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Volumn 5, Issue 5, 2011, Pages

Nano-environmental changes by KCNE proteins modify KCNQ channel function

Author keywords

KCNE; KCNQ1 channel; Potassium channels; Stoichiometry; Voltage sensor

Indexed keywords

POTASSIUM CHANNEL KCNE1; POTASSIUM CHANNEL KCNE2; POTASSIUM CHANNEL KCNE3; POTASSIUM CHANNEL KCNQ; POTASSIUM CHANNEL KCNQ1; UNCLASSIFIED DRUG; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 80052626500     PISSN: 19336950     EISSN: 19336969     Source Type: Journal    
DOI: 10.4161/chan.5.5.16468     Document Type: Review
Times cited : (17)

References (65)
  • 1
    • 29844437655 scopus 로고    scopus 로고
    • International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels
    • Gutman GA, Chandy KG, Grissmer S, Lazdunski M, McKinnon D, Pardo LA, et al. International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels. Pharmacol Rev 2005; 57:473-508.
    • (2005) Pharmacol Rev , vol.57 , pp. 473-508
    • Gutman, G.A.1    Chandy, K.G.2    Grissmer, S.3    Lazdunski, M.4    McKinnon, D.5    Pardo, L.A.6
  • 3
    • 0023734276 scopus 로고
    • Cloning of a membrane protein that induces a slow voltage-gated potassium current
    • Takumi T, Ohkubo H, Nakanishi S. Cloning of a membrane protein that induces a slow voltage-gated potassium current. Science 1988; 242:1042-5.
    • (1988) Science , vol.242 , pp. 1042-1045
    • Takumi, T.1    Ohkubo, H.2    Nakanishi, S.3
  • 6
    • 77950933650 scopus 로고    scopus 로고
    • How is the highly positive endocochlear potential formed? The specific architecture of the stria vascularis and the roles of the ion-transport apparatus
    • Hibino H, Nin F, Tsuzuki C, Kurachi Y. How is the highly positive endocochlear potential formed? The specific architecture of the stria vascularis and the roles of the ion-transport apparatus. Pflugers Arch 2010; 459:521-33.
    • (2010) Pflugers Arch , vol.459 , pp. 521-533
    • Hibino, H.1    Nin, F.2    Tsuzuki, C.3    Kurachi, Y.4
  • 10
    • 0026794064 scopus 로고
    • Specification of subunit assembly by the hydrophilic amino-terminal domain of the Shaker potassium channel
    • Li M, Jan YN, Jan LY. Specification of subunit assembly by the hydrophilic amino-terminal domain of the Shaker potassium channel. Science 1992; 257:1225-30.
    • (1992) Science , vol.257 , pp. 1225-1230
    • Li, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 12
    • 0034268781 scopus 로고    scopus 로고
    • The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel
    • Minor DL, Lin YF, Mobley BC, Avelar A, Jan YN, Jan LY, Berger JM. The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel. Cell 2000; 102:657-70.
    • (2000) Cell , vol.102 , pp. 657-670
    • Minor, D.L.1    Lin, Y.F.2    Mobley, B.C.3    Avelar, A.4    Jan, Y.N.5    Jan, L.Y.6    Berger, J.M.7
  • 14
    • 45249089942 scopus 로고    scopus 로고
    • Second coiled-coil domain of KCNQ channel controls current expression and subfamily specific heteromultimerization by salt bridge networks
    • DOI 10.1113/jphysiol.2007.148601
    • Nakajo K, Kubo Y. Second coiled-coil domain of KCNQ channel controls current expression and sub-family specific heteromultimerization by salt bridge networks. J Physiol 2008; 586:2827-40. (Pubitemid 351837279)
    • (2008) Journal of Physiology , vol.586 , Issue.12 , pp. 2827-2840
    • Nakajo, K.1    Kubo, Y.2
