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Volumn 288, Issue 14, 2013, Pages 9686-9695

Fine-tuning of voltage sensitivity of the Kv1.2 potassium channel by interhelix loop dynamics

Author keywords

[No Author keywords available]

Indexed keywords

COVALENT INTERACTIONS; FUNCTIONAL CONFORMATIONS; MOLECULAR DYNAMICS SIMULATIONS; NON-COVALENT INTERACTION; TRANSMEMBRANE HELICES; TRANSMEMBRANE VOLTAGE; VOLTAGE GATED ION CHANNELS; VOLTAGE-GATED POTASSIUM CHANNELS;

EID: 84875983028     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.437483     Document Type: Article
Times cited : (12)

References (47)
  • 1
    • 0003443746 scopus 로고    scopus 로고
    • 3rd Ed., Sinauer Associates, Inc., Sunderland, MA
    • Hille, B. (2001) Ionic Channels of Excitable Membranes, 3rd Ed., pp. 131-149, Sinauer Associates, Inc., Sunderland, MA
    • (2001) Ionic Channels of Excitable Membranes , pp. 131-149
    • Hille, B.1
  • 2
    • 41149095488 scopus 로고    scopus 로고
    • How membrane proteins sense voltage
    • Bezanilla, F. (2008) How membrane proteins sense voltage. Nat. Rev. Mol. Cell Biol. 9, 323-332
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 323-332
    • Bezanilla, F.1
  • 4
    • 27344442574 scopus 로고    scopus 로고
    • Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane
    • Lee, S. Y., Lee, A., Chen, J., and MacKinnon, R. (2005) Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane. Proc. Natl. Acad. Sci. U.S.A. 102, 15441-15446
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15441-15446
    • Lee, S.Y.1    Lee, A.2    Chen, J.3    Mackinnon, R.4
  • 5
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long, S. B., Campbell, E. B., and Mackinnon, R. (2005) Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309, 897-903
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 8
    • 36248982122 scopus 로고    scopus 로고
    • Atomic structure of a voltage-dependent K(+) channel in a lipid membrane-like environment
    • Long, S. B., Tao, X., Campbell, E. B., and MacKinnon, R. (2007) Atomic structure of a voltage-dependent K(+) channel in a lipid membrane-like environment. Nature 450, 376-382
    • (2007) Nature , vol.450 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    Mackinnon, R.4
  • 10
    • 0028998041 scopus 로고
    • Electrostatic interactions of S4 voltage sensor in Shaker K+ channel
    • Papazian, D. M., Shao, X. M., Seoh, S. A., Mock, A. F., Huang, Y., and Wainstock, D. H. (1995) Electrostatic interactions of S4 voltage sensor in Shaker K+ channel. Neuron 14, 1293-1301
    • (1995) Neuron , vol.14 , pp. 1293-1301
    • Papazian, D.M.1    Shao, X.M.2    Seoh, S.A.3    Mock, A.F.4    Huang, Y.5    Wainstock, D.H.6
  • 12
    • 0028014591 scopus 로고
    • Shaker potassium channel gating. I: Transitions near the open state
    • Hoshi, T., Zagotta, W. N., and Aldrich, R. W. (1994) Shaker potassium channel gating. I: Transitions near the open state. J. Gen. Physiol. 103, 249-278
    • (1994) J. Gen. Physiol. , vol.103 , pp. 249-278
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 13
    • 0031952460 scopus 로고    scopus 로고
    • Activation of Shaker potassium channels. II. Kinetics of the V2 mutant channel
    • Schoppa, N. E., and Sigworth, F. J. (1998) Activation of Shaker potassium channels. II. Kinetics of the V2 mutant channel. J. Gen. Physiol. 111, 295-311
    • (1998) J. Gen. Physiol. , vol.111 , pp. 295-311
    • Schoppa, N.E.1    Sigworth, F.J.2
  • 14
    • 0028085276 scopus 로고
    • Shaker potassium channel gating. II: Transitions in the activation pathway
    • Zagotta, W. N., Hoshi, T., Dittman, J., and Aldrich, R. W. (1994) Shaker potassium channel gating. II: Transitions in the activation pathway. J. Gen. Physiol. 103, 279-319
    • (1994) J. Gen. Physiol. , vol.103 , pp. 279-319
