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Volumn 304, Issue 4, 2013, Pages

Interactions between hERG and KCNQ1 α-subunits are mediated by their COOH termini and modulated by cAMP

Author keywords

Arrhythmia; FRET; Potassium channel; Repolarization reserve

Indexed keywords

CYCLIC AMP; FORSKOLIN; GREEN FLUORESCENT PROTEIN; ISOBUTYLMETHYLXANTHINE; POTASSIUM CHANNEL HERG; POTASSIUM CHANNEL KCNQ1; PROTEIN VARIANT;

EID: 84874068662     PISSN: 03636135     EISSN: 15221539     Source Type: Journal    
DOI: 10.1152/ajpheart.00385.2012     Document Type: Article
Times cited : (22)

References (37)
  • 2
    • 23744494441 scopus 로고    scopus 로고
    • Identification of the cyclic-nucleotide-binding domain as a conserved determinant of ion-channel cell-surface localization
    • Akhavan A, Atanasiu R, Noguchi T, Han W, Holder N, Shrier A. Identification of the cyclic-nucleotide-binding domain as a conserved determinant of ion-channel cell-surface localization. J Cell Sci 118: 2803-2812, 2005.
    • (2005) J Cell Sci , vol.118 , pp. 2803-2812
    • Akhavan, A.1    Atanasiu, R.2    Noguchi, T.3    Han, W.4    Holder, N.5    Shrier, A.6
  • 4
    • 0029952101 scopus 로고    scopus 로고
    • K(V)LQT1 and lsK (minK) proteins associate to form the I(Ks) cardiac potassium current
    • Barhanin J, Lesage F, Guillemare E, Fink M, Lazdunski M, Romey G. K(V)LQT1 and lsK (minK) proteins associate to form the I(Ks) cardiac potassium current. Nature 384: 78-80, 1996.
    • (1996) Nature , vol.384 , pp. 78-80
    • Barhanin, J.1    Lesage, F.2    Guillemare, E.3    Fink, M.4    Lazdunski, M.5    Romey, G.6
  • 5
    • 70749158232 scopus 로고    scopus 로고
    • Trafficking-deficient long QT syndrome mutation KCNQ1-T587M confers severe clinical phenotype by impairment of KCNH2 membrane localization: Evidence for clinically significant IKr-IKs alpha-subunit interaction
    • Biliczki P, Girmatsion Z, Brandes RP, Harenkamp S, Pitard B, Charpentier F, Hebert TE, Hohnloser SH, Baro I, Nattel S, Ehrlich JR. Trafficking-deficient long QT syndrome mutation KCNQ1-T587M confers severe clinical phenotype by impairment of KCNH2 membrane localization: evidence for clinically significant IKr-IKs alpha-subunit interaction. Heart Rhythm 6: 1792-1801, 2009.
    • (2009) Heart Rhythm , vol.6 , pp. 1792-1801
    • Biliczki, P.1    Girmatsion, Z.2    Brandes, R.P.3    Harenkamp, S.4    Pitard, B.5    Charpentier, F.6    Hebert, T.E.7    Hohnloser, S.H.8    Baro, I.9    Nattel, S.10    Ehrlich, J.R.11
  • 6
    • 84856234056 scopus 로고    scopus 로고
    • Structure of the carboxy-terminal region of a KCNH channel
    • Brelidze TI, Carlson AE, Sankaran B, Zagotta WN. Structure of the carboxy-terminal region of a KCNH channel. Nature 481: 530-533, 2012.
    • (2012) Nature , vol.481 , pp. 530-533
    • Brelidze, T.I.1    Carlson, A.E.2    Sankaran, B.3    Zagotta, W.N.4
  • 8
    • 0035907235 scopus 로고    scopus 로고
    • Analysis of the cyclic nucleotide binding domain of the HERG potassium channel and interactions with KCNE2
    • Cui J, Kagan A, Qin D, Mathew J, Melman YF, McDonald TV. Analysis of the cyclic nucleotide binding domain of the HERG potassium channel and interactions with KCNE2. J Biol Chem 276: 17244-17251, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 17244-17251
    • Cui, J.1    Kagan, A.2    Qin, D.3    Mathew, J.4    Melman, Y.F.5    McDonald, T.V.6
  • 11
    • 0347093353 scopus 로고    scopus 로고