  • 15
    • 70349449896 scopus 로고    scopus 로고
    • V7.1 (KCNQ1) A-domain tail coiled-coil reveals structural plasticity and context dependent changes in a putative coiled-coil trimerization motif
    • V7.1 (KCNQ1) A-domain tail coiled-coil reveals structural plasticity and context dependent changes in a putative coiled-coil trimerization motif. Protein Sci 2009; 18:2100-14.
    • (2009) Protein Sci , vol.18 , pp. 2100-2114
    • Xu, Q.1    Minor Jr., D.L.2
  • 19
    • 37049009981 scopus 로고    scopus 로고
    • Structural models for the KCNQ1 voltage-gated potassium channel
    • DOI 10.1021/bi701597s
    • Smith JA, Vanoye CG, George AL Jr, Meiler J, Sanders CR. Structural models for the KCNQ1 voltage-gated potassium channel. Biochemistry 2007; 46:14141-52. (Pubitemid 350250308)
    • (2007) Biochemistry , vol.46 , Issue.49 , pp. 14141-14152
    • Smith, J.A.1    Vanoye, C.G.2    George Jr., A.L.3    Meiler, J.4    Sanders, C.R.5
  • 21
    • 48649098982 scopus 로고    scopus 로고
    • Structure of KCNE1 and implications for how it modulates the KCNQ1 potassium channel
    • Kang C, Tian C, Sonnichsen FD, Smith JA, Meiler J, George AL Jr, et al. Structure of KCNE1 and implications for how it modulates the KCNQ1 potassium channel. Biochemistry 2008; 47:7999-8006.
    • (2008) Biochemistry , vol.47 , pp. 7999-8006
    • Kang, C.1    Tian, C.2    Sonnichsen, F.D.3    Smith, J.A.4    Meiler, J.5    George Jr., A.L.6
  • 22
    • 0032484982 scopus 로고    scopus 로고
    • The conduction pore of a cardiac potassium channel
    • DOI 10.1038/35416
    • Tai KK, Goldstein SA. The conduction pore of a cardiac potassium channel. Nature 1998; 391:605-8. (Pubitemid 28157605)
    • (1998) Nature , vol.391 , Issue.6667 , pp. 605-608
    • Tai, K.-K.1    Goldstein, S.A.N.2
  • 26
    • 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 YF, Um SY, Krumerman A, Kagan A, McDonald TV. KCNE1 binds to the KCNQ1 pore to regulate potassium channel activity. Neuron 2004; 42:927-37. (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
  • 28
    • 34848851880 scopus 로고    scopus 로고
    • Ks implies an α-helical transmembrane span traversing the channel corpus
    • Ks implies an α-helical transmembrane span traversing the channel corpus. Biophys J 2007; 93:2332-40.
    • (2007) Biophys J , vol.93 , pp. 2332-2340
    • Chen, H.1    Goldstein, S.A.2
  • 29
    • 0034642569 scopus 로고    scopus 로고
    • A constitutively open potassium channel formed by KCNQ1 and KCNE3
    • DOI 10.1038/35003200
    • Schroeder BC, Waldegger S, Fehr S, Bleich M, Warth R, Greger R, Jentsch TJ. A constitutively open potassium channel formed by KCNQ1 and KCNE3. Nature 2000; 403:196-9. (Pubitemid 30050962)
    • (2000) Nature , vol.403 , Issue.6766 , pp. 196-199
    • Schroeder, B.C.1    Waldegger, S.2    Fehr, S.3    Bleich, M.4    Warth, R.5    Greger, R.6    Jentsch, T.J.7
  • 35
    • 64549110297 scopus 로고    scopus 로고
    • Functional interactions between KCNE1 C-terminus and the KCNQ1 channel
    • Chen J, Zheng R, Melman YF, McDonald TV. Functional interactions between KCNE1 C-terminus and the KCNQ1 channel. PLoS One 2009; 4:5143.
    • (2009) PLoS One , vol.4 , pp. 5143
    • Chen, J.1    Zheng, R.2    Melman, Y.F.3    McDonald, T.V.4
  • 36
    • 77953041426 scopus 로고    scopus 로고
    • Identification of a protein-protein interaction between KCNE1 and the activation gate machinery of KCNQ1
