메뉴 건너뛰기




Volumn 428, Issue 1, 2010, Pages 75-84

Analysis of the interactions between the C-terminal cytoplasmic domains of KCNQ1 and KCNE1 channel subunits

Author keywords

Ion channel; KCNE1; KCNQ1; Long QT syndrome (LQTS); Voltage gated potassium channel

Indexed keywords

C-TERMINUS; CHANNEL ACTIVATION; CHANNEL REGULATION; CULTURED CELL; CYTOPLASMIC DOMAINS; DEACTIVATION KINETICS; DELETION ANALYSIS; DISSOCIATION CONSTANT; FUNCTIONAL INTERACTION; INTERACTION DOMAIN; ION CHANNEL; LONG QT SYNDROMES; MEMBRANE-SPANNING SEGMENTS; N-TERMINALS; PHYSICAL INTERACTIONS; REPOLARIZATION; SPR (SURFACE PLASMON RESONANCE); TERMINAL PORTIONS; TETRAMERIZATION; TRANSMEMBRANE SEGMENTS; VOLTAGE-GATED POTASSIUM CHANNELS;

EID: 77953412214     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20090977     Document Type: Article
Times cited : (33)

References (32)
  • 1
    • 0034929557 scopus 로고    scopus 로고
    • KCNQ potassium channels: Physiology, pathophysiology, and pharmacology
    • Robbins, J. (2001) KCNQ potassium channels: physiology, pathophysiology, and pharmacology. Pharmacol. Ther. 90, 1-19
    • (2001) Pharmacol. Ther. , vol.90 , pp. 1-19
    • Robbins, J.1
  • 4
    • 0035936798 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of cardiac arrhythmias
    • DOI 10.1016/S0092-8674(01)00243-4
    • Keating, M. T. and Sanguinetti, M. C. (2001) Molecular and cellular mechanisms of cardiac arrhythmias. Cell 104, 569-580 (Pubitemid 32201951)
    • (2001) Cell , vol.104 , Issue.4 , pp. 569-580
    • Keating, M.T.1    Sanguinetti, M.C.2
  • 7
    • 33646810883 scopus 로고    scopus 로고
    • Calmodulin is essential for cardiac IKS channel gating and assembly: Impaired function in long-QT mutations
    • Shamgar, L., Ma, L., Schmitt, N., Haitin, Y., Peretz, A., Wiener, R., Hirsch, J., Pongs, O. and Attali, B. (2006) Calmodulin is essential for cardiac IKS channel gating and assembly: impaired function in long-QT mutations. Circ. Res. 98, 1055-1063
    • (2006) Circ. Res. , vol.98 , pp. 1055-1063
    • Shamgar, L.1    Ma, L.2    Schmitt, N.3    Haitin, Y.4    Peretz, A.5    Wiener, R.6    Hirsch, J.7    Pongs, O.8    Attali, B.9
  • 8
    • 33646814436 scopus 로고    scopus 로고
    • KCNQ1 assembly and function is blocked by long-QT syndrome mutations that disrupt interaction with calmodulin
    • Ghosh, S., Nunziato, D. A. and Pitt, G. S. (2006) KCNQ1 assembly and function is blocked by long-QT syndrome mutations that disrupt interaction with calmodulin. Circ. Res. 98, 1048-1054
    • (2006) Circ. Res. , vol.98 , pp. 1048-1054
    • Ghosh, S.1    Nunziato, D.A.2    Pitt, G.S.3
  • 9
    • 33847091589 scopus 로고    scopus 로고
    • Structural insight into KCNQ (Kv7) channel assembly and channelopathy
    • Howard, R. J., Clark, K. A., Holton, J. M. and Minor, Jr, D. L. (2007) Structural insight into KCNQ (Kv7) channel assembly and channelopathy. Neuron 53, 663-675
    • (2007) Neuron , vol.53 , pp. 663-675
    • Howard, R.J.1    Clark, K.A.2    Holton, J.M.3    Minor Jr., D.L.4
  • 11
    • 0037107123 scopus 로고    scopus 로고
    • Calmodulin is an auxiliary subunit of KCNQ2/3 potassium channels
    • Wen, H. and Levitan, I. B. (2002) Calmodulin is an auxiliary subunit of KCNQ2/3 potassium channels. J. Neurosci. 22, 7991-8001 (Pubitemid 35379104)
