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Volumn 17, Issue 2, 1998, Pages 406-413

The heterotrimeric G protein Go2 regulates catecholamine uptake by secretory vesicles

Author keywords

Catecholamine uptake; Heterotrimeric G protein Go; PC 12 cells; Secretory vesicles; Signal transduction

Indexed keywords

ANTIBODY; CATECHOLAMINE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); GUANOSINE TRIPHOSPHATE DERIVATIVE; NEUROTRANSMITTER; NORADRENALIN; PROTEIN SUBUNIT; RESERPINE; STREPTOLYSIN O; TETANUS TOXIN; TRITIUM;

EID: 0345084463     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.2.406     Document Type: Article
Times cited : (48)

References (37)
  • 1
    • 0023522389 scopus 로고
    • 2+-stimulated catecholamine release from permeabilized PC 12 cells: Biochemical evidence for exocytosis and its modulation by protein kinase C and G-proteins
    • 2+-stimulated catecholamine release from permeabilized PC 12 cells: biochemical evidence for exocytosis and its modulation by protein kinase C and G-proteins. Biochemistry, 26, 7842-7848.
    • (1989) Biochemistry , vol.26 , pp. 7842-7848
    • Ahnert-Hilger, G.1    Bräutigam, M.2    Gratzl, M.3
  • 2
    • 0024368011 scopus 로고
    • Poration by alphatoxin and streptolysin O: An approach to analyze intracellular processes
    • Ahnert-Hilger, G., Mach, W., Föhr, K.-J. and Gratzl, M. (1989b) Poration by alphatoxin and streptolysin O: an approach to analyze intracellular processes. Methods Cell Biol., 31, 63-90.
    • (1989) Methods Cell Biol. , vol.31 , pp. 63-90
    • Ahnert-Hilger, G.1    Mach, W.2    Föhr, K.-J.3    Gratzl, M.4
  • 4
    • 0026747028 scopus 로고
    • Exocytosis from permeabilized bovine adrenal chromaffin cells is differently modulated by GTPτS and GMPPNHP. Evidence for the involvement of various guanine nucleotide binding-protein
    • Ahnert-Hilger, G., Wegenhorst, U., Stecher, B., Spicher, K., Rosenthal, W. and Gratzl, M. (1992) Exocytosis from permeabilized bovine adrenal chromaffin cells is differently modulated by GTPτS and GMPPNHP. Evidence for the involvement of various guanine nucleotide binding-protein. Biochem. J., 284, 321-326.
    • (1992) Biochem. J. , vol.284 , pp. 321-326
    • Ahnert-Hilger, G.1    Wegenhorst, U.2    Stecher, B.3    Spicher, K.4    Rosenthal, W.5    Gratzl, M.6
  • 5
    • 0028143425 scopus 로고
    • Detection of G-protein heterotrimers on large dense core and small synaptic vesicles of neuroendocrine and neuronal cells
    • Ahnert-Hilger, G., Schäfer, T., Spicher, K., Grund, C. Schultz, G. and Wieden-mann, B. (1994) Detection of G-protein heterotrimers on large dense core and small synaptic vesicles of neuroendocrine and neuronal cells. Eur. J. Cell Biol., 65, 26-28.
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 26-28
    • Ahnert-Hilger, G.1    Schäfer, T.2    Spicher, K.3    Grund, C.4    Schultz, G.5    Wieden-mann, B.6
  • 6
    • 0026760089 scopus 로고
    • iα in the basal ganglia reveals its potential role in both signal transduction and vesicle trafficking
    • iα in the basal ganglia reveals its potential role in both signal transduction and vesicle trafficking. J. Neurosci., 12, 3435-3444.
    • (1992) J. Neurosci. , vol.12 , pp. 3435-3444
    • Aronin, N.1    DiFiglia, M.2
  • 7
    • 0023086182 scopus 로고
    • Damage to mammalian cells by proteins that form transmembrane pores
