase by hormones, neurotransmitters and other agonists linked to G-proteins, Annu. Rev. Pharmacol. Toxicol. 36, 481-509.
    • (1996) Annu. Rev. Pharmacol. Toxicol. , vol.36 , pp. 481-509
    • Exton, J.H.1
  • 3
    • 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) Curr. Opin. Cell Biol. , vol.7 , pp. 183-189
    • Lee, S.B.1    Rhee, S.G.2
  • 4
    • 0028296793 scopus 로고
    • Phosphatidylcholine breakdown and signal transduction
    • Exton, J. H. (1994) Phosphatidylcholine breakdown and signal transduction, Biochim. Biophys. Acta 1212, 26-42.
    • (1994) Biochim. Biophys. Acta , vol.1212 , pp. 26-42
    • Exton, J.H.1
  • 6
    • 0026654469 scopus 로고
    • Regulation of inositol phospholipid-specific phospholipase C isozymes
    • Rhee, S. G. & Choi, K. D. (1992) Regulation of inositol phospholipid-specific phospholipase C isozymes, J. Biol. Chem. 267, 12393-12396.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12393-12396
    • Rhee, S.G.1    Choi, K.D.2
  • 8
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ
    • Essen, L.-O., Perisic, O., Cheung, R., Katan, M. & Williams, R. L. (1996) Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ, Nature 380, 595-602.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.-O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 12
    • 0026468420 scopus 로고
    • Inositol-lipid-specific phospholipase C isoenzymes and their differential regulation by receptors
    • Cockcroft, S. & Thomas, G. M. H. (1992) Inositol-lipid-specific phospholipase C isoenzymes and their differential regulation by receptors, Biochem. J. 288, 1-14.
    • (1992) Biochem. J. , vol.288 , pp. 1-14
    • Cockcroft, S.1    Thomas, G.M.H.2
  • 15
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a Gα protein βγ dimer at 2.1 Å resolution
    • Sondek, J., Bohm, A., Lambright, D. G., Hamm, H. E. & Sigler, P. B. (1996) Crystal structure of a Gα protein βγ dimer at 2.1 Å resolution, Nature 379, 369-374.
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1    Bohm, A.2    Lambright, D.G.3    Hamm, H.E.4    Sigler, P.B.5
  • 16
    • 0027132717 scopus 로고
    • The 2.2 Å crystal structure of transducin-α complexed with GTPγS
    • Noel, J. P., Hamm, H. E. & Sigler, P. B. (1993) The 2.2 Å crystal structure of transducin-α complexed with GTPγS, Nature 366, 654-663.
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 19
    • 0026548156 scopus 로고
    • In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors
    • Savarese, T. M. & Fraser, C. M. (1992) In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors, Biochem. J. 283, 1-19.
    • (1992) Biochem. J. , vol.283 , pp. 1-19
    • Savarese, T.M.1    Fraser, C.M.2
  • 20
    • 0027496941 scopus 로고
    • Mutational analysis of muscarinic acetylcholine receptors: Structural basis of ligand/receptor/G protein interactions
    • Wess, J. (1993) Mutational analysis of muscarinic acetylcholine receptors: structural basis of ligand/receptor/G protein interactions, Life Sci. 53, 1447-1463.
    • (1993) Life Sci. , vol.53 , pp. 1447-1463
    • Wess, J.1
  • 22
    • 0028237708 scopus 로고
    • Structural determinants for activation of the α-subunit of a heterotrimeric G protein
    • Lambright, D. G., Noel, J. P., Hamm, H. E. & Sigler, P. B. (1994) Structural determinants for activation of the α-subunit of a heterotrimeric G protein, Nature 369, 621-628.
    • (1994) Nature , vol.369 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 23
    • 0029145416 scopus 로고
    • Structural and functional relationships of heterotrimeric G-proteins
    • Rens-Domiano, S. & Hamm, H. E. (1995) Structural and functional relationships of heterotrimeric G-proteins, FASEB J. 9, 1059-1066.
    • (1995) FASEB J. , vol.9 , pp. 1059-1066
    • Rens-Domiano, S.1    Hamm, H.E.2
  • 24
    • 0025695580 scopus 로고
    • G protein diversity: A distinct class of a subunits is present in vertebrates and invertebrates
    • Strathmann, M. & Simon, M. I. (1990) G protein diversity: a distinct class of a subunits is present in vertebrates and invertebrates. Proc. Natl Acad. Sci. USA 87, 9113-9117.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 9113-9117
    • Strathmann, M.1    Simon, M.I.2
  • 25
    • 0025834532 scopus 로고
    • Diversity of G proteins in signal transduction
    • Simon, M. I., Strathmann, M. P. & Gautam, N. (1991) Diversity of G proteins in signal transduction, Science 252, 802-808.
