메뉴 건너뛰기




Volumn 12, Issue 8, 2009, Pages 988-995

A discrete alcohol pocket involved in GIRK channel activation

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL; G PROTEIN COUPLED INWARDLY RECTIFYING POTASSIUM CHANNEL; INWARDLY RECTIFYING POTASSIUM CHANNEL;

EID: 68149164775     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/nn.2358     Document Type: Article
Times cited : (130)

References (49)
  • 1
    • 1842328604 scopus 로고    scopus 로고
    • Aand glycine receptors. Nature 389, 385-389 (1997).
    • Aand glycine receptors. Nature 389, 385-389 (1997).
  • 2
    • 0024535962 scopus 로고
    • Ethanol inhibits NMDA-activated ion current in hippocampal neurons
    • Lovinger, D.M., White, G. & Weight, F.F. Ethanol inhibits NMDA-activated ion current in hippocampal neurons. Science 243, 1721-1724 (1989).
    • (1989) Science , vol.243 , pp. 1721-1724
    • Lovinger, D.M.1    White, G.2    Weight, F.F.3
  • 3
    • 0032901484 scopus 로고    scopus 로고
    • Effects of ethanol on recombinant human neuronal nicotinic acetylcholine receptors expressed in Xenopus oocytes
    • Cardoso, R.A. et al. Effects of ethanol on recombinant human neuronal nicotinic acetylcholine receptors expressed in Xenopus oocytes. J. Pharmacol. Exp. Ther. 289, 774-780 (1999).
    • (1999) J. Pharmacol. Exp. Ther , vol.289 , pp. 774-780
    • Cardoso, R.A.1
  • 4
    • 0030426270 scopus 로고    scopus 로고
    • Pharmacologic characteristics of potentiation of 5-HT3 receptors by alcohols and diethyl ether in NCB-20 neuroblastoma cells
    • Zhou, Q. & Lovinger, D.M. Pharmacologic characteristics of potentiation of 5-HT3 receptors by alcohols and diethyl ether in NCB-20 neuroblastoma cells. J. Pharmacol. Exp. Ther. 278, 732-740 (1996).
    • (1996) J. Pharmacol. Exp. Ther , vol.278 , pp. 732-740
    • Zhou, Q.1    Lovinger, D.M.2
  • 6
    • 0032568547 scopus 로고    scopus 로고
    • Mutations of gamma-aminobutyric acid and glycine receptors change alcohol cutoff: Evidence for an alcohol receptor?
    • Wick, M.J. et al. Mutations of gamma-aminobutyric acid and glycine receptors change alcohol cutoff: evidence for an alcohol receptor? Proc. Natl. Acad. Sci. USA 95, 6504-6509 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6504-6509
    • Wick, M.J.1
  • 7
    • 0033490206 scopus 로고    scopus 로고
    • G protein-coupled inwardly rectifying potassium channels are targets of alcohol action
    • Lewohl, J.M. et al. G protein-coupled inwardly rectifying potassium channels are targets of alcohol action. Nat. Neurosci. 2, 1084-1090 (1999).
    • (1999) Nat. Neurosci , vol.2 , pp. 1084-1090
    • Lewohl, J.M.1
  • 9
    • 0029112894 scopus 로고
    • Alcohols inhibit a cloned potassium channel at a discrete saturable site. Insights into the molecular basis of general anesthesia
    • Covarrubias, M., Vyas, T.B., Escobar, L. & Wei, A. Alcohols inhibit a cloned potassium channel at a discrete saturable site. Insights into the molecular basis of general anesthesia. J. Biol. Chem. 270, 19408-19416 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 19408-19416
    • Covarrubias, M.1    Vyas, T.B.2    Escobar, L.3    Wei, A.4
  • 11
    • 0034920540 scopus 로고    scopus 로고
    • Potassium channels as targets for ethanol: Studies of G protein-coupled inwardly rectifying potassium channel 2 (GIRK2) null mutant mice
    • Blednov, Y.A., Stoffel, M., Chang, S.R. & Harris, R.A. Potassium channels as targets for ethanol: studies of G protein-coupled inwardly rectifying potassium channel 2 (GIRK2) null mutant mice. J. Pharmacol. Exp. Ther. 298, 521-530 (2001).