    • Bhakdi, S. and Tranum-Jensen, J. (1987) Damage to mammalian cells by proteins that form transmembrane pores. Rev. Physiol. Biochem. Pharmacol., 107, 147-223.
    • (1987) Rev. Physiol. Biochem. Pharmacol. , vol.107 , pp. 147-223
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 8
    • 0025191377 scopus 로고
    • Aluminofluoride and berylofluoride complexes: A new phosphate analog in enzymology
    • Charbre, M. (1990) Aluminofluoride and berylofluoride complexes: a new phosphate analog in enzymology. Trends Biochem. Sci., 15, 6-10.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 6-10
    • Charbre, M.1
  • 9
    • 0028919858 scopus 로고
    • Cellubrevin and synaptobrevins: Similar subcellular localization and biochemical properties in PC 12 cells
    • Chilcote, T.J., Galli, T., Mundigl, O., Edelmann, L., McPherson, P.S., Takai, K. and DeCamilli, P. (1995) Cellubrevin and synaptobrevins: similar subcellular localization and biochemical properties in PC 12 cells. J. Cell Biol., 129, 219-231.
    • (1995) J. Cell Biol. , vol.129 , pp. 219-231
    • Chilcote, T.J.1    Galli, T.2    Mundigl, O.3    Edelmann, L.4    McPherson, P.S.5    Takai, K.6    DeCamilli, P.7
  • 10
    • 0026939128 scopus 로고
    • The transport of neurotransmitters into synaptic vesicles
    • Edwards, R.H. (1992) The transport of neurotransmitters into synaptic vesicles. Curr. Opin. Neurobiol., 2, 586-594.
    • (1992) Curr. Opin. Neurobiol. , vol.2 , pp. 586-594
    • Edwards, R.H.1
  • 11
    • 0026664632 scopus 로고
    • Resolution of regulated secretion into sequential MgATP-dependent and calcium-dependent stages mediated by distinct cytosolic proteins
    • Hay, J.C. and Martin, T.F.J. (1992) Resolution of regulated secretion into sequential MgATP-dependent and calcium-dependent stages mediated by distinct cytosolic proteins. J. Cell Biol., 119, 139-151.
    • (1992) J. Cell Biol. , vol.119 , pp. 139-151
    • Hay, J.C.1    Martin, T.F.J.2
  • 12
    • 0025041769 scopus 로고
    • Energy dependence and functional reconstitution of the γ-aminobutyric acid carrier from synaptic vesicles
    • Hell, J.W., Maycox, P.R. and Jahn, R.J. (1990) Energy dependence and functional reconstitution of the γ-aminobutyric acid carrier from synaptic vesicles. Biol. Chem., 265, 2111-2117.
    • (1990) Biol. Chem. , vol.265 , pp. 2111-2117
    • Hell, J.W.1    Maycox, P.R.2    Jahn, R.J.3
  • 14
    • 0029921401 scopus 로고    scopus 로고
    • Voltage-dependent modulation of N-type calcium channels by G-protein βγ subunits
    • Ikeda, S.R. (1996) Voltage-dependent modulation of N-type calcium channels by G-protein βγ subunits. Nature, 380, 255-258.
    • (1996) Nature , vol.380 , pp. 255-258
    • Ikeda, S.R.1
  • 15
    • 0021273199 scopus 로고
    • Mechanism of pertussis toxin action on the adenylate system: Inhibition of the turn-on reaction of the inhibitory regulatory site
    • Jakobs, K.H., Aktories, K. and Schultz, G. (1984) Mechanism of pertussis toxin action on the adenylate system: inhibition of the turn-on reaction of the inhibitory regulatory site. Eur. J. Biochem., 140, 177-181.
    • (1984) Eur. J. Biochem. , vol.140 , pp. 177-181
    • Jakobs, K.H.1    Aktories, K.2    Schultz, G.3
  • 16
    • 0023872141 scopus 로고
    • Accumulation of biological amines into chromaffin granules: A model for hormone and neurotransmitter transport
    • Johnson, R. (1988) Accumulation of biological amines into chromaffin granules: a model for hormone and neurotransmitter transport. Physiol. Rev., 68, 232-307.