    • (1991) Science , vol.252 , pp. 802-808
    • Simon, M.I.1    Strathmann, M.P.2    Gautam, N.3
  • 30
    • 0027537482 scopus 로고
    • Removal of the carboxyl-terminal region of phospholipase C-β1 by calpain abolishes activation by Gαq
    • Park, D., Jhon, D.-Y., Lee, C.-W., Ryu, S.-H. & Rhee, S. G. (1993) Removal of the carboxyl-terminal region of phospholipase C-β1 by calpain abolishes activation by Gαq, J. Biol. Chem. 268, 3710-3714.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3710-3714
    • Park, D.1    Jhon, D.-Y.2    Lee, C.-W.3    Ryu, S.-H.4    Rhee, S.G.5
  • 33
  • 35
    • 0028283331 scopus 로고
    • Activation of phospholipase C β4 by helerotrimeric GTP-binding proteins
    • Jiang, H., Wu, D. & Simon, M. I. (1994) Activation of phospholipase C β4 by helerotrimeric GTP-binding proteins, J. Biol. Chem. 269, 7593-7596.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7593-7596
    • Jiang, H.1    Wu, D.2    Simon, M.I.3
  • 38
    • 0027495684 scopus 로고
    • New roles for G-protein βγ-dimers in transmembrane signalling
    • Clapham, D. E. & Neer, E. J. (1993) New roles for G-protein βγ-dimers in transmembrane signalling, Nature 365, 403-406.
    • (1993) Nature , vol.365 , pp. 403-406
    • Clapham, D.E.1    Neer, E.J.2
  • 39
    • 0028177677 scopus 로고
    • The active role of βγ in signal transduction
    • Sternweis, P. C. (1994) The active role of βγ in signal transduction, Curr. Opin. Cell Biol. 6, 198-203.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 198-203
    • Sternweis, P.C.1
  • 40
    • 0021748090 scopus 로고
    • Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain
    • Sternweis, P. C. & Robishaw, J. D. (1984) Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain, J. Biol. Chem. 259, 13806-13813.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13806-13813
    • Sternweis, P.C.1    Robishaw, J.D.2
  • 43
    • 0027936892 scopus 로고
    • Membrane organization in G-protein mechanisms
    • Neubig, R. R. (1994) Membrane organization in G-protein mechanisms, FASEB J. 8, 939-946.
    • (1994) FASEB J. , vol.8 , pp. 939-946
    • Neubig, R.R.1
  • 44
    • 0025759035 scopus 로고
    • Multiple forms of phosphoinositide-specific phospholipase C and different modes of activation
    • Rhee, S. G., Kim, H., Suy, P.-G. & Choi, W. C. (1991) Multiple forms of phosphoinositide-specific phospholipase C and different modes of activation, Biochem. Soc. Trans. 19, 337-341.
    • (1991) Biochem. Soc. Trans. , vol.19 , pp. 337-341
    • Rhee, S.G.1    Kim, H.2    Suy, P.-G.3    Choi, W.C.4
  • 47
    • 0027508316 scopus 로고
    • Purification, molecular cloning, and sequencing of phospholipase C-β4
    • Lee, C.-W., Park, D. J., Lee, K.-H., Kim, C. G. & Rhee, S. G. (1993) Purification, molecular cloning, and sequencing of phospholipase C-β4, J. Biol. Chem. 268, 21318-21327.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21318-21327
    • Lee, C.-W.1    Park, D.J.2    Lee, K.-H.3    Kim, C.G.4    Rhee, S.G.5
  • 48
    • 0024471697 scopus 로고
    • Indirect immunoflourescence localization of β-adrenergic receptors and G-proteins in human A431 cells
    • Wang, H. Y., Berrios, M. & Malbon, C. C. (1989) Indirect immunoflourescence localization of β-adrenergic receptors and G-proteins in human A431 cells. Biochem. J. 263, 519-532.
    • (1989) Biochem. J. , vol.263 , pp. 519-532
    • Wang, H.Y.1    Berrios, M.2    Malbon, C.C.3
  • 50
    • 0029670035 scopus 로고    scopus 로고
    • 2-adrenergic receptor subtypes achieve basolateral localization in Madin-Darby canine kidney II cells via different targeting mechanisms
    • 2-adrenergic receptor subtypes achieve basolateral localization in Madin-Darby canine kidney II cells via different targeting mechanisms, J. Biol. Chem. 271, 5017-5024.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5017-5024
    • Wozniak, M.1    Limbird, L.E.2
  • 51
    • 0029929903 scopus 로고    scopus 로고
    • Differential distribution of α subunits and βγ subunits of heterotrimeric G proteins on Golgi membranes of the exocrine pancreas
    • Denker, S. P., McCaffery, J. M., Palade, G. E., Insel, P. A. & Farquhar, M. G. (1996) Differential distribution of α subunits and βγ subunits of heterotrimeric G proteins on Golgi membranes of the exocrine pancreas, J. Cell Biol. 133, 1027-1040.
