메뉴 건너뛰기




Volumn 20, Issue 8, 2012, Pages 1343-1352

How does KCNE1 regulate the Kv7.1 potassium channel? Model-structure, mutations, and dynamics of the Kv7.1-KCNE1 complex

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; POTASSIUM CHANNEL KCNE1;

EID: 84864838991     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.05.016     Document Type: Article
Times cited : (28)

References (61)
  • 1
    • 0033517136 scopus 로고    scopus 로고
    • Stilbenes and fenamates rescue the loss of I(KS) channel function induced by an LQT5 mutation and other IsK mutants
    • DOI 10.1093/emboj/18.15.4137
    • I. Abitbol, A. Peretz, C. Lerche, A.E. Busch, and B. Attali Stilbenes and fenamates rescue the loss of I(KS) channel function induced by an LQT5 mutation and other IsK mutants EMBO J. 18 1999 4137 4148 (Pubitemid 29364117)
    • (1999) EMBO Journal , vol.18 , Issue.15 , pp. 4137-4148
    • Abitbol, I.1    Peretz, A.2    Lerche, C.3    Busch, A.E.4    Attali, B.5
  • 3
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • W529-33
    • H. Ashkenazy, E. Erez, E. Martz, T. Pupko, and N. Ben-Tal ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids Nucleic Acids Res. 38 Web Server issue, Suppl 2010 W529-33
    • (2010) Nucleic Acids Res. , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 5
    • 77953050209 scopus 로고    scopus 로고
    • On the functional significance of soft modes predicted by coarse-grained models for membrane proteins
    • I. Bahar On the functional significance of soft modes predicted by coarse-grained models for membrane proteins J. Gen. Physiol. 135 2010 563 573
    • (2010) J. Gen. Physiol. , vol.135 , pp. 563-573
    • Bahar, I.1
  • 6
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    • I. Bahar, A.R. Atilgan, and B. Erman Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential Fold. Des. 2 1997 173 181 (Pubitemid 127740467)
    • (1997) Folding and Design , vol.2 , Issue.3 , pp. 173-181
    • Bahar, I.1    Atilgan, A.R.2    Erman, B.3
  • 7
    • 77949634796 scopus 로고    scopus 로고
    • Normal mode analysis of biomolecular structures: Functional mechanisms of membrane proteins
    • I. Bahar, T.R. Lezon, A. Bakan, and I.H. Shrivastava Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins Chem. Rev. 110 2010 1463 1497
    • (2010) Chem. Rev. , vol.110 , pp. 1463-1497
    • Bahar, I.1    Lezon, T.R.2    Bakan, A.3    Shrivastava, I.H.4
  • 8
    • 60849099626 scopus 로고    scopus 로고
    • Prediction of membrane protein structures with complex topologies using limited constraints
    • P. Barth, B. Wallner, and D. Baker Prediction of membrane protein structures with complex topologies using limited constraints Proc. Natl. Acad. Sci. USA 106 2009 1409 1414
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1409-1414
    • Barth, P.1    Wallner, B.2    Baker, D.3
  • 9
    • 77955087369 scopus 로고    scopus 로고
    • Conformational dynamics in the selectivity filter of KcsA in response to potassium ion concentration
    • M.P. Bhate, B.J. Wylie, L. Tian, and A.E. McDermott Conformational dynamics in the selectivity filter of KcsA in response to potassium ion concentration J. Mol. Biol. 401 2010 155 166
    • (2010) J. Mol. Biol. , vol.401 , pp. 155-166
    • Bhate, M.P.1    Wylie, B.J.2    Tian, L.3    McDermott, A.E.4
  • 11
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • S.K. Burley, and G.A. Petsko Aromatic-aromatic interaction: a mechanism of protein structure stabilization Science 229 1985 23 28