    • (1988) Physiol. Rev. , vol.68 , pp. 232-307
    • Johnson, R.1
  • 17
    • 0030575941 scopus 로고    scopus 로고
    • Specificity of interaction between receptor and G-protein: Use of antisense techniques to relate G-protein subunits to function
    • Kalkbrenner, F., Dippel, E., Wittig, B. and Schultz, G. (1996) Specificity of interaction between receptor and G-protein: use of antisense techniques to relate G-protein subunits to function. Biochim. Biophys. Acta. 1314, 125-139.
    • (1996) Biochim. Biophys. Acta. , vol.1314 , pp. 125-139
    • Kalkbrenner, F.1    Dippel, E.2    Wittig, B.3    Schultz, G.4
  • 18
    • 0030965452 scopus 로고    scopus 로고
    • Phosphorylation of a vesicular monoamine transporter by casein kinase II
    • Krantz, D.E., Peter, D., Liu, Y. and Edwards, H. (1997) Phosphorylation of a vesicular monoamine transporter by casein kinase II. J. Biol. Chem., 272, 6752-6759.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6752-6759
    • Krantz, D.E.1    Peter, D.2    Liu, Y.3    Edwards, H.4
  • 20
    • 0031044233 scopus 로고    scopus 로고
    • The role of vesicular transport proteins in synaptic transmission and neural degeneration
    • Liu, Y. and Edwards, R. (1997) The role of vesicular transport proteins in synaptic transmission and neural degeneration. Annu. Rev. Neurosci., 20, 125-156.
    • (1997) Annu. Rev. Neurosci. , vol.20 , pp. 125-156
    • Liu, Y.1    Edwards, R.2
  • 22
    • 0025021999 scopus 로고
    • Amino acid neurotransmission: Spotlights on synaptic vesicles
    • Maycox, P.R., Hell, J.W. and Jahn, R. (1990) Amino acid neurotransmission: spotlights on synaptic vesicles. Trends Neurosci., 13, 83-87.
    • (1990) Trends Neurosci. , vol.13 , pp. 83-87
    • Maycox, P.R.1    Hell, J.W.2    Jahn, R.3
  • 23
    • 0028850893 scopus 로고
    • Cyclic AMP-dependent modulation of vesicular monoamine transport in pheochromocytoma cells
    • Nakanishi, N., Onozawa, S., Matsumoto, R., Hasegawa, H. and Yamada, S. (1995) Cyclic AMP-dependent modulation of vesicular monoamine transport in pheochromocytoma cells. J. Neurochem., 64, 600-607.
    • (1995) J. Neurochem. , vol.64 , pp. 600-607
    • Nakanishi, N.1    Onozawa, S.2    Matsumoto, R.3    Hasegawa, H.4    Yamada, S.5
  • 24
    • 0030600131 scopus 로고    scopus 로고
    • Potential roles of heterotrimeric G proteins of the endomembrane system
    • Nürnberg, B. and Ahnert-Hilger, G. (1996) Potential roles of heterotrimeric G proteins of the endomembrane system. FEBS Lett., 389, 61-65.
    • (1996) FEBS Lett. , vol.389 , pp. 61-65
    • Nürnberg, B.1    Ahnert-Hilger, G.2
  • 26
    • 0028263975 scopus 로고
    • The chromaffin granule and synaptic vesicle amine transporters differ in substrate recognition and sensitivity to inhibitors
    • Peter, D., Jiminez, J., Liu, Y., Kim, J. and Edwards, R.H. (1994) The chromaffin granule and synaptic vesicle amine transporters differ in substrate recognition and sensitivity to inhibitors. J. Biol. Chem., 269, 7231-7237.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7231-7237
    • Peter, D.1    Jiminez, J.2    Liu, Y.3    Kim, J.4    Edwards, R.H.5
  • 27
    • 0025097871 scopus 로고
    • Energetics of reserpine binding and occlusion by the chromaffin granule biogenic amine transporter
    • Rudnick, G., Steiner-Mordoch, S.S., Fishkes, H., Stern-Bach, Y. and Schuldiner, S. (1990) Energetics of reserpine binding and occlusion by the chromaffin granule biogenic amine transporter. Biochemistry, 29, 603-608.