    • (1996) J. Cell Biol. , vol.133 , pp. 1027-1040
    • Denker, S.P.1    McCaffery, J.M.2    Palade, G.E.3    Insel, P.A.4    Farquhar, M.G.5
  • 52
    • 0025880464 scopus 로고
    • Assignment of G-protein subtypes to specific receptors inducing inhibition of calcium currents
    • Kleuss, C., Hescheler, J., Ewel, J., Rosenthal, W., Schultz, G. & Wittig, B. (1991) Assignment of G-protein subtypes to specific receptors inducing inhibition of calcium currents, Nature 353, 43-48.
    • (1991) Nature , vol.353 , pp. 43-48
    • Kleuss, C.1    Hescheler, J.2    Ewel, J.3    Rosenthal, W.4    Schultz, G.5    Wittig, B.6
  • 53
    • 0026752495 scopus 로고
    • Different β-subunits determine G-protein interaction with transmembrane receptors
    • Kleuss, C., Scherubl, H., Hescheler, J., Schultz, G. & Wittig, B. (1992) Different β-subunits determine G-protein interaction with transmembrane receptors. Nature 358, 424-426.
    • (1992) Nature , vol.358 , pp. 424-426
    • Kleuss, C.1    Scherubl, H.2    Hescheler, J.3    Schultz, G.4    Wittig, B.5
  • 54
    • 0027530916 scopus 로고
    • Selectivity of signal transduction determined by 7 subunits of heterotrimeric G proteins
    • Kleuss, C., Scherubl, H., Hescheler, J., Schultz, G. & Wittig, B. (1993) Selectivity of signal transduction determined by 7 subunits of heterotrimeric G proteins, Science 259, 832-834.
    • (1993) Science , vol.259 , pp. 832-834
    • Kleuss, C.1    Scherubl, H.2    Hescheler, J.3    Schultz, G.4    Wittig, B.5
  • 56
    • 0029966537 scopus 로고    scopus 로고
    • A heterotrimeric G protein complex couples the muscarinic m1 receptor to phospholpase C-β
    • Dippel, E., Kalkbrenner, F., Wittig, B. & Schultz, G. (1996) A heterotrimeric G protein complex couples the muscarinic m1 receptor to phospholpase C-β, Proc. Natl Acad. Sci. USA 93, 1391-1396.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1391-1396
    • Dippel, E.1    Kalkbrenner, F.2    Wittig, B.3    Schultz, G.4
  • 57
    • 8044239591 scopus 로고    scopus 로고
    • Phospholipase D
    • in the press
    • Exton, J. H. (1997) Phospholipase D, Physiol. Rev., in the press.
    • (1997) Physiol. Rev.
    • Exton, J.H.1
  • 58
    • 0029564902 scopus 로고
    • Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family
    • Hammond, S. M., Altshuller, Y. M., Sung, T.-C., Rudge, S. A., Rose, K., Engebrecht, J. A., Morris, A. J. & Frohman, M. A. (1995) Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family, J. Biol. Chem. 270, 29640-29643.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29640-29643
    • Hammond, S.M.1    Altshuller, Y.M.2    Sung, T.-C.3    Rudge, S.A.4    Rose, K.5    Engebrecht, J.A.6    Morris, A.J.7    Frohman, M.A.8
  • 59
    • 0029805684 scopus 로고    scopus 로고
    • Tissue specific distribution and subcellular distribution of phospholipase D in rat. Evidence for distinct RhoA- and ARF-regulated isozymes
    • in the press
    • Provost, J. J., Fudge. J., Israelit, S., Siddiqi, A. R. & Exton, J. H. (1996) Tissue specific distribution and subcellular distribution of phospholipase D in rat. Evidence for distinct RhoA- and ARF-regulated isozymes, Biochem. J., in the press.
    • (1996) Biochem. J.
    • Provost, J.J.1    Fudge, J.2    Israelit, S.3    Siddiqi, A.R.4    Exton, J.H.5
  • 60
    • 0029072489 scopus 로고
    • A phospholipase D-mediated pathway for generating diacylglycerol in nuclei from Madin-Darby canine kidney cells
    • Balboa, M. A., Balsinde, J., Dennis, H. A. & Insel, P. A. (1995) A phospholipase D-mediated pathway for generating diacylglycerol in nuclei from Madin-Darby canine kidney cells, J. Biol. Chem. 270, 11738-11749.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11738-11749
    • Balboa, M.A.1    Balsinde, J.2    Dennis, H.A.3    Insel, P.A.4
  • 61
    • 0030903197 scopus 로고    scopus 로고
    • Arf and RhoA regulate both the cytosolic and the membrane-bound phospholpase D from human placenta
    • in the press
    • Vinggaard, A. M., Provost, J. J., Exton, J. H. & Hansen, H. S. (1997) Arf and RhoA regulate both the cytosolic and the membrane-bound phospholpase D from human placenta, Cell. Signalling, in the press.