    • (2002) Journal of Neuroscience , vol.22 , Issue.18 , pp. 7991-8001
    • Wen, H.1    Levitan, I.B.2
  • 12
    • 0037047394 scopus 로고    scopus 로고
    • The identification and characterization of a noncontinuous calmodulin-binding site in noninactivating voltage-dependent KCNQ potassium channels
    • Yus-Najera, E., Santana-Castro, I. and Villarroel, A. (2002) The identification and characterization of a noncontinuous calmodulin-binding site in noninactivating voltage-dependent KCNQ potassium channels. J. Biol. Chem. 277, 28545-28553
    • (2002) J. Biol. Chem. , vol.277 , pp. 28545-28553
    • Yus-Najera, E.1    Santana-Castro, I.2    Villarroel, A.3
  • 13
    • 0032474439 scopus 로고    scopus 로고
    • Conformation and ion-channeling activity of a 27-residue peptide modeled on the single-transmembrane segment of the IsK (minK) protein
    • Aggeli, A., Bannister, M. L., Bell, M., Boden, N., Findlay, J. B., Hunter, M., Knowles, P. F. and Yang, J. C. (1998) Conformation and ion-channeling activity of a 27-residue peptide modeled on the single-transmembrane segment of the IsK (minK) protein. Biochemistry 37, 8121-8131
    • (1998) Biochemistry , vol.37 , pp. 8121-8131
    • Aggeli, A.1    Bannister, M.L.2    Bell, M.3    Boden, N.4    Findlay, J.B.5    Hunter, M.6    Knowles, P.F.7    Yang, J.C.8
  • 14
    • 2942746320 scopus 로고    scopus 로고
    • KCNE1 binds to the KCNQ1 pore to regulate potassium channel activity
    • DOI 10.1016/j.neuron.2004.06.001, PII S0896627304003307
    • Melman, Y. F., Um, S. Y., Krumerman, A., Kagan, A. and McDonald, T. V. (2004) KCNE1 binds to the KCNQ1 pore to regulate potassium channel activity. Neuron 42, 927-937 (Pubitemid 38798231)
    • (2004) Neuron , vol.42 , Issue.6 , pp. 927-937
    • Melman, Y.F.1    Um, S.Y.2    Krumerman, A.3    Kagan, A.4    McDonald, T.V.5
  • 15
    • 0035794229 scopus 로고    scopus 로고
    • Structural determinants of KvLQT1 control by the KCNE family of proteins
    • Melman, Y. F., Domenech, A., de la Luna, S. and McDonald, T. V. (2001) Structural determinants of KvLQT1 control by the KCNE family of proteins. J. Biol. Chem. 276, 6439-6444
    • (2001) J. Biol. Chem. , vol.276 , pp. 6439-6444
    • Melman, Y.F.1    Domenech, A.2    De La Luna, S.3    McDonald, T.V.4
  • 16
    • 0037067686 scopus 로고    scopus 로고
    • A single transmembrane site in the KCNE-encoded proteins controls the specificity of KvLQT1 channel gating
    • Melman, Y. F., Krumerman, A. and McDonald, T. V. (2002) A single transmembrane site in the KCNE-encoded proteins controls the specificity of KvLQT1 channel gating. J. Biol. Chem. 277, 25187-25194
    • (2002) J. Biol. Chem. , vol.277 , pp. 25187-25194
    • Melman, Y.F.1    Krumerman, A.2    McDonald, T.V.3
  • 17
    • 33846582472 scopus 로고    scopus 로고
    • The role of S4 charges in voltage-dependent and voltage-independent KCNQ1 potassium channel complexes
    • Panaghie, G. and Abbott, G. W. (2007) The role of S4 charges in voltage-dependent and voltage-independent KCNQ1 potassium channel complexes. J. Gen. Physiol. 129, 121-133
    • (2007) J. Gen. Physiol. , vol.129 , pp. 121-133
    • Panaghie, G.1    Abbott, G.W.2
  • 18
    • 64549110297 scopus 로고    scopus 로고
    • Functional interactions between KCNE1 C-terminus and the KCNQ1 channel