    • (1990) Biochemistry , vol.29 , pp. 603-608
    • Rudnick, G.1    Steiner-Mordoch, S.S.2    Fishkes, H.3    Stern-Bach, Y.4    Schuldiner, S.5
  • 28
    • 0028132743 scopus 로고
    • Neurotransmitter transporters: New members of known families
    • Schloss, P., Püschel, A.W. and Betz, H. (1994) Neurotransmitter transporters: new members of known families. Curr. Opin. Cell Biol., 6, 595-599.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 595-599
    • Schloss, P.1    Püschel, A.W.2    Betz, H.3
  • 29
    • 0017867128 scopus 로고
    • Role of a transmembrane pH gradient in epinephrine transport by chromaffin granule membrane vesicles
    • Schuldiner, S., Fishkes, H. and Kanner, B.I. (1978) Role of a transmembrane pH gradient in epinephrine transport by chromaffin granule membrane vesicles. Proc. Natl Acad. Sci. USA, 75, 3713-3716.
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 3713-3716
    • Schuldiner, S.1    Fishkes, H.2    Kanner, B.I.3
  • 31
    • 0025247884 scopus 로고
    • Identification and purification of a functional amine transporter from bovine chromaffin granules
    • Stern-Bach, Y., Greenberg-Ofrath, N., Flechner, I. and Schuldiner, S. (1990) Identification and purification of a functional amine transporter from bovine chromaffin granules. J. Biol. Chem., 265, 3961-3966.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3961-3966
    • Stern-Bach, Y.1    Greenberg-Ofrath, N.2    Flechner, I.3    Schuldiner, S.4
  • 34
    • 0026008186 scopus 로고
    • The regulation of quantal size
    • Van der Kloot, W. (1991) The regulation of quantal size. Prog. Neurobiol., 36, 93-130.
    • (1991) Prog. Neurobiol. , vol.36 , pp. 93-130
    • Van Der Kloot, W.1
  • 35
    • 0028149889 scopus 로고
    • GAP-43 controls the availability of secretory chromaffin granules for regulated exocytosis by stimulating a granule-associated Go
    • Vitale, N., Deloulme, J.-C., Thierse, D., Aunis, D. and Bader, M.F. (1994) GAP-43 controls the availability of secretory chromaffin granules for regulated exocytosis by stimulating a granule-associated Go. J. Biol. Chem., 269, 30293-30298.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30293-30298
    • Vitale, N.1    Deloulme, J.-C.2    Thierse, D.3    Aunis, D.4    Bader, M.F.5
  • 36
    • 0029864710 scopus 로고    scopus 로고
    • Expression of active streptolysin-O in E. coli as maltose-binding protein-streptolysin-O fusion protein: The N-terminal 70 amino acids are not required for hemolytic activity
    • Weller, U., Müller, L., Meßner, M. and Bhakdi, S. (1996) Expression of active streptolysin-O in E. coli as maltose-binding protein-streptolysin-O fusion protein: the N-terminal 70 amino acids are not required for hemolytic activity. Eur. J. Biochem., 236, 34-39.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 34-39
    • Weller, U.1    Müller, L.2    Meßner, M.3    Bhakdi, S.4
  • 37
    • 0029583203 scopus 로고
    • The pharmacological profile of the vesicular monoamine transporter resembles that of multidrug transporters
    • Yelin, R. and Schuldiner, S. (1995) The pharmacological profile of the vesicular monoamine transporter resembles that of multidrug transporters. FEBS Lett., 377, 201-207.
    • (1995) FEBS Lett. , vol.377 , pp. 201-207
    • Yelin, R.1    Schuldiner, S.2


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