    • (2001) J. Pharmacol. Exp. Ther , vol.298 , pp. 521-530
    • Blednov, Y.A.1    Stoffel, M.2    Chang, S.R.3    Harris, R.A.4
  • 12
    • 0028322077 scopus 로고
    • Activation of the cloned muscarinic potassium channel by G protein βγ-subunits
    • Reuveny, E. et al. Activation of the cloned muscarinic potassium channel by G protein βγ-subunits. Nature 370, 143-146 (1994).
    • (1994) Nature , vol.370 , pp. 143-146
    • Reuveny, E.1
  • 13
    • 0028180952 scopus 로고
    • Recombinant G protein βγ-subunits activate the muscarinic-gated atrial potassium channel
    • Wickman, K.D. et al. Recombinant G protein βγ-subunits activate the muscarinic-gated atrial potassium channel. Nature 368, 255-257 (1994).
    • (1994) Nature , vol.368 , pp. 255-257
    • Wickman, K.D.1
  • 15
    • 0028826886 scopus 로고
    • Identification of domains conferring G protein regulation on inward rectifier potassium channels
    • Kunkel, M.T. & Peralta, E.G. Identification of domains conferring G protein regulation on inward rectifier potassium channels. Cell 83, 443-449 (1995).
    • (1995) Cell , vol.83 , pp. 443-449
    • Kunkel, M.T.1    Peralta, E.G.2
  • 16
    • 0032479052 scopus 로고    scopus 로고
    • + channel activation. J. Biol. Chem. 273, 16946-16952 (1998).
    • + channel activation. J. Biol. Chem. 273, 16946-16952 (1998).
  • 17
    • 0033617167 scopus 로고    scopus 로고
    • Identification of a potassium channel site that interacts with G protein βγ subunits to mediate agonist-induced signaling
    • He, C., Zhang, H., Mirshahi, T. & Logothetis, D.E. Identification of a potassium channel site that interacts with G protein βγ subunits to mediate agonist-induced signaling. J. Biol. Chem. 274, 12517-12524 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 12517-12524
    • He, C.1    Zhang, H.2    Mirshahi, T.3    Logothetis, D.E.4
  • 18
    • 0043237432 scopus 로고    scopus 로고
    • + channel
    • + channel. J. Biol. Chem. 278, 29174-29183 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 29174-29183
    • Ivanina, T.1
  • 20
    • 0034893726 scopus 로고    scopus 로고
    • Mutational analysis of ethanol interactions with G protein-coupled inwardly rectifying potassium channels
    • Hara, K., Lewohl, J.M., Yamakura, T. & Harris, R.A. Mutational analysis of ethanol interactions with G protein-coupled inwardly rectifying potassium channels. Alcohol 24, 5-8 (2001).
    • (2001) Alcohol , vol.24 , pp. 5-8
    • Hara, K.1    Lewohl, J.M.2    Yamakura, T.3    Harris, R.A.4
  • 21
    • 33746047139 scopus 로고    scopus 로고
    • Andersen's syndrome mutation effects on the structure and assembly of the cytoplasmic domains of Kir2.1
    • Pegan, S., Arrabit, C., Slesinger, P.A. & Choe, S. Andersen's syndrome mutation effects on the structure and assembly of the cytoplasmic domains of Kir2.1. Biochemistry 45, 8599-8606 (2006).
    • (2006) Biochemistry , vol.45 , pp. 8599-8606
    • Pegan, S.1    Arrabit, C.2    Slesinger, P.A.3    Choe, S.4
  • 22
    • 0041819527 scopus 로고    scopus 로고
    • Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster
    • Kruse, S.W., Zhao, R., Smith, D.P. & Jones, D.N. Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster. Nat. Struct. Biol. 10, 694-700 (2003).
    • (2003) Nat. Struct. Biol , vol.10 , pp. 694-700
    • Kruse, S.W.1    Zhao, R.2    Smith, D.P.3    Jones, D.N.4
  • 23
    • 0037184996 scopus 로고    scopus 로고
    • Structural basis of inward rectification: Cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 Å resolution
    • Nishida, M. & MacKinnon, R. Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 Å resolution. Cell 111, 957-965 (2002).
    • (2002) Cell , vol.111 , pp. 957-965
    • Nishida, M.1    MacKinnon, R.2
  • 24
    • 14544298750 scopus 로고    scopus 로고
    • Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification
    • Pegan, S. et al. Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification. Nat. Neurosci. 8, 279-287 (2005).
