메뉴 건너뛰기




Volumn 10, Issue 3, 2002, Pages 469-481

The βγ subunits of G proteins gate a K+ channel by pivoted bending of a transmembrane segment

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GLYCINE; GUANINE NUCLEOTIDE BINDING PROTEIN; MUTANT PROTEIN; POTASSIUM CHANNEL; PROLINE; TETRAMER;

EID: 0036753545     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(02)00659-7     Document Type: Article
Times cited : (114)

References (59)
  • 2
    • 0033957834 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000
    • Bairoch A., Apweiler R. The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000. Nucleic Acids Res. 28:2000;45-48.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 45-48
    • Bairoch, A.1    Apweiler, R.2
  • 4
    • 0034123344 scopus 로고    scopus 로고
    • Homology modeling and molecular dynamics simulation studies of an inward rectifier potassium channel
    • Capener C.E., Shrivastava I.H., Ranatunga K.M., Forrest L.R., Smith G.R., Sansom M.S. Homology modeling and molecular dynamics simulation studies of an inward rectifier potassium channel. Biophys. J. 78:2000;2929-2942.
    • (2000) Biophys. J. , vol.78 , pp. 2929-2942
    • Capener, C.E.1    Shrivastava, I.H.2    Ranatunga, K.M.3    Forrest, L.R.4    Smith, G.R.5    Sansom, M.S.6
  • 8
    • 4243961394 scopus 로고    scopus 로고
    • Fast gating transitions determined by dynamic rearrangements in the selectivity filter of KcsA
    • Cuello L.G., Perozo E. Fast gating transitions determined by dynamic rearrangements in the selectivity filter of KcsA. Biophys. J. 82:2002;174a-175a.
    • (2002) Biophys. J. , vol.82
    • Cuello, L.G.1    Perozo, E.2
  • 12
    • 3042695848 scopus 로고    scopus 로고
    • A family of putative Kir potassium channels in prokaryotes
    • Durell S.R., Guy H.R. A family of putative Kir potassium channels in prokaryotes. BMC. Evol. Biol. 1:2001;14.
    • (2001) BMC. Evol. Biol. , vol.1 , pp. 14
    • Durell, S.R.1    Guy, H.R.2
  • 14
    • 0034977038 scopus 로고    scopus 로고
    • Conformational changes in S6 coupled to the opening of cyclic nucleotide-gated channels
    • Flynn G.E., Zagotta W.N. Conformational changes in S6 coupled to the opening of cyclic nucleotide-gated channels. Neuron. 30:2001;689-698.
    • (2001) Neuron , vol.30 , pp. 689-698
    • Flynn, G.E.1    Zagotta, W.N.2
  • 15
    • 0033617167 scopus 로고    scopus 로고
    • Identification of a potassium channel site that interacts with a 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 a G protein βγ subunits to mediate agonist-induced signaling. J. Biol. Chem. 274:1999;12517-12524.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12517-12524
    • He, C.1    Zhang, H.2    Mirshahi, T.3    Logothetis, D.E.4
  • 17
    • 0025783632 scopus 로고
    • Estimating the number of channels in patch recordings
    • Horn R. Estimating the number of channels in patch recordings. Biophys. J. 60:1991;433-439.
    • (1991) Biophys. J. , vol.60 , pp. 433-439
    • Horn, R.1
  • 21
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang Y., Lee A., Chen J., Cadene M., Chait B.T., MacKinnon R. Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 417:2002;515-522. a.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 27
    • 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. 83:1995;443-449.
    • (1995) Cell , vol.83 , pp. 443-449
    • Kunkel, M.T.1    Peralta, E.G.2
  • 28
    • 0030795112 scopus 로고    scopus 로고
    • Gated access to the pore of a voltage-dependent K+ channel