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 12
    • 0026489631 scopus 로고
    • Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping
    • C.L. Careaga, and J.J. Falke Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping J. Mol. Biol. 226 1992 1219 1235
    • (1992) J. Mol. Biol. , vol.226 , pp. 1219-1235
    • Careaga, C.L.1    Falke, J.J.2
  • 13
    • 78049405427 scopus 로고    scopus 로고
    • Analysis and functional implications of phosphorylation of neuronal voltage-gated potassium channels
    • O. Cerda, and J.S. Trimmer Analysis and functional implications of phosphorylation of neuronal voltage-gated potassium channels Neurosci. Lett. 486 2010 60 67
    • (2010) Neurosci. Lett. , vol.486 , pp. 60-67
    • Cerda, O.1    Trimmer, J.S.2
  • 15
    • 0141996211 scopus 로고    scopus 로고
    • Ks pore demonstrates two MinK subunits in each channel complex
    • DOI 10.1016/S0896-6273(03)00570-1
    • H. Chen, L.A. Kim, S. Rajan, S. Xu, and S.A. Goldstein Charybdotoxin binding in the I(Ks) pore demonstrates two MinK subunits in each channel complex Neuron 40 2003 15 23 (Pubitemid 37229082)
    • (2003) Neuron , vol.40 , Issue.1 , pp. 15-23
    • Chen, H.1    Kim, L.A.2    Rajan, S.3    Xu, S.4    Goldstein, S.A.N.5
  • 16
    • 58849133458 scopus 로고    scopus 로고
    • Location of KCNE1 relative to KCNQ1 in the I(KS) potassium channel by disulfide cross-linking of substituted cysteines
    • D.Y. Chung, P.J. Chan, J.R. Bankston, L. Yang, G. Liu, S.O. Marx, A. Karlin, and R.S. Kass Location of KCNE1 relative to KCNQ1 in the I(KS) potassium channel by disulfide cross-linking of substituted cysteines Proc. Natl. Acad. Sci. USA 106 2009 743 748
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 743-748
    • Chung, D.Y.1    Chan, P.J.2    Bankston, J.R.3    Yang, L.4    Liu, G.5    Marx, S.O.6    Karlin, A.7    Kass, R.S.8
  • 22
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • DOI 10.1093/nar/gkh340
    • R.C. Edgar MUSCLE: multiple sequence alignment with high accuracy and high throughput Nucleic Acids Res. 32 2004 1792 1797 (Pubitemid 38832724)
    • (2004) Nucleic Acids Research , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1
  • 25
    • 0035342450 scopus 로고    scopus 로고
    • Residue frequencies and pairing preferences at protein-protein interfaces
    • F. Glaser, D.M. Steinberg, I.A. Vakser, and N. Ben-Tal Residue frequencies and pairing preferences at protein-protein interfaces Proteins 43 2001 89 102
    • (2001) Proteins , vol.43 , pp. 89-102
    • Glaser, F.1    Steinberg, D.M.2    Vakser, I.A.3    Ben-Tal, N.4
  • 26
    • 50949126927 scopus 로고    scopus 로고
    • Cooperative transition between open and closed conformations in potassium channels
    • T. Haliloglu, and N. Ben-Tal Cooperative transition between open and closed conformations in potassium channels PLoS Comput. Biol. 4 2008 e1000164
    • (2008) PLoS Comput. Biol. , vol.4 , pp. 1000164
    • Haliloglu, T.1    Ben-Tal, N.2
  • 28
    • 0034303612 scopus 로고    scopus 로고
    • Neuronal KCNQ potassium channels: Physiology and role in disease
    • T.J. Jentsch Neuronal KCNQ potassium channels: physiology and role in disease Nat. Rev. Neurosci. 1 2000 21 30
    • (2000) Nat. Rev. Neurosci. , vol.1 , pp. 21-30
    • Jentsch, T.J.1
  • 29
    • 29144529013 scopus 로고    scopus 로고
