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Volumn 407, Issue 2, 2011, Pages 366-371

Inverse agonist-like action of cadmium on G-protein-gated inward-rectifier K+ channels

Author keywords

Allosteric regulation; Crystallography; Electrophysiology; G protein; Inward rectifier K+ channel

Indexed keywords

CADMIUM; CYSTEINE; G PROTEIN COUPLED INWARDLY RECTIFYING POTASSIUM CHANNEL;

EID: 79953697068     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.03.025     Document Type: Article
Times cited : (12)

References (35)
  • 1
    • 0242657337 scopus 로고    scopus 로고
    • Potassium channels
    • MacKinnon R. Potassium channels. FEBS Lett. 2003, 555:62-65.
    • (2003) FEBS Lett. , vol.555 , pp. 62-65
    • MacKinnon, R.1
  • 2
    • 74949143771 scopus 로고    scopus 로고
    • Inwardly rectifying potassium channels: their structure, function, and physiological roles
    • Hibino H., Inanobe A., Furutani K., Murakami S., Findlay I., Kurachi Y. Inwardly rectifying potassium channels: their structure, function, and physiological roles. Physiol. Rev. 2010, 90:291-366.
    • (2010) Physiol. Rev. , vol.90 , pp. 291-366
    • Hibino, H.1    Inanobe, A.2    Furutani, K.3    Murakami, S.4    Findlay, I.5    Kurachi, Y.6
  • 3
    • 79953729405 scopus 로고    scopus 로고
    • Inward rectifying K+ channels
    • Aschcroft F.M. Inward rectifying K+ channels. Ion Channels Dis. 2000, 135-159.
    • (2000) Ion Channels Dis. , pp. 135-159
    • Aschcroft, F.M.1
  • 4
    • 0037184996 scopus 로고    scopus 로고
    • Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8Å resolution
    • Nishida M., MacKinnon R. Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8Å resolution. Cell 2002, 111:957-965.
    • (2002) Cell , vol.111 , pp. 957-965
    • Nishida, M.1    MacKinnon, R.2
  • 6
    • 0344861820 scopus 로고    scopus 로고
    • Merging functional studies with structures of inward-rectifier K+ channels
    • Bichet D., Haass F.A., Jan L.Y. Merging functional studies with structures of inward-rectifier K+ channels. Nat. Rev. Neurosci. 2003, 4:957-967.
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 957-967
    • Bichet, D.1    Haass, F.A.2    Jan, L.Y.3
  • 7
    • 34547129073 scopus 로고    scopus 로고
    • Diverse Kir modulators act in close proximity to residues implicated in phosphoinositide binding
    • Logothetis D.E., Lupyan D., Rosenhouse-Dantsker A. Diverse Kir modulators act in close proximity to residues implicated in phosphoinositide binding. J. Physiol. 2007, 582:953-965.
    • (2007) J. Physiol. , vol.582 , pp. 953-965
    • Logothetis, D.E.1    Lupyan, D.2    Rosenhouse-Dantsker, A.3
  • 8
    • 26444584556 scopus 로고    scopus 로고
    • Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography
    • Kuo A., Domene C., Johnson L.N., Doyle D.A., Venien-Bryan C. Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography. Structure 2005, 13:1463-1472.
    • (2005) Structure , vol.13 , pp. 1463-1472
    • Kuo, A.1    Domene, C.2    Johnson, L.N.3    Doyle, D.A.4    Venien-Bryan, C.5
  • 9
    • 35548982646 scopus 로고    scopus 로고
    • Direct visualization of KirBac3.1 potassium channel gating by atomic force microscopy
    • Jaroslawski S., Zadek B., Ashcroft F., Venien-Bryan C., Scheuring S. Direct visualization of KirBac3.1 potassium channel gating by atomic force microscopy. J. Mol. Biol. 2007, 374:500-505.
    • (2007) J. Mol. Biol. , vol.374 , pp. 500-505
    • Jaroslawski, S.1    Zadek, B.2    Ashcroft, F.3    Venien-Bryan, C.4    Scheuring, S.5
  • 10
    • 77953714921 scopus 로고    scopus 로고
    • Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels
    • Clarke O.B., Caputo A.T., Hill A.P., Vandenberg J.I., Smith B.J., Gulbis J.M. Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels. Cell 2010, 141:1018-1029.
    • (2010) Cell , vol.141 , pp. 1018-1029
    • Clarke, O.B.1    Caputo, A.T.2    Hill, A.P.3    Vandenberg, J.I.4    Smith, B.J.5    Gulbis, J.M.6
  • 11
    • 78649641632 scopus 로고    scopus 로고
    • A structural determinant for the control of PIP2 sensitivity in G protein-gated inward rectifier K+ channels