    • (2005) Nat. Neurosci , vol.8 , pp. 279-287
    • Pegan, S.1
  • 27
    • 0031436257 scopus 로고    scopus 로고
    • Probing the G-protein regulation of GIRK1 and GIRK4, the two subunits of the KACh channel, using functional homomeric mutants
    • Vivaudou, M. et al. Probing the G-protein regulation of GIRK1 and GIRK4, the two subunits of the KACh channel, using functional homomeric mutants. J. Biol. Chem. 272, 31553-31560 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 31553-31560
    • Vivaudou, M.1
  • 28
    • 0033161908 scopus 로고    scopus 로고
    • + channels by distinct PtdIns(4,5)P2 interactions. Nat. Cell Biol. 1, 183-188 (1999).
    • + channels by distinct PtdIns(4,5)P2 interactions. Nat. Cell Biol. 1, 183-188 (1999).
  • 31
    • 0032546013 scopus 로고    scopus 로고
    • 2and its stabilization by G βγ. Nature 391, 803-806 (1998).
    • 2and its stabilization by G βγ. Nature 391, 803-806 (1998).
  • 32
    • 0036143966 scopus 로고    scopus 로고
    • Inhibition of N-methyl-d-aspartate receptors by straight-chain diols: Implications for the mechanism of the alcohol cutoff effect
    • Peoples, R.W. & Ren, H. Inhibition of N-methyl-d-aspartate receptors by straight-chain diols: implications for the mechanism of the alcohol cutoff effect. Mol. Pharmacol. 61, 169-176 (2002).
    • (2002) Mol. Pharmacol , vol.61 , pp. 169-176
    • Peoples, R.W.1    Ren, H.2
  • 33
    • 0029874974 scopus 로고    scopus 로고
    • Aand glutamate receptors: relation to in vivo effects. Br. J. Pharmacol. 118, 378-384 (1996).
    • Aand glutamate receptors: relation to in vivo effects. Br. J. Pharmacol. 118, 378-384 (1996).
  • 34
    • 0028300618 scopus 로고
    • Structures of horse liver alcohol dehydrogenase complexed with NAD+ and substituted benzyl alcohols
    • Ramaswamy, S., Eklund, H. & Plapp, B.V. Structures of horse liver alcohol dehydrogenase complexed with NAD+ and substituted benzyl alcohols. Biochemistry 33, 5230-5237 (1994).
    • (1994) Biochemistry , vol.33 , pp. 5230-5237
    • Ramaswamy, S.1    Eklund, H.2    Plapp, B.V.3
  • 35
    • 0034665877 scopus 로고    scopus 로고
    • Crystal structures of mouse class II alcohol dehydrogenase reveal determinants of substrate specificity and catalytic efficiency
    • Svensson, S., Hoog, J.O., Schneider, G. & Sandalova, T. Crystal structures of mouse class II alcohol dehydrogenase reveal determinants of substrate specificity and catalytic efficiency. J. Mol. Biol. 302, 441-453 (2000).
    • (2000) J. Mol. Biol , vol.302 , pp. 441-453
    • Svensson, S.1    Hoog, J.O.2    Schneider, G.3    Sandalova, T.4
  • 36
    • 0028978520 scopus 로고
    • Engineering yeast alcohol dehydrogenase. Replacing Trp54 by Leu broadens substrate specificity
    • Weinhold, E.G. & Benner, S.A. Engineering yeast alcohol dehydrogenase. Replacing Trp54 by Leu broadens substrate specificity. Protein Eng. 8, 457-461 (1995).
    • (1995) Protein Eng , vol.8 , pp. 457-461
    • Weinhold, E.G.1    Benner, S.A.2
  • 37
    • 39149094255 scopus 로고    scopus 로고
    • The role of multiple hydrogen-bonding groups in specific alcohol binding sites in proteins: Insights from structural studies of LUSH
    • Thode, A.B., Kruse, S.W., Nix, J.C. & Jones, D.N. The role of multiple hydrogen-bonding groups in specific alcohol binding sites in proteins: insights from structural studies of LUSH. J. Mol. Biol. 376, 1360-1376 (2008).
    • (2008) J. Mol. Biol , vol.376 , pp. 1360-1376
    • Thode, A.B.1    Kruse, S.W.2    Nix, J.C.3    Jones, D.N.4
  • 38
    • 0035119276 scopus 로고    scopus 로고
    • + channel with backbone mutations in the selectivity filter
    • + channel with backbone mutations in the selectivity filter. Nat. Neurosci. 4, 239-246 (2001).