    • (1997) Cell. Signalling
    • Vinggaard, A.M.1    Provost, J.J.2    Exton, J.H.3    Hansen, H.S.4
  • 62
    • 0029065704 scopus 로고
    • Phospholipase D is present on Golgi-enriched membranes and its activation by ADP-ribosylation factor is sensitive to brefeldin A
    • Ktistakis, N. T., Brown, H. A., Sternweis, P. C. & Roth, M. G. (1995) Phospholipase D is present on Golgi-enriched membranes and its activation by ADP-ribosylation factor is sensitive to brefeldin A, Proc. Natl Acad. Sci. USA 92, 4952-4956.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 4952-4956
    • Ktistakis, N.T.1    Brown, H.A.2    Sternweis, P.C.3    Roth, M.G.4
  • 63
    • 0018734854 scopus 로고
    • Partial purification and properties of a rat brain phospholipase D
    • Taki, T. & Kanter, J. N. (1979) Partial purification and properties of a rat brain phospholipase D, J. Biol Chem. 254, 9761-9765.
    • (1979) J. Biol Chem. , vol.254 , pp. 9761-9765
    • Taki, T.1    Kanter, J.N.2
  • 64
    • 0027943755 scopus 로고
    • Purification and characterization of phosphatidylcholine phospholipase D from pig lung
    • Okamura, S.-L. & Yamashita, S. (1994) Purification and characterization of phosphatidylcholine phospholipase D from pig lung, J. Biol. Chem. 269, 31207-31213.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31207-31213
    • Okamura, S.-L.1    Yamashita, S.2
  • 65
    • 0027999909 scopus 로고
    • Activation of rat liver phospholipase D by the small GTP binding protein rhoA
    • Malcolm, K. C., Ross, A. H., Qiu, R.-G., Symons, M. & Exton, J. H. (1994) Activation of rat liver phospholipase D by the small GTP binding protein rhoA, J. Biol. Chem. 269, 25951-25954.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25951-25954
    • Malcolm, K.C.1    Ross, A.H.2    Qiu, R.-G.3    Symons, M.4    Exton, J.H.5
  • 66
    • 0028927083 scopus 로고
    • Regulation of phospholipase D in HL60 cells. Evidence for a cytosolic phospholipase D
    • Siddiqi, A. R., Smith, J. L., Ross, A. H., Qiu, R.-G., Symons, M. & Exton, J. H. (1995) Regulation of phospholipase D in HL60 cells. Evidence for a cytosolic phospholipase D, J. Biol. Chem. 270, 8466-8473.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8466-8473
    • Siddiqi, A.R.1    Smith, J.L.2    Ross, A.H.3    Qiu, R.-G.4    Symons, M.5    Exton, J.H.6
  • 67
    • 0029075145 scopus 로고
    • Partial purification and characterization of Arf-sensitive phospholipase D from porcine brain
    • Brown, H. A., Gutowski, S., Kahn, R. A. & Sternweis, P. C. (1995) Partial purification and characterization of Arf-sensitive phospholipase D from porcine brain, J. Biol. Chem. 270, 14935-14943.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14935-14943
    • Brown, H.A.1    Gutowski, S.2    Kahn, R.A.3    Sternweis, P.C.4
  • 68
    • 0027986677 scopus 로고
    • Activation of rat brain phospholipase D by ADP-ribosylation factors 1, 5, and 6; separation of ADP-ribosylation factor-dependent and oleate-dependent enzymes
    • Massenburg, D., Han, J.-S., Liyanage, M., Patton, W. A., Rhee, S. G., Moss, J. & Vaughan, M. (1994) Activation of rat brain phospholipase D by ADP-ribosylation factors 1, 5, and 6; separation of ADP-ribosylation factor-dependent and oleate-dependent enzymes, Proc. Natl Acad. Sci. USA 91, 11718-11722.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11718-11722
    • Massenburg, D.1    Han, J.-S.2    Liyanage, M.3    Patton, W.A.4    Rhee, S.G.5    Moss, J.6    Vaughan, M.7
  • 70
    • 0030004457 scopus 로고    scopus 로고
    • Acidic phospholipids inhibit the phospholipase D activity of rat brain neuronal nuclei
    • Kanter, J. N., McCartney, D. G., Singh, I. N. & Freysz, L. (1996) Acidic phospholipids inhibit the phospholipase D activity of rat brain neuronal nuclei, FEBS Lett. 383, 6-8.