    • KvLQT1 modulates the distribution and biophysical properties of HERG. A novel alpha-subunit interaction between delayed rectifier currents
    • Ehrlich JR, Pourrier M, Weerapura M, Ethier N, Marmabachi AM, Hebert TE, Nattel S. KvLQT1 modulates the distribution and biophysical properties of HERG. A novel alpha-subunit interaction between delayed rectifier currents. J Biol Chem 279: 1233-1241, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 1233-1241
    • Ehrlich, J.R.1    Pourrier, M.2    Weerapura, M.3    Ethier, N.4    Marmabachi, A.M.5    Hebert, T.E.6    Nattel, S.7
  • 12
    • 33745064965 scopus 로고    scopus 로고
    • Assessment of prestin self-association using fluorescence resonance energy transfer
    • Greeson JN, Organ LE, Pereira FA, Raphael RM. Assessment of prestin self-association using fluorescence resonance energy transfer. Brain Res 1091: 140-150, 2006.
    • (2006) Brain Res , vol.1091 , pp. 140-150
    • Greeson, J.N.1    Organ, L.E.2    Pereira, F.A.3    Raphael, R.M.4
  • 13
    • 79952120982 scopus 로고    scopus 로고
    • hERG potassium channel gating is mediated by N-and C-terminal region interactions
    • Gustina AS, Trudeau MC. hERG potassium channel gating is mediated by N-and C-terminal region interactions. J Gen Physiol 137: 315-325, 2011.
    • (2011) J Gen Physiol , vol.137 , pp. 315-325
    • Gustina, A.S.1    Trudeau, M.C.2
  • 14
    • 69149108876 scopus 로고    scopus 로고
    • A recombinant N-terminal domain fully restores deactivation gating in N-truncated and long QT syndrome mutant hERG potassium channels
    • Gustina AS, Trudeau MC. A recombinant N-terminal domain fully restores deactivation gating in N-truncated and long QT syndrome mutant hERG potassium channels. Proc Natl Acad Sci USA 106: 13082-13087, 2009.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13082-13087
    • Gustina, A.S.1    Trudeau, M.C.2
  • 15
    • 0034966964 scopus 로고    scopus 로고
    • Slow delayed rectifier current and repolarization in canine cardiac Purkinje cells
    • Han W, Wang Z, Nattel S. Slow delayed rectifier current and repolarization in canine cardiac Purkinje cells. Am J Physiol Heart Circ Physiol 280: H1075-H1080, 2001.
    • (2001) Am J Physiol Heart Circ Physiol , vol.280
    • Han, W.1    Wang, Z.2    Nattel, S.3
  • 19
    • 0037238461 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser
    • Karpova TS, Baumann CT, He L, Wu X, Grammer A, Lipsky P, Hager GL, McNally JG. Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser. J Microsc 209: 56-70, 2003.
    • (2003) J Microsc , vol.209 , pp. 56-70
    • Karpova, T.S.1    Baumann, C.T.2    He, L.3    Wu, X.4    Grammer, A.5    Lipsky, P.6    Hager, G.L.7    McNally, J.G.8
  • 20
    • 84858952456 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic characterization of a cyclic nucleotide-binding homology domain from the mouse EAG potassium channel
    • Marques-Carvalho MJ, Morais-Cabral JH. Crystallization and preliminary X-ray crystallographic characterization of a cyclic nucleotide-binding homology domain from the mouse EAG potassium channel. Acta Crystallogr Sect F Struct Biol Cryst Commun 68: 337-339, 2012.
    • (2012) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.68 , pp. 337-339
    • Marques-Carvalho, M.J.1    Morais-Cabral, J.H.2
  • 21
    • 0037127028 scopus 로고    scopus 로고
    • Requirement of a macromolecular signaling complex for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel
    • Marx SO, Kurokawa J, Reiken S, Motoike H, D'Armiento J, Marks AR, Kass RS. Requirement of a macromolecular signaling complex for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel. Science 295: 496-499, 2002.
    • (2002) Science , vol.295 , pp. 496-499
    • Marx, S.O.1    Kurokawa, J.2    Reiken, S.3    Motoike, H.4    D'Armiento, J.5    Marks, A.R.6    Kass, R.S.7
  • 24
    • 0034633010 scopus 로고    scopus 로고
    • Forster distances between green fluorescent protein pairs
    • Patterson GH, Piston DW, Barisas BG. Forster distances between green fluorescent protein pairs. Anal Biochem 284: 438-440, 2000.
    • (2000) Anal Biochem , vol.284 , pp. 438-440
    • Patterson, G.H.1    Piston, D.W.2    Barisas, B.G.3
  • 25
    • 34548417621 scopus 로고    scopus 로고
    • Fluorescent protein FRET: The good, the bad and the ugly
    • Piston DW, Kremers GJ. Fluorescent protein FRET: the good, the bad and the ugly. Trends Biochem Sci 32: 407-414, 2007.
    • (2007) Trends Biochem Sci , vol.32 , pp. 407-414
    • Piston, D.W.1    Kremers, G.J.2
  • 28
    • 0032066007 scopus 로고    scopus 로고
    • Taking the "idio" out of "idiosyncratic": Predicting torsades de pointes
    • Roden DM. Taking the "idio" out of "idiosyncratic": predicting torsades de pointes. Pacing Clin Electrophysiol 21: 1029-1034, 1998.
    • (1998) Pacing Clin Electrophysiol , vol.21 , pp. 1029-1034
    • Roden, D.M.1
  • 29
    • 24744454175 scopus 로고    scopus 로고
    • Protecting the heart against arrhythmias: Potassium current physiology and repolarization reserve
    • Roden DM, Yang T. Protecting the heart against arrhythmias: potassium current physiology and repolarization reserve. Circulation 112: 1376-1378, 2005.
    • (2005) Circulation , vol.112 , pp. 1376-1378
    • Roden, D.M.1    Yang, T.2
  • 31
    • 0029002969 scopus 로고
    • A mechanistic link between an inherited and an acquired cardiac arrhythmia: HERG encodes the IKr potassium channel
    • Sanguinetti MC, Jiang C, Curran ME, Keating MT. A mechanistic link between an inherited and an acquired cardiac arrhythmia: HERG encodes the IKr potassium channel. Cell 81: 299-307, 1995.
    • (1995) Cell , vol.81 , pp. 299-307
    • Sanguinetti, M.C.1    Jiang, C.2    Curran, M.E.3    Keating, M.T.4
  • 32
    • 0025351245 scopus 로고
    • + current. Differential sensitivity to block by class III antiarrhythmic agents
    • + current. Differential sensitivity to block by class III antiarrhythmic agents. J Gen Physiol 96: 195-215, 1990.
    • (1990) J Gen Physiol , vol.96 , pp. 195-215
    • Sanguinetti, M.C.1    Jurkiewicz, N.K.2
  • 33
    • 0029007356 scopus 로고
    • HERG, a human inward rectifier in the voltage-gated potassium channel family
    • Trudeau MC, Warmke JW, Ganetzky B, Robertson GA. HERG, a human inward rectifier in the voltage-gated potassium channel family. Science 269: 92-95, 1995.
    • (1995) Science , vol.269 , pp. 92-95
    • Trudeau, M.C.1    Warmke, J.W.2    Ganetzky, B.3    Robertson, G.A.4
  • 35
    • 0028292927 scopus 로고
    • A family of potassium channel genes related to eag in Drosophila and mammals
    • Warmke JW, Ganetzky B. A family of potassium channel genes related to eag in Drosophila and mammals. Proc Natl Acad Sci USA 91: 3438-3442, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3438-3442
    • Warmke, J.W.1    Ganetzky, B.2
  • 36
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias DA, Violin JD, Newton AC, Tsien RY. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296: 913-916, 2002.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.