    • Liu Y., Holmgren M., Jurman M.E., Yellen G. Gated access to the pore of a voltage-dependent K+ channel. Neuron. 19:1997;175-184.
    • (1997) Neuron , vol.19 , pp. 175-184
    • Liu, Y.1    Holmgren, M.2    Jurman, M.E.3    Yellen, G.4
  • 29
    • 0034817286 scopus 로고    scopus 로고
    • Structure of the KcsA channel intracellular gate in the open state
    • Liu Y.S., Sompornpisut P., Perozo E. Structure of the KcsA channel intracellular gate in the open state. Nat. Struct. Biol. 8:2001;883-887.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 883-887
    • Liu, Y.S.1    Sompornpisut, P.2    Perozo, E.3
  • 32
    • 0037071897 scopus 로고    scopus 로고
    • Alterations in conserved Kir channel-PIP2 interactions underlie channelopathies
    • Lopes C.M., Zhang H., Rohacs T., Jin T., Yang J., Logothetis D.E. Alterations in conserved Kir channel-PIP2 interactions underlie channelopathies. Neuron. 34:2002;933-944.
    • (2002) Neuron , vol.34 , pp. 933-944
    • Lopes, C.M.1    Zhang, H.2    Rohacs, T.3    Jin, T.4    Yang, J.5    Logothetis, D.E.6
  • 34
    • 0035950089 scopus 로고    scopus 로고
    • Ion conduction pore is conserved among potassium channels
    • Lu Z., Klem A.M., Ramu Y. Ion conduction pore is conserved among potassium channels. Nature. 413:2001;809-813. a.
    • (2001) Nature , vol.413 , pp. 809-813
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 35
    • 0035119276 scopus 로고    scopus 로고
    • Probing ion permeation and gating in a K+ channel with backbone mutations in the selectivity filter
    • Lu T., Ting A.Y., Mainland J., Jan L.Y., Schultz P.G., Yang J. Probing ion permeation and gating in a K+ channel with backbone mutations in the selectivity filter. Nat. Neurosci. 4:2001;239-246. b.
    • (2001) Nat. Neurosci. , vol.4 , pp. 239-246
    • Lu, T.1    Ting, A.Y.2    Mainland, J.3    Jan, L.Y.4    Schultz, P.G.5    Yang, J.6
  • 36
    • 0032478696 scopus 로고    scopus 로고
    • Structural conservation in prokaryotic and eukaryotic potassium channels
    • MacKinnon R., Cohen S.L., Kuo A., Lee A., Chait B.T. Structural conservation in prokaryotic and eukaryotic potassium channels. Science. 280:1998;106-109.
    • (1998) Science , vol.280 , pp. 106-109
    • MacKinnon, R.1    Cohen, S.L.2    Kuo, A.3    Lee, A.4    Chait, B.T.5
  • 37
    • 0033582936 scopus 로고    scopus 로고
    • Transmembrane structure of an inwardly rectifying potassium channel
    • Minor D.L.J., Masseling S.J., Jan Y.N., Jan L.Y. Transmembrane structure of an inwardly rectifying potassium channel. Cell. 96:1999;879-891.
    • (1999) Cell , vol.96 , pp. 879-891
    • Minor, D.L.J.1    Masseling, S.J.2    Jan, Y.N.3    Jan, L.Y.4
  • 38
    • 0011121286 scopus 로고    scopus 로고
    • Localization and quantification of GFP-tagged ion channels expressed in Xenopus oocytes
    • A.N. Lopatin, & C.G. Nichols. Totowa, NJ: Humana Press
    • Mirshahi T., Logothetis D.E., Sassaroli M. Localization and quantification of GFP-tagged ion channels expressed in Xenopus oocytes. Lopatin A.N., Nichols C.G. Ion Channel Localization. 2001;Humana Press, Totowa, NJ. 215-231.pp.
    • (2001) Ion Channel Localization , pp. 215-231
    • Mirshahi, T.1    Logothetis, D.E.2    Sassaroli, M.3
  • 40
    • 4243815854 scopus 로고    scopus 로고
    • Cold draft through the teepee: MTSEA access to the inner vestibule of ATP closed KIR6.2 channels implies gating does not occur at the smokehole
    • Phillips L.R., Loussouarn G., Nichols C.G. Cold draft through the teepee. MTSEA access to the inner vestibule of ATP closed KIR6.2 channels implies gating does not occur at the smokehole Biophys. J. 82:2002;590a.