    • Zagotta, W.N.1    Hoshi, T.2    Dittman, J.3    Aldrich, R.W.4
  • 15
    • 79954991393 scopus 로고    scopus 로고
    • Intermediate states of the Kv1.2 voltage sensor from atomistic molecular dynamics simulations
    • Delemotte, L., Tarek, M., Klein, M. L., Amaral, C., and Treptow, W. (2011) Intermediate states of the Kv1.2 voltage sensor from atomistic molecular dynamics simulations. Proc. Natl. Acad. Sci. U.S.A. 108, 6109-6114
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 6109-6114
    • Delemotte, L.1    Tarek, M.2    Klein, M.L.3    Amaral, C.4    Treptow, W.5
  • 17
    • 34547628129 scopus 로고    scopus 로고
    • Dynamics of the kv1.2 voltage-gated k+ channel in a membrane environment
    • Jogini, V., and Roux, B. (2007) Dynamics of the kv1.2 voltage-gated k+ channel in a membrane environment. Biophys. J. 93, 3070-3082
    • (2007) Biophys. J. , vol.93 , pp. 3070-3082
    • Jogini, V.1    Roux, B.2
  • 23
    • 33845637597 scopus 로고    scopus 로고
    • Phospholipids and the origin of cationic gating charges in voltage sensors
    • Schmidt, D., Jiang, Q. X., and MacKinnon, R. (2006) Phospholipids and the origin of cationic gating charges in voltage sensors. Nature 444, 775-779
    • (2006) Nature , vol.444 , pp. 775-779
    • Schmidt, D.1    Jiang, Q.X.2    Mackinnon, R.3
  • 24
    • 39149109885 scopus 로고    scopus 로고
    • Removal of phospho-head groups of membrane lipids immobilizes voltage sensors of K+ channels
    • Xu, Y., Ramu, Y., and Lu, Z. (2008) Removal of phospho-head groups of membrane lipids immobilizes voltage sensors of K+ channels. Nature 451, 826-829
    • (2008) Nature , vol.451 , pp. 826-829
    • Xu, Y.1    Ramu, Y.2    Lu, Z.3
  • 26
    • 0030893809 scopus 로고    scopus 로고
    • Electrostatic interactions between transmembrane segments mediate folding of Shaker K+ channel subunits
    • Tiwari-Woodruff, S. K., Schulteis, C. T., Mock, A. F., and Papazian, D. M. (1997) Electrostatic interactions between transmembrane segments mediate folding of Shaker K+ channel subunits. Biophys. J. 72, 1489-1500
    • (1997) Biophys. J. , vol.72 , pp. 1489-1500
    • Tiwari-Woodruff, S.K.1    Schulteis, C.T.2    Mock, A.F.3    Papazian, D.M.4
  • 27
    • 55549144756 scopus 로고    scopus 로고
    • Non-linear intramolecular interactions and voltage sensitivity of a KV1 family potassium channel from Polyorchis penicillatus (Eschscholtz 1829)
    • Klassen, T. L., O'Mara, M. L., Redstone, M., Spencer, A. N., and Gallin, W. J. (2008) Non-linear intramolecular interactions and voltage sensitivity of a KV1 family potassium channel from Polyorchis penicillatus (Eschscholtz 1829). J. Exp. Biol. 211, 3442-3453
    • (2008) J. Exp. Biol. , vol.211 , pp. 3442-3453
    • Klassen, T.L.1    O'Mara, M.L.2    Redstone, M.3    Spencer, A.N.4    Gallin, W.J.5
  • 28
    • 0033823077 scopus 로고    scopus 로고
    • Modulation of the Shaker K(+) channel gating kinetics by the S3-S4 linker
    • Gonzalez, C., Rosenman, E., Bezanilla, F., Alvarez, O., and Latorre, R. (2000) Modulation of the Shaker K(+) channel gating kinetics by the S3-S4 linker. J. Gen. Physiol. 115, 193-208
    • (2000) J. Gen. Physiol. , vol.115 , pp. 193-208
    • Gonzalez, C.1    Rosenman, E.2    Bezanilla, F.3    Alvarez, O.4    Latorre, R.5
  • 29
    • 0035859893 scopus 로고    scopus 로고
    • Periodic perturbations in Shaker K+ channel gating kinetics by deletions in the S3-S4 linker
    • Gonzalez, C., Rosenman, E., Bezanilla, F., Alvarez, O., and Latorre, R. (2001) Periodic perturbations in Shaker K+ channel gating kinetics by deletions in the S3-S4 linker. Proc. Natl. Acad. Sci. U.S.A. 98, 9617-9623
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 9617-9623
    • Gonzalez, C.1    Rosenman, E.2    Bezanilla, F.3    Alvarez, O.4    Latorre, R.5