    • (1996) FEBS Lett. , vol.383 , pp. 6-8
    • Kanter, J.N.1    McCartney, D.G.2    Singh, I.N.3    Freysz, L.4
  • 71
    • 0025162155 scopus 로고
    • Signaling through phosphatidylcholine breakdown
    • Exton, J. H. (1990) Signaling through phosphatidylcholine breakdown, J. Biol. Chem. 265, 1-4.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1-4
    • Exton, J.H.1
  • 72
    • 0027217553 scopus 로고
    • Upregulation of phospholipase D activity induced by overexpression of protein kinase C-α. Studies in intact Swiss/ 3T3 cells and in detergent-solubilized membranes in vitro
    • Eldar, H., Ben-Av, P., Schmidt, U.-S., Livneh, E. & Liscovitch, M. (1993) Upregulation of phospholipase D activity induced by overexpression of protein kinase C-α. Studies in intact Swiss/ 3T3 cells and in detergent-solubilized membranes in vitro. J. Biol. Chem. 268, 12560-12564.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12560-12564
    • Eldar, H.1    Ben-Av, P.2    Schmidt, U.-S.3    Livneh, E.4    Liscovitch, M.5
  • 73
    • 0026754819 scopus 로고
    • Differential regulation of phosphoinositide and phosphatildylcholine hydrolysis by protein kinase C-β1 overexpression. Effects on stimulation by α-thrombin, guanosine 5′-O-(thiotriphosphate). and calcium
    • Pachter, J. A., Pai, J.-K., Mayer-Ezell, R., Petrin, J. M., Dobek, E. & Bishop, W. R. (1992) Differential regulation of phosphoinositide and phosphatildylcholine hydrolysis by protein kinase C-β1 overexpression. Effects on stimulation by α-thrombin, guanosine 5′-O-(thiotriphosphate). and calcium, J. Biol. Chem. 267, 9826-9830.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9826-9830
    • Pachter, J.A.1    Pai, J.-K.2    Mayer-Ezell, R.3    Petrin, J.M.4    Dobek, E.5    Bishop, W.R.6
  • 76
    • 0028931859 scopus 로고
    • Stimulation of phospholipase D by epidermal growth factor requires protein kinase C activation in Swiss 3T3 cells
    • Yeo, E.-J. & Exton, J. H. (1995) Stimulation of phospholipase D by epidermal growth factor requires protein kinase C activation in Swiss 3T3 cells, J. Biol. Chem. 270, 3980-3988.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3980-3988
    • Yeo, E.-J.1    Exton, J.H.2
  • 77
    • 0028034025 scopus 로고
    • Activation of phospholipase D induced by platelet-derived growth factor is dependent upon the level of phospholipase C-γ1
    • 76a. Lee, Y. H., Kim, H. S., Pai, J.-K., Ryu, S. H. & Suh, P.-G. (1994) Activation of phospholipase D induced by platelet-derived growth factor is dependent upon the level of phospholipase C-γ1, J. Biol. Chem. 269, 26842-26847.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26842-26847
    • Lee, Y.H.1    Kim, H.S.2    Pai, J.-K.3    Ryu, S.H.4    Suh, P.-G.5
  • 78
    • 0026767452 scopus 로고
    • Activation of phospholipase D by protein kinase C. Evidence for a phosphorylation-independent mechanism
    • Conricode, K. M., Brewer, K. A. & Exton, J. H. (1992) Activation of phospholipase D by protein kinase C. Evidence for a phosphorylation-independent mechanism, J. Biol. Chem. 267, 7199-7202.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7199-7202
    • Conricode, K.M.1    Brewer, K.A.2    Exton, J.H.3
  • 79
    • 0028269446 scopus 로고
    • Phospholipase D activation in fibroblast membranes by the α and β isoforms of protein kinase C
    • Conricode, K. M., Smith, J. L., Burns, D. J. & Exton, J. H. (1994) Phospholipase D activation in fibroblast membranes by the α and β isoforms of protein kinase C, FEBS Lett. 342, 149-153.