    • Lvov A, Gage SD, Berrios VM, Kobertz WR. Identification of a protein-protein interaction between KCNE1 and the activation gate machinery of KCNQ1. J Gen Physiol 2010; 135:607-18.
    • (2010) J Gen Physiol , vol.135 , pp. 607-618
    • Lvov, A.1    Gage, S.D.2    Berrios, V.M.3    Kobertz, W.R.4
  • 37
    • 77953412214 scopus 로고    scopus 로고
    • Analysis of the interactions between the C-terminal cytoplasmic domains of KCNQ1 and KCNE1 channel subunits
    • Zheng R, Thompson K, Obeng-Gyimah E, Alessi D, Chen J, Cheng H, McDonald TV. Analysis of the interactions between the C-terminal cytoplasmic domains of KCNQ1 and KCNE1 channel subunits. Biochem J 2010; 428:75-84.
    • (2010) Biochem J , vol.428 , pp. 75-84
    • Zheng, R.1    Thompson, K.2    Obeng-Gyimah, E.3    Alessi, D.4    Chen, J.5    Cheng, H.6    McDonald, T.V.7
  • 38
    • 67651151053 scopus 로고    scopus 로고
    • Intracellular domains interactions and gated motions of IKS potassium channel subunits
    • Haitin Y, Wiener R, Shaham D, Peretz A, Cohen EB, Shamgar L, et al. Intracellular domains interactions and gated motions of IKS potassium channel subunits. EMBO J 2009; 28:1994-2005.
    • (2009) EMBO J , vol.28 , pp. 1994-2005
    • Haitin, Y.1    Wiener, R.2    Shaham, D.3    Peretz, A.4    Cohen, E.B.5    Shamgar, L.6
  • 39
    • 33846582472 scopus 로고    scopus 로고
    • The role of S4 charges in voltage-dependent and voltage-independent KCNQ1 potassium channel complexes
    • DOI 10.1085/jgp.200609612
    • Panaghie G, Abbott GW. The role of S4 charges in voltage-dependent and voltage-independent KCNQ1 potassium channel complexes. J Gen Physiol 2007; 129:121-33. (Pubitemid 46184870)
    • (2007) Journal of General Physiology , vol.129 , Issue.2 , pp. 121-133
    • Panaghie, G.1    Abbott, G.W.2
  • 40
    • 34548825159 scopus 로고    scopus 로고
    • KCNE1 and KCNE3 stabilize and/or slow voltage sensing S4 segment of KCNQ1 channel
    • DOI 10.1085/jgp.200709805
    • Nakajo K, Kubo Y. KCNE1 and KCNE3 stabilize and/ or slow voltage sensing S4 segment of KCNQ1 channel. J Gen Physiol 2007; 130:269-81. (Pubitemid 47443289)
    • (2007) Journal of General Physiology , vol.130 , Issue.3 , pp. 269-281
    • Nakajo, K.1    Kubo, Y.2
  • 41
    • 38049075811 scopus 로고    scopus 로고
    • KCNE peptides differently affect voltage sensor equilibrium and equilibration rates in KCNQ1 K+ channels
    • Rocheleau JM, Kobertz WR. KCNE peptides differently affect voltage sensor equilibrium and equilibration rates in KCNQ1 K+ channels. J Gen Physiol 2008; 131:59-68.
    • (2008) J Gen Physiol , vol.131 , pp. 59-68
    • Rocheleau, J.M.1    Kobertz, W.R.2
  • 42
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutants
    • Akabas MH, Stauffer DA, Xu M, Karlin A. Acetylcholine receptor channel structure probed in cysteine-substitution mutants. Science 1992; 258:307-10.
    • (1992) Science , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 43
    • 0030070436 scopus 로고    scopus 로고
    • + channel S4
    • DOI 10.1016/S0896-6273(00)80056-2
    • Larsson HP, Baker OS, Dhillon DS, Isacoff EY. Transmembrane movement of the shaker K+ channel S4. Neuron 1996; 16:387-97. (Pubitemid 26072371)
    • (1996) Neuron , vol.16 , Issue.2 , pp. 387-397
    • Larsson, H.P.1    Baker, O.S.2    Dhillon, D.S.3    Isacoff, E.Y.4
  • 44
    • 0030059224 scopus 로고    scopus 로고
