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Volumn 20, Issue 5, 2000, Pages 569-577

Forskolin modulates acetylcholine receptor gating by interacting with the small extracellular loop between the M2 and M3 transmembrane domains

Author keywords

Allosteric modulator; Chimeric subunits; Forskolin; Nicotinic acetylcholine receptors; Transduction

Indexed keywords

FORSKOLIN; NICOTINIC RECEPTOR; HYBRID PROTEIN;

EID: 0034297331     PISSN: 02724340     EISSN: None     Source Type: Journal    
DOI: 10.1023/a:1007011911611     Document Type: Article
Times cited : (4)

References (36)
  • 2
    • 0017755172 scopus 로고
    • Voltage jump analysis of procaine action at frog end-plate
    • Adams, P. R. (1977). Voltage jump analysis of procaine action at frog end-plate. J. Physiol. (Lond.) 268:291-318.
    • (1977) J. Physiol. (Lond.) , vol.268 , pp. 291-318
    • Adams, P.R.1
  • 3
    • 0027052187 scopus 로고
    • Forskolin acts as a noncompetitive inhibitor of nicotinic acetylcholine receptors
    • Aylwin, M. L., and White, M. M. (1992). Forskolin acts as a noncompetitive inhibitor of nicotinic acetylcholine receptors. Mol. Pharmacol. 41:908-913.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 908-913
    • Aylwin, M.L.1    White, M.M.2
  • 4
    • 0024268177 scopus 로고
    • Control of Torpedo acetylcholine receptor biosynthesis in Xenopus oocytes
    • Buller, A. L., and White, M. M. (1988). Control of Torpedo acetylcholine receptor biosynthesis in Xenopus oocytes. Proc. Natl. Acad. Sci. USA 85:8717-8721.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8717-8721
    • Buller, A.L.1    White, M.M.2
  • 5
    • 0029954238 scopus 로고    scopus 로고
    • A single residue in the M2-M3 loop is a major determinant of coupling between binding and gating in neuronal nicotinic receptors
    • Campos-Caro, A., Sala, S., Ballesta, J. J., Vicente-Agullo, F., Criado, M., and Sala, F. (1996). A single residue in the M2-M3 loop is a major determinant of coupling between binding and gating in neuronal nicotinic receptors. Proc. Natl. Acad. Sci. USA 93:6118-6123.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6118-6123
    • Campos-Caro, A.1    Sala, S.2    Ballesta, J.J.3    Vicente-Agullo, F.4    Criado, M.5    Sala, F.6
  • 6
    • 0022558294 scopus 로고
    • Effects of chlorpromazine and phencyclidine on mouse C2 acetylcholine receptor kinetics
    • Changeux, J.-P., Pinset, C., and Ribera, A. B. (1986). Effects of chlorpromazine and phencyclidine on mouse C2 acetylcholine receptor kinetics. J. Physiol. (Lond.) 378:497-513.
    • (1986) J. Physiol. (Lond.) , vol.378 , pp. 497-513
    • Changeux, J.-P.1    Pinset, C.2    Ribera, A.B.3
  • 7
    • 0025355129 scopus 로고
    • An open-channel blocker interacts with adjacent turns of alpha-helices in the nicotinic acetylcholine receptor
    • Charnet, P., Labarca, C., Leonard, R. J., Vogelaar, N. J., Czyzyk, L., Gouin, A., Davidson, N., and Lester, H. A. (1990). An open-channel blocker interacts with adjacent turns of alpha-helices in the nicotinic acetylcholine receptor. Neuron 4:87-95.
    • (1990) Neuron , vol.4 , pp. 87-95
    • Charnet, P.1    Labarca, C.2    Leonard, R.J.3    Vogelaar, N.J.4    Czyzyk, L.5    Gouin, A.6    Davidson, N.7    Lester, H.A.8
  • 8
    • 0031468619 scopus 로고    scopus 로고
    • Identification of amino acids contributing to high and low affinity d-tubocurarine sites on the Torpedo nicotinic acetylcholine receptor
    • Chiara, D. C., and Cohen, J. B. (1997). Identification of amino acids contributing to high and low affinity d-tubocurarine sites on the Torpedo nicotinic acetylcholine receptor. J. Biol. Chem. 272:32940-32950.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32940-32950
    • Chiara, D.C.1    Cohen, J.B.2
  • 9
    • 0027522236 scopus 로고
    • Functional architecture of the nicotinic acetylcholine receptor: A prototype of ligand-gated ion channels