    • (2001) Nat. Neurosci , vol.4 , pp. 239-246
    • Lu, T.1
  • 39
    • 34548386717 scopus 로고    scopus 로고
    • Crystal structure of a Kir3.1-prokaryotic Kir channel chimera
    • Nishida, M., Cadene, M., Chait, B.T. & MacKinnon, R. Crystal structure of a Kir3.1-prokaryotic Kir channel chimera. EMBO J. 26, 4005-4015 (2007).
    • (2007) EMBO J , vol.26 , pp. 4005-4015
    • Nishida, M.1    Cadene, M.2    Chait, B.T.3    MacKinnon, R.4
  • 40
    • 0035049090 scopus 로고    scopus 로고
    • Yeast screen for constitutively active mutant G protein-activated potassium channels
    • Yi, B.A., Lin, Y.F., Jan, Y.N. & Jan, L.Y. Yeast screen for constitutively active mutant G protein-activated potassium channels. Neuron 29, 657-667 (2001).
    • (2001) Neuron , vol.29 , pp. 657-667
    • Yi, B.A.1    Lin, Y.F.2    Jan, Y.N.3    Jan, L.Y.4
  • 41
    • 0034744617 scopus 로고    scopus 로고
    • Coupling G βγ-dependent activation to channel opening via pore elements in inwardly rectifying potassium channels
    • Sadja, R., Smadja, K., Alagem, N. & Reuveny, E. Coupling G βγ-dependent activation to channel opening via pore elements in inwardly rectifying potassium channels. Neuron 29, 669-680 (2001).
    • (2001) Neuron , vol.29 , pp. 669-680
    • Sadja, R.1    Smadja, K.2    Alagem, N.3    Reuveny, E.4
  • 42
    • 0036753545 scopus 로고    scopus 로고
    • + channel by pivoted bending of a transmembrane segment
    • + channel by pivoted bending of a transmembrane segment. Mol. Cell 10, 469-481 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 469-481
    • Jin, T.1
  • 43
    • 14044277646 scopus 로고    scopus 로고
    • Mutation of critical GIRK subunit residues disrupts N- and C-termini association and channel function
    • Sarac, R. et al. Mutation of critical GIRK subunit residues disrupts N- and C-termini association and channel function. J. Neurosci. 25, 1836-1846 (2005).
    • (2005) J. Neurosci , vol.25 , pp. 1836-1846
    • Sarac, R.1
  • 44
    • 0038664388 scopus 로고    scopus 로고
    • Conformational rearrangements associated with the gating of the G protein-coupled potassium channel revealed by FRET microscopy
    • Riven, I., Kalmanzon, E., Segev, L. & Reuveny, E. Conformational rearrangements associated with the gating of the G protein-coupled potassium channel revealed by FRET microscopy. Neuron 38, 225-235 (2003).
    • (2003) Neuron , vol.38 , pp. 225-235
    • Riven, I.1    Kalmanzon, E.2    Segev, L.3    Reuveny, E.4
  • 45
    • 0032557490 scopus 로고    scopus 로고
    • Molecular basis for interactions of G protein βγ subunits with effectors
    • Ford, C.E. et al. Molecular basis for interactions of G protein βγ subunits with effectors. Science 280, 1271-1274 (1998).
    • (1998) Science , vol.280 , pp. 1271-1274
    • Ford, C.E.1
  • 46
    • 13444254031 scopus 로고    scopus 로고
    • Pertussis toxin-sensitive Galpha subunits selectively bind to C-terminal domain of neuronal GIRK channels: Evidence for a heterotrimeric G protein-channel complex
    • Clancy, S.M. et al. Pertussis toxin-sensitive Galpha subunits selectively bind to C-terminal domain of neuronal GIRK channels: evidence for a heterotrimeric G protein-channel complex. Mol. Cell. Neurosci. 28, 375-389 (2005).
    • (2005) Mol. Cell. Neurosci , vol.28 , pp. 375-389
    • Clancy, S.M.1
  • 47
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K. & Pease, L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59 (1989).
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 48
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Dundas, J. et al. CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res. 34, W116-118 (2006).
    • (2006) Nucleic Acids Res , vol.34
    • Dundas, J.1
  • 49
    • 0028773889 scopus 로고
    • Volume changes on protein folding
    • Harpaz, Y., Gerstein, M. & Chothia, C. Volume changes on protein folding. Structure 2, 641-649 (1994).
    • (1994) Structure , vol.2 , pp. 641-649
    • Harpaz, Y.1    Gerstein, M.2    Chothia, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.