    • Inanobe A., Nakagawa A., Matsuura T., Kurachi Y. A structural determinant for the control of PIP2 sensitivity in G protein-gated inward rectifier K+ channels. J. Biol. Chem. 2010, 285:38517-38523.
    • (2010) J. Biol. Chem. , vol.285 , pp. 38517-38523
    • Inanobe, A.1    Nakagawa, A.2    Matsuura, T.3    Kurachi, Y.4
  • 12
    • 78751530099 scopus 로고    scopus 로고
    • NMR analyses of the Gbetagamma binding and conformational rearrangements of the cytoplasmic pore of G protein-activated inwardly rectifying potassium channel 1 (GIRK1)
    • Yokogawa M., Osawa M., Takeuchi K., Mase Y., Shimada I. NMR analyses of the Gbetagamma binding and conformational rearrangements of the cytoplasmic pore of G protein-activated inwardly rectifying potassium channel 1 (GIRK1). J. Biol. Chem. 2011, 286:2215-2223.
    • (2011) J. Biol. Chem. , vol.286 , pp. 2215-2223
    • Yokogawa, M.1    Osawa, M.2    Takeuchi, K.3    Mase, Y.4    Shimada, I.5
  • 13
    • 0033571493 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel splicing variant of the Kir3.2 subunit predominantly expressed in mouse testis
    • Inanobe A., Horio Y., Fujita A., Tanemoto M., Hibino H., Inageda K., Kurachi Y. Molecular cloning and characterization of a novel splicing variant of the Kir3.2 subunit predominantly expressed in mouse testis. J. Physiol. 1999, 521:19-30.
    • (1999) J. Physiol. , vol.521 , pp. 19-30
    • Inanobe, A.1    Horio, Y.2    Fujita, A.3    Tanemoto, M.4    Hibino, H.5    Inageda, K.6    Kurachi, Y.7
  • 14
    • 0001664516 scopus 로고    scopus 로고
    • Na+ activation of the muscarinic K+ channel by a G-protein-independent mechanism
    • Sui J.L., Chan K.W., Logothetis D.E. Na+ activation of the muscarinic K+ channel by a G-protein-independent mechanism. J. Gen. Physiol. 1996, 108:381-391.
    • (1996) J. Gen. Physiol. , vol.108 , pp. 381-391
    • Sui, J.L.1    Chan, K.W.2    Logothetis, D.E.3
  • 15
    • 0032546013 scopus 로고    scopus 로고
    • Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gβγ
    • Huang C.L., Feng S., Hilgemann D.W. Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gβγ. Nature 1998, 391:803-806.
    • (1998) Nature , vol.391 , pp. 803-806
    • Huang, C.L.1    Feng, S.2    Hilgemann, D.W.3
  • 16
    • 0018464246 scopus 로고
    • Calculation of the concentrations of free cations and cation-ligand complexes in solutions containing multiple divalent cations and ligands
    • Goldstein D.A. Calculation of the concentrations of free cations and cation-ligand complexes in solutions containing multiple divalent cations and ligands. Biophys. J. 1979, 26:235-242.
    • (1979) Biophys. J. , vol.26 , pp. 235-242
    • Goldstein, D.A.1
  • 17
    • 34547130933 scopus 로고    scopus 로고
    • Structural diversity in the cytoplasmic region of G protein-gated inward rectifier K+ channels
    • Inanobe A., Matsuura T., Nakagawa A., Kurachi Y. Structural diversity in the cytoplasmic region of G protein-gated inward rectifier K+ channels. Channels 2007, 1:39-45.
    • (2007) Channels , vol.1 , pp. 39-45
    • Inanobe, A.1    Matsuura, T.2    Nakagawa, A.3    Kurachi, Y.4
  • 18
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 19
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • N.Collaborative Computational Project
    • N.Collaborative Computational Project The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 1994, 50:760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 21
    • 0033230296 scopus 로고    scopus 로고
    • Molecular mechanism for sodium-dependent activation of G protein-gated K+ channels
    • Ho I.H., Murrell-Lagnado R.D. Molecular mechanism for sodium-dependent activation of G protein-gated K+ channels. J. Physiol. 1999, 520(Pt 3):645-651.
    • (1999) J. Physiol. , vol.520 , Issue.PART 3 , pp. 645-651
    • Ho, I.H.1    Murrell-Lagnado, R.D.2
  • 22
    • 14544298750 scopus 로고    scopus 로고
    • Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification
    • Pegan S., Arrabit C., Zhou W., Kwiatkowski W., Collins A., Slesinger P.A., Choe S. Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification. Nat. Neurosci. 2005, 8:279-287.
    • (2005) Nat. Neurosci. , vol.8 , pp. 279-287
    • Pegan, S.1    Arrabit, C.2    Zhou, W.3    Kwiatkowski, W.4    Collins, A.5    Slesinger, P.A.6    Choe, S.7