    • The KCNQ1 potassium channel: From gene to physiological function
    • DOI 10.1152/physiol.00031.2005
    • T. Jespersen, M. Grunnet, and S.P. Olesen The KCNQ1 potassium channel: from gene to physiological function Physiology (Bethesda) 20 2005 408 416 (Pubitemid 41812424)
    • (2005) Physiology , Issue.6 , pp. 408-416
    • Jespersen, T.1    Grunnet, M.2    Olesen, S.-P.3
  • 30
    • 77952850689 scopus 로고    scopus 로고
    • Quality assessment of protein model-structures using evolutionary conservation
    • M. Kalman, and N. Ben-Tal Quality assessment of protein model-structures using evolutionary conservation Bioinformatics 26 2010 1299 1307
    • (2010) Bioinformatics , vol.26 , pp. 1299-1307
    • Kalman, M.1    Ben-Tal, N.2
  • 33
    • 84855467714 scopus 로고    scopus 로고
    • Structural correlates of selectivity and inactivation in potassium channels
    • J.G. McCoy, and C.M. Nimigean Structural correlates of selectivity and inactivation in potassium channels Biochim. Biophys. Acta 1818 2012 272 285
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 272-285
    • McCoy, J.G.1    Nimigean, C.M.2
  • 34
    • 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
    • Y.F. Melman, S.Y. Um, A. Krumerman, A. Kagan, and T.V. McDonald KCNE1 binds to the KCNQ1 pore to regulate potassium channel activity Neuron 42 2004 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
  • 36
    • 80052626500 scopus 로고    scopus 로고
    • Nano-environmental changes by KCNE proteins modify KCNQ channel function
    • K. Nakajo, and Y. Kubo Nano-environmental changes by KCNE proteins modify KCNQ channel function Channels (Austin) 5 2011 397 401
    • (2011) Channels (Austin) , vol.5 , pp. 397-401
    • Nakajo, K.1    Kubo, Y.2
  • 39
    • 33645851047 scopus 로고    scopus 로고
    • Interaction of KCNE subunits with the KCNQ1 K+ channel pore
    • G. Panaghie, K.K. Tai, and G.W. Abbott Interaction of KCNE subunits with the KCNQ1 K+ channel pore J. Physiol. 570 2006 455 467
    • (2006) J. Physiol. , vol.570 , pp. 455-467
    • Panaghie, G.1    Tai, K.K.2    Abbott, G.W.3
  • 40
    • 55549094111 scopus 로고    scopus 로고
    • Voltage-dependent C-type inactivation in a constitutively open K+ channel
    • G. Panaghie, K. Purtell, K.K. Tai, and G.W. Abbott Voltage-dependent C-type inactivation in a constitutively open K+ channel Biophys. J. 95 2008 2759 2778
    • (2008) Biophys. J. , vol.95 , pp. 2759-2778
    • Panaghie, G.1    Purtell, K.2    Tai, K.K.3    Abbott, G.W.4
  • 41
    • 0031848480 scopus 로고    scopus 로고
    • Activation and inactivation of homomeric KvLQT1 potassium channels
    • M. Pusch, R. Magrassi, B. Wollnik, and F. Conti Activation and inactivation of homomeric KvLQT1 potassium channels Biophys. J. 75 1998 785 792 (Pubitemid 28357520)
    • (1998) Biophysical Journal , vol.75 , Issue.2 , pp. 785-792
    • Pusch, M.1    Magrassi, R.2    Wollnik, B.3    Conti, F.4
  • 44
    • 0142181060 scopus 로고    scopus 로고
    • Tight coupling of rubidium conductance and inactivation in human KCNQ1 potassium channels
    • DOI 10.1113/jphysiol.2003.046490
    • G. Seebohm, M.C. Sanguinetti, and M. Pusch Tight coupling of rubidium conductance and inactivation in human KCNQ1 potassium channels J. Physiol. 552 2003 369 378 (Pubitemid 37321836)
    • (2003) Journal of Physiology , vol.552 , Issue.2 , pp. 369-378
    • Seebohm, G.1    Sanguinetti, M.C.2    Pusch, M.3
  • 45
    • 14944352048 scopus 로고    scopus 로고