    • Chen, J., Zheng, R., Melman, Y. F. and McDonald, T. V. (2009) Functional interactions between KCNE1 C-terminus and the KCNQ1 channel. PLoS ONE 4, e5143
    • (2009) PLoS ONE , vol.4
    • Chen, J.1    Zheng, R.2    Melman, Y.F.3    McDonald, T.V.4
  • 21
    • 0033811345 scopus 로고    scopus 로고
    • MinK subdomains that mediate modulation of and association with KvLQT1
    • Tapper, A. R. and George, Jr, A. L. (2000) MinK subdomains that mediate modulation of and association with KvLQT1. J. Gen. Physiol. 116, 379-390
    • (2000) J. Gen. Physiol. , vol.116 , pp. 379-390
    • Tapper, A.R.1    George Jr., A.L.2
  • 22
    • 0034426852 scopus 로고    scopus 로고
    • Experimental design for analysis of complex kinetics using surface plasmon resonance
    • DOI 10.1006/meth.1999.0924
    • Lipschultz, C. A., Li, Y. and Smith-Gill, S. (2000) Experimental design for analysis of complex kinetics using surface plasmon resonance. Methods 20, 310-318 (Pubitemid 32905165)
    • (2000) Methods , vol.20 , Issue.3 , pp. 310-318
    • Lipschultz, C.A.1    Li, Y.2    Smith-Gill, S.3
  • 23
    • 0001068447 scopus 로고    scopus 로고
    • Measuring protein interactions by optical biosensors
    • Colgin, J. E., Dunn, B. M., Ploegh, H. L., Speicher, D. W. and Wingfield, P. T. eds John Wiley and Sons, Chichester
    • Schuck, P., Boyd, L. and Andersen, P. (1999) Measuring protein interactions by optical biosensors. In Current Protocols in Protein Science (Colgin, J. E., Dunn, B. M., Ploegh, H. L., Speicher, D. W. and Wingfield, P. T. eds), pp. 20.22.21-20.22.22, John Wiley and Sons, Chichester
    • (1999) Current Protocols in Protein Science
    • Schuck, P.1    Boyd, L.2    Andersen, P.3
  • 24
    • 44349127924 scopus 로고    scopus 로고
    • KCNQ1 and KCNE1 in the IKs channel complex make state-dependent contacts in their extracellular domains
    • Xu, X., Jiang, M., Hsu, K. L., Zhang, M. and Tseng, G. N. (2008) KCNQ1 and KCNE1 in the IKs channel complex make state-dependent contacts in their extracellular domains. J. Gen. Physiol. 131, 589-603
    • (2008) J. Gen. Physiol. , vol.131 , pp. 589-603
    • Xu, X.1    Jiang, M.2    Hsu, K.L.3    Zhang, M.4    Tseng, G.N.5
  • 27
    • 35348847305 scopus 로고    scopus 로고
    • Preparation, functional characterization, and NMR studies of human KCNE1, a voltage-gated potassium channel accessory subunit associated with deafness and long QT syndrome
    • Tian, C., Vanoye, C. G., Kang, C., Welch, R. C., Kim, H. J., George, Jr, A. L. and Sanders, C. R. (2007) Preparation, functional characterization, and NMR studies of human KCNE1, a voltage-gated potassium channel accessory subunit associated with deafness and long QT syndrome. Biochemistry 46, 11459-11472
    • (2007) Biochemistry , vol.46 , pp. 11459-11472
    • Tian, C.1    Vanoye, C.G.2    Kang, C.3    Welch, R.C.4    Kim, H.J.5    George Jr., A.L.6    Sanders, C.R.7
  • 29
    • 33751513050 scopus 로고    scopus 로고
    • Secondary structure of a KCNE cytoplasmic domain
    • Rocheleau, J. M., Gage, S. D. and Kobertz, W. R. (2006) Secondary structure of a KCNE cytoplasmic domain. J. Gen. Physiol. 128, 721-729
    • (2006) J. Gen. Physiol. , vol.128 , pp. 721-729
    • Rocheleau, J.M.1    Gage, S.D.2    Kobertz, W.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.