    • (1994) FEBS Lett. , vol.342 , pp. 149-153
    • Conricode, K.M.1    Smith, J.L.2    Burns, D.J.3    Exton, J.H.4
  • 80
    • 0029671455 scopus 로고    scopus 로고
    • Regulation of phospholipase D by protein kinase C is synergistic with ADP-ribosylation factor and independent of protein kinase activity
    • Singer, W. D., Brown, H. A., Jiang, X. & Sternweis, P. C. (1996) Regulation of phospholipase D by protein kinase C is synergistic with ADP-ribosylation factor and independent of protein kinase activity, J. Biol. Chem. 271, 4504-4510.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4504-4510
    • Singer, W.D.1    Brown, H.A.2    Jiang, X.3    Sternweis, P.C.4
  • 81
    • 0030044056 scopus 로고    scopus 로고
    • Regulation of membrane-bound phospholipase D by protein kinase C in HL60 cells. Synergistic action of small GTP-binding protein RhoA
    • Ohguchi, K., Banno, Y., Nakashima, S. & Nozawa, Y. (1996) Regulation of membrane-bound phospholipase D by protein kinase C in HL60 cells. Synergistic action of small GTP-binding protein RhoA, J. Biol. Chem. 271, 4366-4372.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4366-4372
    • Ohguchi, K.1    Banno, Y.2    Nakashima, S.3    Nozawa, Y.4
  • 82
    • 0029015710 scopus 로고
    • Structure and function of ARF proteins: Activators of cholera toxin and critical components of intracellular vesicular transport processes
    • Moss, J. & Vaughan, M. (1995) Structure and function of ARF proteins: activators of cholera toxin and critical components of intracellular vesicular transport processes. J. Biol. Chem. 270, 12327-12330.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12327-12330
    • Moss, J.1    Vaughan, M.2
  • 83
    • 0027142022 scopus 로고
    • ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity
    • Brown, H. A., Gutowski, S., Moomaw, C. R., Slaughter, C. & Sternweis, P. C. (1993) ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity, Cell 75, 1137-1144.
    • (1993) Cell , vol.75 , pp. 1137-1144
    • Brown, H.A.1    Gutowski, S.2    Moomaw, C.R.3    Slaughter, C.4    Sternweis, P.C.5
  • 85
    • 0028843233 scopus 로고
    • Low molecular mass GTP-binding proteins in HL-60 granulocytes. Assessment of the role of ARF and of a 50-kDa cytosolic protein in phospholipase D activation
    • Bourgoin, S., Harbour, D., Desmarais, Y., Takai, Y. & Beaulieu, A. (1995) Low molecular mass GTP-binding proteins in HL-60 granulocytes. Assessment of the role of ARF and of a 50-kDa cytosolic protein in phospholipase D activation, J. Biol. Chem. 270, 3172-3178.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3172-3178
    • Bourgoin, S.1    Harbour, D.2    Desmarais, Y.3    Takai, Y.4    Beaulieu, A.5
  • 86
    • 0028878026 scopus 로고
    • ADP-ribosylation factor functions synergistically with a 50 kDa cytosolic factor in cell-free activation of human neutrophil phospholipase D
    • Lambeth, J. D., Kwak, J.-Y., Bowman, E. P., Perry, D., Uhlinger, D. J. & Lopez, I. (1995) ADP-ribosylation factor functions synergistically with a 50 kDa cytosolic factor in cell-free activation of human neutrophil phospholipase D, J. Biol. Chem. 270, 2431-2434.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2431-2434
    • Lambeth, J.D.1    Kwak, J.-Y.2    Bowman, E.P.3    Perry, D.4    Uhlinger, D.J.5    Lopez, I.6
  • 87
    • 0029155727 scopus 로고
    • ADP-ribosylation factor translocation correlates with potentiation of GTPγS-stimulated phospholipase D activity in membrane fractions of HL-60 cells
    • Houle, M. G., Kahn, R. A., Naccache, P. H. & Bourgoin, S. (1995) ADP-ribosylation factor translocation correlates with potentiation of GTPγS-stimulated phospholipase D activity in membrane fractions of HL-60 cells, J. Biol. Chem. 270, 22795-22800.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22795-22800
    • Houle, M.G.1    Kahn, R.A.2    Naccache, P.H.3    Bourgoin, S.4
  • 88
    • 0028791183 scopus 로고
    • Evidence for ADP-ribosylation-factor-mediated activation of phospholipase D by m3 muscarinic acetylcholine receptor
    • Rümenapp, U., Geiszt, M., Wahn, F., Schmidt, M. & Jakobs, K. H. (1995) Evidence for ADP-ribosylation-factor-mediated activation of phospholipase D by m3 muscarinic acetylcholine receptor, Eur. J. Biochem. 234, 240-244.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 240-244
    • Rümenapp, U.1    Geiszt, M.2    Wahn, F.3    Schmidt, M.4    Jakobs, K.H.5
  • 89
    • 0026677375 scopus 로고
    • Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein
    • Donaldson, J. G., Dinazzi, D. & Klausner, R. D. (1992) Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein, Nature 360, 350-352.
    • (1992) Nature , vol.360 , pp. 350-352
    • Donaldson, J.G.1    Dinazzi, D.2    Klausner, R.D.3
  • 90
    • 0026746713 scopus 로고
    • Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF
    • Helms, J. B. & Rothman, J. E. (1992) Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF, Nature 360, 352-354.