    • + channels
    • DOI 10.1113/jphysiol.2004.080887
    • G. Seebohm, P. Westenskow, F. Lang, and M.C. Sanguinetti Mutation of colocalized residues of the pore helix and transmembrane segments S5 and S6 disrupt deactivation and modify inactivation of KCNQ1 K+ channels J. Physiol. 563 2005 359 368 (Pubitemid 40360897)
    • (2005) Journal of Physiology , vol.563 , Issue.2 , pp. 359-368
    • Seebohm, G.1    Westenskow, P.2    Lang, F.3    Sanguinetti, M.C.4
  • 46
    • 37649021608 scopus 로고    scopus 로고
    • Global twisting motion of single molecular KcsA potassium channel upon gating
    • H. Shimizu, M. Iwamoto, T. Konno, A. Nihei, Y.C. Sasaki, and S. Oiki Global twisting motion of single molecular KcsA potassium channel upon gating Cell 132 2008 67 78
    • (2008) Cell , vol.132 , pp. 67-78
    • Shimizu, H.1    Iwamoto, M.2    Konno, T.3    Nihei, A.4    Sasaki, Y.C.5    Oiki, S.6
  • 47
    • 33744926664 scopus 로고    scopus 로고
    • Common mechanism of pore opening shared by five different potassium channels
    • DOI 10.1529/biophysj.105.080093
    • I.H. Shrivastava, and I. Bahar Common mechanism of pore opening shared by five different potassium channels Biophys. J. 90 2006 3929 3940 (Pubitemid 43846111)
    • (2006) Biophysical Journal , vol.90 , Issue.11 , pp. 3929-3940
    • Shrivastava, I.H.1    Bahar, I.2
  • 48
    • 37049009981 scopus 로고    scopus 로고
    • Structural models for the KCNQ1 voltage-gated potassium channel
    • DOI 10.1021/bi701597s
    • J.A. Smith, C.G. Vanoye, A.L. George Jr.; J. Meiler, and C.R. Sanders Structural models for the KCNQ1 voltage-gated potassium channel Biochemistry 46 2007 14141 14152 (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
  • 49
    • 57749196006 scopus 로고    scopus 로고
    • Sensing voltage across lipid membranes
    • K.J. Swartz Sensing voltage across lipid membranes Nature 456 2008 891 897
    • (2008) Nature , vol.456 , pp. 891-897
    • Swartz, K.J.1
  • 50
    • 33747840389 scopus 로고    scopus 로고
    • GRAMM-X public web server for protein-protein docking
    • W310-4
    • A. Tovchigrechko, and I.A. Vakser GRAMM-X public web server for protein-protein docking Nucleic Acids Res. 34 Web Server issue 2006 W310-4
    • (2006) Nucleic Acids Res. , vol.34
    • Tovchigrechko, A.1    Vakser, I.A.2
  • 51
    • 0032127234 scopus 로고    scopus 로고
    • + channel (minK) subunits
    • DOI 10.1111/j.1469-7793.1998.037bz.x
    • M. Tristani-Firouzi, and M.C. Sanguinetti Voltage-dependent inactivation of the human K+ channel KvLQT1 is eliminated by association with minimal K+ channel (minK) subunits J. Physiol. 510 1998 37 45 (Pubitemid 28351923)
    • (1998) Journal of Physiology , vol.510 , Issue.1 , pp. 37-45
    • Tristani-Firouzi, M.1    Sanguinetti, M.C.2
  • 52
    • 0043238084 scopus 로고    scopus 로고
    • Dynamical properties of the MscL of Escherichia coli: A normal mode analysis
    • DOI 10.1016/S0022-2836(03)00851-9
    • H. Valadié, J.J. Lacapcre, Y.H. Sanejouand, and C. Etchebest Dynamical properties of the MscL of Escherichia coli: a normal mode analysis J. Mol. Biol. 332 2003 657 674 (Pubitemid 37075988)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.3 , pp. 657-674
    • Valadie, H.1    Lacapcre, J.J.2    Sanejouand, Y.-H.3    Etchebest, C.4
  • 53
    • 79953117902 scopus 로고    scopus 로고
    • Working model for the structural basis for KCNE1 modulation of the KCNQ1 potassium channel