    • (2002) Biophys. J. , vol.82
    • Phillips, L.R.1    Loussouarn, G.2    Nichols, C.G.3
  • 43
    • 0033063884 scopus 로고    scopus 로고
    • The role of a conserved proline residue in mediating conformational changes associated with voltage gating of Cx32 gap junctions
    • Ri Y., Ballesteros J., Abrams C., Oh S., Verselis V., Weinstein H., Bargiello The role of a conserved proline residue in mediating conformational changes associated with voltage gating of Cx32 gap junctions. Biophys. J. 76(6):1999;2887-2898.
    • (1999) Biophys. J. , vol.76 , Issue.6 , pp. 2887-2898
    • Ri, Y.1    Ballesteros, J.2    Abrams, C.3    Oh, S.4    Verselis, V.5    Weinstein, H.6    Bargiello7
  • 45
    • 0034744617 scopus 로고    scopus 로고
    • Coupling Gβγ-dependent activation to channel opening via pore elements in inwardly rectifying potassium channels
    • Sadja R., Smadja K., Alagem N., Reuveny E. Coupling Gβγ-dependent activation to channel opening via pore elements in inwardly rectifying potassium channels. Neuron. 29:2001;669-680.
    • (2001) Neuron , vol.29 , pp. 669-680
    • Sadja, R.1    Smadja, K.2    Alagem, N.3    Reuveny, E.4
  • 46
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 48
    • 0034327611 scopus 로고    scopus 로고
    • Hinges, swivels and switches: The role of prolines in signalling via transmembrane alpha-helices
    • Sansom M.S., Weinstein H. Hinges, swivels and switches. the role of prolines in signalling via transmembrane alpha-helices Trends Pharmacol. Sci. 21:2000;445-451.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 445-451
    • Sansom, M.S.1    Weinstein, H.2
  • 49
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider T.D., Stephens R.M. Sequence logos. a new way to display consensus sequences Nucleic Acids Res. 18:1990;6097-6100.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 52
    • 0027968068 scopus 로고
    • Clustal w: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. Clustal w. improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 54
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley W.C., White S.H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:1996;842-848.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 55
    • 0030005250 scopus 로고    scopus 로고
    • Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides
    • Wimley W.C., Creamer T.P., White S.H. Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides. Biochemistry. 35:1996;5109-5124.
    • (1996) Biochemistry , vol.35 , pp. 5109-5124
    • Wimley, W.C.1    Creamer, T.P.2    White, S.H.3
  • 56
    • 0003341858 scopus 로고    scopus 로고
    • Where is the activation gate for PIP2 gating of Kir2.1 channels?
    • Xiao J., Yang J. Where is the activation gate for PIP2 gating of Kir2.1 channels? Biophys. J. 82:2002;180a.
    • (2002) Biophys. J. , vol.82
    • Xiao, J.1    Yang, J.2
  • 57
    • 0029982561 scopus 로고    scopus 로고
    • A domain on the G protein β subunit interacts with both adenylyl cyclase 2 and the muscarinic atrial potassium channel
    • Yan K., Gautam N. A domain on the G protein β subunit interacts with both adenylyl cyclase 2 and the muscarinic atrial potassium channel. J. Biol. Chem. 271:1996;17597-17600.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17597-17600
    • Yan, K.1    Gautam, N.2
  • 58
    • 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. 29:2001;657-667.
    • (2001) Neuron , vol.29 , pp. 657-667
    • Yi, B.A.1    Lin, Y.F.2    Jan, Y.N.3    Jan, L.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.