  • 23
    • 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. 2007, 26:4005-4015.
    • (2007) EMBO J. , vol.26 , pp. 4005-4015
    • Nishida, M.1    Cadene, M.2    Chait, B.T.3    MacKinnon, R.4
  • 24
    • 77954635392 scopus 로고    scopus 로고
    • Conformational changes during the gating of a potassium channel revealed by structural mass spectrometry
    • Gupta S., Bavro V.N., D'Mello R., Tucker S.J., Venien-Bryan C., Chance M.R. Conformational changes during the gating of a potassium channel revealed by structural mass spectrometry. Structure 2010, 18:839-846.
    • (2010) Structure , vol.18 , pp. 839-846
    • Gupta, S.1    Bavro, V.N.2    D'Mello, R.3    Tucker, S.J.4    Venien-Bryan, C.5    Chance, M.R.6
  • 27
    • 0032545369 scopus 로고    scopus 로고
    • PH-dependent gating of ROMK (Kir1.1) channels involves conformational changes in both N and C termini
    • Schulte U., Hahn H., Wiesinger H., Ruppersberg J.P., Fakler B. PH-dependent gating of ROMK (Kir1.1) channels involves conformational changes in both N and C termini. J. Biol. Chem. 1998, 273:34575-34579.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34575-34579
    • Schulte, U.1    Hahn, H.2    Wiesinger, H.3    Ruppersberg, J.P.4    Fakler, B.5
  • 28
    • 0031707993 scopus 로고    scopus 로고
    • Mechanism of ATP-sensitive K channel inhibition by sulfhydryl modification
    • Trapp S., Tucker S.J., Ashcroft F.M. Mechanism of ATP-sensitive K channel inhibition by sulfhydryl modification. J. Gen. Physiol. 1998, 112:325-332.
    • (1998) J. Gen. Physiol. , vol.112 , pp. 325-332
    • Trapp, S.1    Tucker, S.J.2    Ashcroft, F.M.3
  • 29
    • 0033103166 scopus 로고    scopus 로고
    • Architecture of a K+ channel inner pore revealed by stoichiometric covalent modification
    • Lu T., Nguyen B., Zhang X., Yang J. Architecture of a K+ channel inner pore revealed by stoichiometric covalent modification. Neuron 1999, 22:571-580.
    • (1999) Neuron , vol.22 , pp. 571-580
    • Lu, T.1    Nguyen, B.2    Zhang, X.3    Yang, J.4
  • 30
    • 0033958664 scopus 로고    scopus 로고
    • Structure and dynamics of the pore of inwardly rectifying KATP channels
    • Loussouarn G., Makhina E.N., Rose T., Nichols C.G. Structure and dynamics of the pore of inwardly rectifying KATP channels. J. Biol. Chem. 2000, 275:1137-1144.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1137-1144
    • Loussouarn, G.1    Makhina, E.N.2    Rose, T.3    Nichols, C.G.4
  • 31
    • 0037073771 scopus 로고    scopus 로고
    • A role for the middle C terminus of G-protein-activated inward rectifier potassium channels in regulating gating
    • Guo Y., Waldron G.J., Murrell-Lagnado R. A role for the middle C terminus of G-protein-activated inward rectifier potassium channels in regulating gating. J. Biol. Chem. 2002, 277:48289-48294.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48289-48294
    • Guo, Y.1    Waldron, G.J.2    Murrell-Lagnado, R.3
  • 32
    • 0035929626 scopus 로고    scopus 로고
    • Redox-dependent gating of G protein-coupled inwardly rectifying K+ channels
    • Zeidner G., Sadja R., Reuveny E. Redox-dependent gating of G protein-coupled inwardly rectifying K+ channels. J. Biol. Chem. 2001, 276:35564-35570.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35564-35570
    • Zeidner, G.1    Sadja, R.2    Reuveny, E.3
  • 33
    • 0031593981 scopus 로고    scopus 로고
    • The diversity of GABAA receptors. Pharmacological and electrophysiological properties of GABAA channel subtypes
    • Hevers W., Luddens H. The diversity of GABAA receptors. Pharmacological and electrophysiological properties of GABAA channel subtypes. Mol. Neurobiol. 1998, 18:35-86.
    • (1998) Mol. Neurobiol. , vol.18 , pp. 35-86
    • Hevers, W.1    Luddens, H.2
  • 35
    • 3242784885 scopus 로고    scopus 로고
    • Mechanism of the nuclear receptor molecular switch
    • Nagy L., Schwabe J.W. Mechanism of the nuclear receptor molecular switch. Trends Biochem. Sci. 2004, 29:317-324.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 317-324
    • Nagy, L.1    Schwabe, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.