    • W.D. Van Horn, C.G. Vanoye, and C.R. Sanders Working model for the structural basis for KCNE1 modulation of the KCNQ1 potassium channel Curr. Opin. Struct. Biol. 21 2011 283 291
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 283-291
    • Van Horn, W.D.1    Vanoye, C.G.2    Sanders, C.R.3
  • 54
    • 34548861782 scopus 로고    scopus 로고
    • Protein-Protein Docking with Backbone Flexibility
    • DOI 10.1016/j.jmb.2007.07.050, PII S0022283607010030
    • C. Wang, P. Bradley, and D. Baker Protein-protein docking with backbone flexibility J. Mol. Biol. 373 2007 503 519 (Pubitemid 47445567)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.2 , pp. 503-519
    • Wang, C.1    Bradley, P.2    Baker, D.3
  • 55
    • 0032545276 scopus 로고    scopus 로고
    • MinK-KvLQT1 fusion proteins, evidence for multiple stoichiometries of the assembled IsK channel
    • W. Wang, J. Xia, and R.S. Kass MinK-KvLQT1 fusion proteins, evidence for multiple stoichiometries of the assembled IsK channel J. Biol. Chem. 273 1998 34069 34074
    • (1998) J. Biol. Chem. , vol.273 , pp. 34069-34074
    • Wang, W.1    Xia, J.2    Kass, R.S.3
  • 56
    • 79957480803 scopus 로고    scopus 로고
    • Gating-related molecular motions in the extracellular domain of the IKs channel: Implications for IKs channelopathy
    • Y.H. Wang, M. Jiang, X.L. Xu, K.L. Hsu, M. Zhang, and G.N. Tseng Gating-related molecular motions in the extracellular domain of the IKs channel: implications for IKs channelopathy J. Membr. Biol. 239 2011 137 156
    • (2011) J. Membr. Biol. , vol.239 , pp. 137-156
    • Wang, Y.H.1    Jiang, M.2    Xu, X.L.3    Hsu, K.L.4    Zhang, M.5    Tseng, G.N.6
  • 58
    • 1942534554 scopus 로고    scopus 로고
    • Compound Mutations: A Common Cause of Severe Long-QT Syndrome
    • DOI 10.1161/01.CIR.0000125524.34234.13
    • P. Westenskow, I. Splawski, K.W. Timothy, M.T. Keating, and M.C. Sanguinetti Compound mutations: a common cause of severe long-QT syndrome Circulation 109 2004 1834 1841 (Pubitemid 38509116)
    • (2004) Circulation , vol.109 , Issue.15 , pp. 1834-1841
    • Westenskow, P.1    Splawski, I.2    Timothy, K.W.3    Keating, M.T.4    Sanguinetti, M.C.5
  • 59
    • 44349127924 scopus 로고    scopus 로고
    • Ks channel complex make state-dependent contacts in their extracellular domains
    • DOI 10.1085/jgp.200809976
    • X. Xu, M. Jiang, K.L. Hsu, M. Zhang, and G.N. Tseng KCNQ1 and KCNE1 in the IKs channel complex make state-dependent contacts in their extracellular domains J. Gen. Physiol. 131 2008 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
  • 60
    • 77952721198 scopus 로고    scopus 로고
    • Independent and cooperative motions of the Kv1.2 channel: Voltage sensing and gating
    • A. Yeheskel, T. Haliloglu, and N. Ben-Tal Independent and cooperative motions of the Kv1.2 channel: voltage sensing and gating Biophys. J. 98 2010 2179 2188
    • (2010) Biophys. J. , vol.98 , pp. 2179-2188
    • Yeheskel, A.1    Haliloglu, T.2    Ben-Tal, N.3
  • 61
    • 15244344363 scopus 로고    scopus 로고
    • The VGL-chanome: A protein superfamily specialized for electrical signaling and ionic homeostasis
    • F.H. Yu, and W.A. Catterall The VGL-chanome: a protein superfamily specialized for electrical signaling and ionic homeostasis Sci. STKE 2004 2004 re15
    • (2004) Sci. STKE , vol.2004 , pp. 15
    • Yu, F.H.1    Catterall, W.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.