    • Direct physical measure of conformational rearrangement underlying potassium channel gating
    • Mannuzzu LM, Moronne MM, Isacoff EY. Direct physical measure of conformational rearrangement underlying potassium channel gating. Science 1996; 271:213-6. (Pubitemid 26033303)
    • (1996) Science , vol.271 , Issue.5246 , pp. 213-216
    • Mannuzzu, L.M.1    Moronne, M.M.2    Isacoff, E.Y.3
  • 49
    • 44349127924 scopus 로고    scopus 로고
    • Ks channel complex make state-dependent contacts in their extracellular domains
    • DOI 10.1085/jgp.200809976
    • Xu X, Jiang M, Hsu KL, Zhang M, Tseng GN. KCNQ1 and KCNE1 in the IKs channel complex make state-dependent contacts in their extracellular domains. J Gen Physiol 2008; 131:589-603. (Pubitemid 351749199)
    • (2008) Journal of General Physiology , vol.131 , Issue.6 , pp. 589-603
    • Xu, L.1    Jiang, M.2    Hsu, K.-L.3    Zhang, M.4    Tseng, G.-N.5
  • 53
    • 0029034215 scopus 로고
    • Subunit composition of minK potassium channels
    • Wang KW, Goldstein SA. Subunit composition of minK potassium channels. Neuron 1995; 14:1303-9.
    • (1995) Neuron , vol.14 , pp. 1303-1309
    • Wang, K.W.1    Goldstein, S.A.2
  • 57
    • 34247843089 scopus 로고    scopus 로고
    • Subunit counting in membrane-bound proteins
    • DOI 10.1038/nmeth1024, PII NMETH1024
    • Ulbrich MH, Isacoff EY. Subunit counting in membrane- bound proteins. Nat Methods 2007; 4:319-21. (Pubitemid 46766975)
    • (2007) Nature Methods , vol.4 , Issue.4 , pp. 319-321
    • Ulbrich, M.H.1    Isacoff, E.Y.2
  • 58
    • 52949144934 scopus 로고    scopus 로고
    • Rules of engagement for NMDA receptor subunits
    • Ulbrich MH, Isacoff EY. Rules of engagement for NMDA receptor subunits. Proc Natl Acad Sci USA 2008; 105:14163-8.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14163-14168
    • Ulbrich, M.H.1    Isacoff, E.Y.2
  • 60
    • 29344448027 scopus 로고    scopus 로고
    • Expression and transcriptional control of human KCNE genes
    • DOI 10.1016/j.ygeno.2005.09.004, PII S0888754305002521
    • Lundquist AL, Turner CL, Ballester LY, George AL Jr. Expression and transcriptional control of human KCNE genes. Genomics 2006; 87:119-28. (Pubitemid 43005108)
    • (2006) Genomics , vol.87 , Issue.1 , pp. 119-128
    • Lundquist, A.L.1    Turner, C.L.2    Ballester, L.Y.3    George Jr., A.L.4
  • 61
    • 22544475622 scopus 로고    scopus 로고
    • In vitro molecular interactions and distribution of KCNE family with KCNQ1 in the human heart
    • Bendahhou S, Marionneau C, Haurogne K, Larroque MM, Derand R, Szuts V, et al. In vitro molecular interactions and distribution of KCNE family with KCNQ1 in the human heart. Cardiovasc Res 2005; 67:529-38.
    • (2005) Cardiovasc Res , vol.67 , pp. 529-538
    • Bendahhou, S.1    Marionneau, C.2    Haurogne, K.3    Larroque, M.M.4    Derand, R.5    Szuts, V.6
  • 62
    • 33646127798 scopus 로고    scopus 로고
    • Modulation of functional properties of KCNQ1 channel by association of KCNE1 and KCNE2
    • Toyoda F, Ueyama H, Ding WG, Matsuura H. Modulation of functional properties of KCNQ1 channel by association of KCNE1 and KCNE2. Biochem Biophys Res Commun 2006; 344:814-20.
    • (2006) Biochem Biophys Res Commun , vol.344 , pp. 814-820
    • Toyoda, F.1    Ueyama, H.2    Ding, W.G.3    Matsuura, H.4


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