    • Devillers-Thiery, A., Galzi, J. L., Eisele, J. L., Bertrand, S., Bertrand, D., and Changeux, J. P. (1993). Functional architecture of the nicotinic acetylcholine receptor: A prototype of ligand-gated ion channels. J. Membr. Biol. 136:97-112.
    • (1993) J. Membr. Biol. , vol.136 , pp. 97-112
    • Devillers-Thiery, A.1    Galzi, J.L.2    Eisele, J.L.3    Bertrand, S.4    Bertrand, D.5    Changeux, J.P.6
  • 10
    • 0025291849 scopus 로고
    • 3H]quinacrine azide in the active state of the nicotinic acetylcholine receptor
    • 3H]quinacrine azide in the active state of the nicotinic acetylcholine receptor. J. Biol. Chem. 265:11017-11029.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11017-11029
    • DiPaola, M.1    Kao, P.N.2    Karlin, A.3
  • 11
    • 0027223874 scopus 로고
    • Selective enhancement of the interaction of curare with the acetylcholine receptor
    • Filatov, G. N., Aylwin, M. L., and White, M. M. (1993). Selective enhancement of the interaction of curare with the acetylcholine receptor. Mol. Pharmacol. 44:237-241.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 237-241
    • Filatov, G.N.1    Aylwin, M.L.2    White, M.M.3
  • 12
    • 0029123899 scopus 로고
    • The role of conserved leucines in the M2 domain of the acetylcholine receptor in channel gating
    • Filatov, G. N., and White, M. M. (1995). The role of conserved leucines in the M2 domain of the acetylcholine receptor in channel gating. Mol. Pharmacol. 48:379-384.
    • (1995) Mol. Pharmacol. , vol.48 , pp. 379-384
    • Filatov, G.N.1    White, M.M.2
  • 14
    • 0004165099 scopus 로고
    • San Diego, CA: Academic Press
    • Higuchi, R. (1990). Recombinant PCR. San Diego, CA: Academic Press, 177-184.
    • (1990) Recombinant PCR , pp. 177-184
    • Higuchi, R.1
  • 15
    • 0030011258 scopus 로고    scopus 로고
    • The emerging three-dimensional structure of a receptor: The nicotinic acetylcholine receptor
    • Hucho, F., Tsetlin, V. I., and Machold, J. (1996). The emerging three-dimensional structure of a receptor: The nicotinic acetylcholine receptor. Eur. J. Biochem. 239:539-557.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 539-557
    • Hucho, F.1    Tsetlin, V.I.2    Machold, J.3
  • 16
    • 0021132711 scopus 로고
    • Identification of α subunit half-cystine specifically labelled by an affinity reagent for the acetylcholine receptor binding site
    • Kao, P. N., Dwork, A. J., Kaldany, R.-R. J., Silver, M. L., Wideman, J., Stein, S., and Karlin, A. (1984). Identification of α subunit half-cystine specifically labelled by an affinity reagent for the acetylcholine receptor binding site. J. Biol. Chem. 259:11662-11665.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11662-11665
    • Kao, P.N.1    Dwork, A.J.2    Kaldany, R.-R.J.3    Silver, M.L.4    Wideman, J.5    Stein, S.6    Karlin, A.7
  • 17
    • 0029593370 scopus 로고
    • Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins
    • Karlin, A., and Akabas, M. H. (1995). Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins. Neuron 15:1231-1244.
    • (1995) Neuron , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, M.H.2
  • 18
    • 0028177448 scopus 로고
    • Mutagenesis of the GABA pi receptor alters agonist affinity and channel gating
    • Kusama, T., Wang, J.-B., Spivak, C. E., and Uhl, G. R. (1994). Mutagenesis of the GABA pi receptor alters agonist affinity and channel gating. NeuroReport 5:1209-1212.
    • (1994) NeuroReport , vol.5 , pp. 1209-1212
    • Kusama, T.1    Wang, J.-B.2    Spivak, C.E.3    Uhl, G.R.4
  • 19
    • 0029163027 scopus 로고
    • Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors
    • Labarca, C., Nowak, M. W., Zhang, H., Tang, L., Deshpande, P., and Lester, H. A. (1995). Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors. Nature 376:514-516.
    • (1995) Nature , vol.376 , pp. 514-516
    • Labarca, C.1    Nowak, M.W.2    Zhang, H.3    Tang, L.4    Deshpande, P.5    Lester, H.A.6