    • (1992) Nature , vol.360 , pp. 352-354
    • Helms, J.B.1    Rothman, J.E.2
  • 91
    • 0029968827 scopus 로고    scopus 로고
    • Rho family GTPases: The cytoskeleton and beyond
    • Symons, M. (1996) Rho family GTPases: the cytoskeleton and beyond. Trends Biochem. Sci. 21, 178-181.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 178-181
    • Symons, M.1
  • 92
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D. & Hall, A. (1995) Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia, Cell 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 93
    • 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. & Hall, A. (1992) 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) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 94
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A. J., Paterson, H. F., Johnston, C. L., Diegmann, D. & Hall, A. (1992) The small GTP-binding protein rac regulates growth factor-induced membrane ruffling, Cell 70, 401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diegmann, D.4    Hall, A.5
  • 95
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
    • Kozma, R., Ahmed, S., Best, A. & Lim, L. (1995) The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts, Mol. Cell. Biol. 15, 1942-1952.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1942-1952
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 96
    • 0028903247 scopus 로고
    • An essential role for Rac in Ras transformation
    • Qiu, R.-G., Chen, J., Korn, D., McCormick, F. & Symons, M. (1995) An essential role for Rac in Ras transformation, Nature 374, 457-459.
    • (1995) Nature , vol.374 , pp. 457-459
    • Qiu, R.-G.1    Chen, J.2    Korn, D.3    McCormick, F.4    Symons, M.5
  • 99
    • 0028800305 scopus 로고
    • Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation
    • Khosravi-Far, R., Solski, P. A., Clark, G. J., Kinch, M. S. & Der, C. J. (1995) Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation, Mol. Cell. Biol. 15, 6443-6453.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6443-6453
    • Khosravi-Far, R.1    Solski, P.A.2    Clark, G.J.3    Kinch, M.S.4    Der, C.J.5
  • 101
    • 0027372389 scopus 로고
    • Neutrophil phospholipase D is activated by a membrane-associated Rho family small molecular mass GTP-binding protein
    • Bowman, E. P., Uhlinger, D. J. & Lambeth, J. D. (1993) Neutrophil phospholipase D is activated by a membrane-associated Rho family small molecular mass GTP-binding protein, J. Biol. Chem. 268, 21509-21512.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21509-21512
    • Bowman, E.P.1    Uhlinger, D.J.2    Lambeth, J.D.3
  • 102
    • 0028784295 scopus 로고
    • RhoA and a cytosolic 50-kDa factor reconstitute GTPγS-dependent phospholipase D activity in human neutrophil subcellular fractions
    • Kwak, J.-Y., Lopez, I., Uhlinger, D. J., Ryu, S. Y. & Lambeth, J. D. (1995) RhoA and a cytosolic 50-kDa factor reconstitute GTPγS-dependent phospholipase D activity in human neutrophil subcellular fractions, J. Biol. Chem. 270, 27093-27098.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27093-27098
    • Kwak, J.-Y.1    Lopez, I.2    Uhlinger, D.J.3    Ryu, S.Y.4    Lambeth, J.D.5
  • 103
    • 0029064643 scopus 로고
    • Activation of membrane-hound phospholipase D by protein kinase C in HL60 cells: Synergistic action of a small GTP-binding protein RhoA
    • Ohguchi, K., Banno, Y. Nakashima, S. & Nozawa, Y. (1995) Activation of membrane-hound phospholipase D by protein kinase C in HL60 cells: synergistic action of a small GTP-binding protein RhoA. Biochem. Biophys. Res. Commun. 211, 306-311.
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 306-311
    • Ohguchi, K.1    Banno, Y.2    Nakashima, S.3    Nozawa, Y.4
  • 104
    • 0029610366 scopus 로고
    • Nuclear phospholipase D in Madin-Darby canine kidney cells. Guanosine 5′-O-(thiolriphosphate)-stimulated activation is mediated by RhoA and is downstream of protein kinase C
    • Balboa, M. A. & Insel, P. A. (1995) Nuclear phospholipase D in Madin-Darby canine kidney cells. Guanosine 5′-O-(thiolriphosphate)-stimulated activation is mediated by RhoA and is downstream of protein kinase C, J. Biol. Chem. 270, 29843-29847.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29843-29847
    • Balboa, M.A.1    Insel, P.A.2
  • 105
    • 0028788631 scopus 로고
    • Synergistic activation of rat brain phospholipase D by ADP-ribosylation factor and rhoA p21, and its inhibition by Clostridium botulinum C3 exoenzyme
    • Kuribara, H., Tago, K., Yokozeki, T., Sasaki, T., Takai, Y., Morii, N., Narumiya, S., Katada, T. & Kanaho, Y. (1995) Synergistic activation of rat brain phospholipase D by ADP-ribosylation factor and rhoA p21, and its inhibition by Clostridium botulinum C3 exoenzyme, J. Biol. Chem. 270, 25667-25671.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25667-25671
    • Kuribara, H.1    Tago, K.2    Yokozeki, T.3    Sasaki, T.4    Takai, Y.5    Morii, N.6    Narumiya, S.7    Katada, T.8    Kanaho, Y.9
  • 106
    • 0030037396 scopus 로고    scopus 로고
    • Activation of phospholipase D and phosphatidylinositol 4-phosphate 5-kinase in HL60 membranes is mediated by endogenous Arf but not Rho
    • Martin, A., Brown, F. D., Hodgkin, M. N., Brudwell, A. J., Cook, S. J., Hart, M. & Wakelam, M. J. O. (1996) Activation of phospholipase D and phosphatidylinositol 4-phosphate 5-kinase in HL60 membranes is mediated by endogenous Arf but not Rho, J. Biol. Chem. 271, 17397-17403.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17397-17403
    • Martin, A.1    Brown, F.D.2    Hodgkin, M.N.3    Brudwell, A.J.4    Cook, S.J.5    Hart, M.6    Wakelam, M.J.O.7
  • 107
    • 12644264656 scopus 로고    scopus 로고
    • Differential translocation of Rho-family GTPases by lysophosphatidic acid, ebdothelin-1 and platelet-derived growth factor
    • in the press
    • Fleming, I. N. & Exton, J. H. (1996) Differential translocation of Rho-family GTPases by lysophosphatidic acid, ebdothelin-1 and platelet-derived growth factor, J. Biol. Chem., in the press.