  • 21
    • 0024213680 scopus 로고
    • Evidence that the M2 membrane spanning region lines the ion channel pore of the nicotinic receptor
    • Leonard, R. J., Labarca, C. G., Charnet, P., Davidson, N., and Lester, H. A. (1988). Evidence that the M2 membrane spanning region lines the ion channel pore of the nicotinic receptor. Science 242:1578-1581.
    • (1988) Science , vol.242 , pp. 1578-1581
    • Leonard, R.J.1    Labarca, C.G.2    Charnet, P.3    Davidson, N.4    Lester, H.A.5
  • 22
    • 0029018726 scopus 로고
    • Mutations affecting the glycine receptor agonist transduction mechanism convert the competitive antagonist, picrotoxin, into an allosteric potentiator
    • Lynch, J. W., Rajendra, S., Barry, P. H., and Schofield, P. R. (1995). Mutations affecting the glycine receptor agonist transduction mechanism convert the competitive antagonist, picrotoxin, into an allosteric potentiator. J. Biol. Chem. 270:13799-13806.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13799-13806
    • Lynch, J.W.1    Rajendra, S.2    Barry, P.H.3    Schofield, P.R.4
  • 23
    • 0031027684 scopus 로고    scopus 로고
    • Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor channel
    • Lynch, J. W., Rajendra, S., Pierce, K. D., Handford, C. A., Barry, P. H., and Schofield, P. R. (1997). Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor channel. EMBO J. 16:110-120.
    • (1997) EMBO J. , vol.16 , pp. 110-120
    • Lynch, J.W.1    Rajendra, S.2    Pierce, K.D.3    Handford, C.A.4    Barry, P.H.5    Schofield, P.R.6
  • 24
    • 0022970887 scopus 로고
    • Direct anesthetic-like effects of forskolin on the nicotinic acetylcholine receptors of PC12 cells
    • McHugh, E. M., and McGee, R. J. (1986). Direct anesthetic-like effects of forskolin on the nicotinic acetylcholine receptors of PC12 cells. J. Biol. Chem. 261:3103-3106.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3103-3106
    • McHugh, E.M.1    McGee, R.J.2
  • 25
    • 0017905087 scopus 로고
    • Local anesthetics transiently block currents through single acetylcholine-receptor channels
    • Neher, E., and Steinbach, J. H. (1978). Local anesthetics transiently block currents through single acetylcholine-receptor channels. J. Physiol. (Lond.) 277:153-176.
    • (1978) J. Physiol. (Lond.) , vol.277 , pp. 153-176
    • Neher, E.1    Steinbach, J.H.2
  • 26
    • 0024399875 scopus 로고
    • Mechanisms of noncompetitive inhibition of acetylcholine-induced single-channel currents
    • Papke, R. L., and Oswald, R. E. (1989). Mechanisms of noncompetitive inhibition of acetylcholine-induced single-channel currents. J. Gen. Physiol. 93:785-811.
    • (1989) J. Gen. Physiol. , vol.93 , pp. 785-811
    • Papke, R.L.1    Oswald, R.E.2
  • 27
    • 0025308169 scopus 로고
    • d-Tubocurarine binding sites are located at α-γ and α-δ subunit interfaces of the nicotinic acetylcholine receptor
    • Pedersen, S. E., and Cohen, J. B. (1990). d-Tubocurarine binding sites are located at α-γ and α-δ subunit interfaces of the nicotinic acetylcholine receptor. Proc. Natl. Acad. Sci. USA 87:2785-2789.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2785-2789
    • Pedersen, S.E.1    Cohen, J.B.2
  • 28
    • 0028361803 scopus 로고
    • Startle disease mutations reduce the agonist sensitivity of the human inhibitory glycine receptor
    • Rajendra, S., Lynch, J. W., Pierce, K. D., French, C. R., Barry, P. H., and Schofield, P. R. (1994). Startle disease mutations reduce the agonist sensitivity of the human inhibitory glycine receptor. J. Biol. Chem. 269:18739-18742.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18739-18742
    • Rajendra, S.1    Lynch, J.W.2    Pierce, K.D.3    French, C.R.4    Barry, P.H.5    Schofield, P.R.6
  • 29
    • 0025195179 scopus 로고
    • The noncompetitive blocker [3H]chlorpromazine labels three amino acids of the acetylcholine receptor gamma subunit: Implications for the alpha-helical organization of regions MII and for the structure of the ion channel
    • Revah, F., Galzi, J.-L., Giraudat, J., Haumont, P. Y., Lederer, F., and Changeux, J. P. (1990). The noncompetitive blocker [3H]chlorpromazine labels three amino acids of the acetylcholine receptor gamma subunit: Implications for the alpha-helical organization of regions MII and for the structure of the ion channel. Proc. Natl. Acad. Sci. USA 87:4675-4679.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4675-4679
    • Revah, F.1    Galzi, J.-L.2    Giraudat, J.3    Haumont, P.Y.4    Lederer, F.5    Changeux, J.P.6
  • 30
    • 0031864943 scopus 로고    scopus 로고
    • A residue in the middle of the M2-M3 loop of the beta4 subunit specifically affects gating of neuronal nicotinic receptors
    • Rovira, J. C., Ballesta, J. J., Vicente-Agullo, F., Campos-Caro, A., Criado, M., Sala, F., and Sala, M. (1998). A residue in the middle of the M2-M3 loop of the beta4 subunit specifically affects gating of neuronal nicotinic receptors. FEBS Lett. 433:89-92.
    • (1998) FEBS Lett. , vol.433 , pp. 89-92
    • Rovira, J.C.1    Ballesta, J.J.2    Vicente-Agullo, F.3    Campos-Caro, A.4    Criado, M.5    Sala, F.6    Sala, M.7
  • 31
    • 2342652901 scopus 로고
    • Forskolin: Unique diterpene activator of adenylate cyclase in membranes and in intact cells
    • Seamon, K. B., Padgett, W., and Daly, J. W. (1981). Forskolin: Unique diterpene activator of adenylate cyclase in membranes and in intact cells. Proc. Natl. Acad. Sci. USA 78:3363-3367.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 3363-3367
    • Seamon, K.B.1    Padgett, W.2    Daly, J.W.3
  • 32
    • 0020380861 scopus 로고
    • Local anesthetics and histrionicotoxin are allosteric inhibitors of the acetylcholine receptor
    • Sine, S. M., and Taylor, P. (1982). Local anesthetics and histrionicotoxin are allosteric inhibitors of the acetylcholine receptor. J. Biol. Chem. 257:8106-8114.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8106-8114
    • Sine, S.M.1    Taylor, P.2
  • 33
    • 0023753033 scopus 로고
    • Modulation of acetylcholine receptor desensitization by forskolin is independent of cAMP
    • Wagoner, P. K., and Pallotta, B. S. (1988). Modulation of acetylcholine receptor desensitization by forskolin is independent of cAMP. Science 240:1655-1657.
    • (1988) Science , vol.240 , pp. 1655-1657
    • Wagoner, P.K.1    Pallotta, B.S.2
  • 34
    • 0026625673 scopus 로고
    • Agonist-induced changes in the structure of the acetylcholine receptor M2 regions revealed by photoincorporation of an uncharged nicotinic noncompetitive antagonist
    • White, B. H., and Cohen, J. B. (1992). Agonist-induced changes in the structure of the acetylcholine receptor M2 regions revealed by photoincorporation of an uncharged nicotinic noncompetitive antagonist. J. Biol. Chem. 267:15770-15783.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15770-15783
    • White, B.H.1    Cohen, J.B.2
  • 35
    • 0023708347 scopus 로고
    • Forskolin alters acetylcholine receptor gating by a mechanism independent of adenylate cyclase activation
    • White, M. M. (1988). Forskolin alters acetylcholine receptor gating by a mechanism independent of adenylate cyclase activation. Mol. Pharmacol. 34:427-430.
    • (1988) Mol. Pharmacol. , vol.34 , pp. 427-430
    • White, M.M.1
  • 36
    • 0025845349 scopus 로고
    • Short chain and long chain alkanols have different sites of action on nicotinic acetylcholine receptor channels from Torpedo
    • Wood, S. C., Forman, S. A., and Miller, K. W. (1991). Short chain and long chain alkanols have different sites of action on nicotinic acetylcholine receptor channels from Torpedo. Mol. Pharmacol. 39:332-338.
    • (1991) Mol. Pharmacol. , vol.39 , pp. 332-338
    • Wood, S.C.1    Forman, S.A.2    Miller, K.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.