    • (1996) J. Biol. Chem.
    • Fleming, I.N.1    Exton, J.H.2
  • 108
    • 0029941137 scopus 로고    scopus 로고
    • Reconstitution of GTP-γ-S-dependent phospholipase D activity with ARF, RhoA, and a soluble 36-kDa protein
    • Shimooku, K., Akisue, T., Jinnai, H., Hitomi, T., Ogino, C., Yoshida, K., Nakamura, S.-I. & Nishizuka, Y. (1996) Reconstitution of GTP-γ-S-dependent phospholipase D activity with ARF, RhoA, and a soluble 36-kDa protein, FEBS Lett. 387, 141-144.
    • (1996) FEBS Lett. , vol.387 , pp. 141-144
    • Shimooku, K.1    Akisue, T.2    Jinnai, H.3    Hitomi, T.4    Ogino, C.5    Yoshida, K.6    Nakamura, S.-I.7    Nishizuka, Y.8
  • 109
    • 0030063978 scopus 로고    scopus 로고
    • Inhibition of receptor signaling to phospholipase D by Clostridium difficile toxin B. Role of Rho proteins
    • Schmidt, M., Rümenapp, U., Bienek, C., Keller, J., von Eichel-Streiber, C. & Jakobs, K. H. (1996) Inhibition of receptor signaling to phospholipase D by Clostridium difficile toxin B. Role of Rho proteins, J. Biol. Chem. 271, 2422-2426.
    • (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
  • 110
    • 0024392752 scopus 로고
    • Long-term phorbol ester treatment dissociates phospholipase D activation from phosphoinositide hydrolysis and prostacyclin synthesis in endothelial cells stimulated with bradykinin
    • Martin, T. W., Feldman, D. R., Goldstein, K. E. & Wagner, J. R. (1989) Long-term phorbol ester treatment dissociates phospholipase D activation from phosphoinositide hydrolysis and prostacyclin synthesis in endothelial cells stimulated with bradykinin, Biochem. Biophys. Res. Commun. 165, 319-326.
    • (1989) Biochem. Biophys. Res. Commun. , vol.165 , pp. 319-326
    • Martin, T.W.1    Feldman, D.R.2    Goldstein, K.E.3    Wagner, J.R.4
  • 111
    • 16844366239 scopus 로고    scopus 로고
    • Evidence for Rho-mediated agonist stimulation of phospholipase D in Rat1 fibroblasts. Effects of Clostridium botulinum C3 exoenzyme
    • 109a. Malcolm, K. C., Elliott, C. M. & Exton, J. H. (1996) Evidence for Rho-mediated agonist stimulation of phospholipase D in Rat1 fibroblasts. Effects of Clostridium botulinum C3 exoenzyme, J. Biol. Chem. 271, 13135-13139.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13135-13139
    • Malcolm, K.C.1    Elliott, C.M.2    Exton, J.H.3
  • 112
    • 0031019308 scopus 로고    scopus 로고
    • Role of Rho family proteins in phospholipase D activation by growth factors
    • in the press
    • Hess, J. A., Ross, A. H., Qiu, R.-G., Symons, M. & Exton, J. H. (1997) Role of Rho family proteins in phospholipase D activation by growth factors, J. Biol. Chem., in the press.
    • (1997) J. Biol. Chem.
    • Hess, J.A.1    Ross, A.H.2    Qiu, R.-G.3    Symons, M.4    Exton, J.H.5


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