  • 30
    • 0029152786 scopus 로고
    • Role of glycogen synthase kinase 3 beta as a negative regulator of dorsoventral axis formation in Xenopus embryos
    • Dominguez, I., Itoh, K., and Sokol, S. Y. (1995) Role of glycogen synthase kinase 3 beta as a negative regulator of dorsoventral axis formation in Xenopus embryos. Proc. Natl. Acad. Sci. U.S.A. 92, 8498-8502
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8498-8502
    • Dominguez, I.1    Itoh, K.2    Sokol, S.Y.3
  • 31
    • 0032826459 scopus 로고    scopus 로고
    • Two-microelectrode voltage clamp of Xenopus oocytes: Voltage errors and compensation for local current flow
    • Baumgartner, W., Islas, L., and Sigworth, F. J. (1999) Two-microelectrode voltage clamp of Xenopus oocytes: voltage errors and compensation for local current flow. Biophys. J. 77, 1980-1991
    • (1999) Biophys. J. , vol.77 , pp. 1980-1991
    • Baumgartner, W.1    Islas, L.2    Sigworth, F.J.3
  • 32
    • 0032870377 scopus 로고    scopus 로고
    • Modulation of jellyfish potassium channels by external potassium ions
    • Grigoriev, N. G., Spafford, J. D., and Spencer, A. N. (1999) Modulation of jellyfish potassium channels by external potassium ions. J. Neurophysiol. 82, 1728-1739
    • (1999) J. Neurophysiol. , vol.82 , pp. 1728-1739
    • Grigoriev, N.G.1    Spafford, J.D.2    Spencer, A.N.3
  • 33
    • 0027305423 scopus 로고
    • Functional expression of Na(+)-dependent nucleoside transport systems of rat intestine in isolated oocytes of Xenopus laevis. Demonstration that rat jejunum expresses the purine-selective system N1 (cif) and a second, novel system N3 having broad specificity for purine and pyrimidine nucleosides
    • Huang, Q. Q., Harvey, C. M., Paterson, A. R., Cass, C. E., and Young, J. D. (1993) Functional expression of Na(+)-dependent nucleoside transport systems of rat intestine in isolated oocytes of Xenopus laevis. Demonstration that rat jejunum expresses the purine-selective system N1 (cif) and a second, novel system N3 having broad specificity for purine and pyrimidine nucleosides. J. Biol. Chem. 268, 20613-20619
    • (1993) J. Biol. Chem. , vol.268 , pp. 20613-20619
    • Huang, Q.Q.1    Harvey, C.M.2    Paterson, A.R.3    Cass, C.E.4    Young, J.D.5
  • 34
    • 0021646375 scopus 로고
    • Chloride current induced by injection of calcium into Xenopus oocytes
    • Miledi, R., and Parker, I. (1984) Chloride current induced by injection of calcium into Xenopus oocytes. J. Physiol. 357, 173-183
    • (1984) J. Physiol. , vol.357 , pp. 173-183
    • Miledi, R.1    Parker, I.2
  • 35
    • 80052189786 scopus 로고    scopus 로고
    • JShaw1, a low-threshold, fast-activating Kv3 from the hydrozoan jellyfish Polyorchis penicillatus
    • Sand, R. M., Atherton, D. M., Spencer, A. N., and Gallin, W. J. (2011) jShaw1, a low-threshold, fast-activating Kv3 from the hydrozoan jellyfish Polyorchis penicillatus. The J. Exp. Biol. 214, 3124-3137
    • (2011) The J. Exp. Biol. , vol.214 , pp. 3124-3137
    • Sand, R.M.1    Atherton, D.M.2    Spencer, A.N.3    Gallin, W.J.4
  • 36
    • 35649001607 scopus 로고
    • A quantitative description of membrane current and its application to conduction and excitation in nerve
    • Hodgkin, A. L., and Huxley, A. F. (1952) A quantitative description of membrane current and its application to conduction and excitation in nerve. J. Physiol. 117, 500-544
    • (1952) J. Physiol. , vol.117 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 37
    • 77954895219 scopus 로고    scopus 로고
    • Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based x-ray crystallographic refinement
    • Chen, X., Wang, Q., Ni, F., and Ma, J. (2010) Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based x-ray crystallographic refinement. Proc. Natl. Acad. Sci. U.S.A. 107, 11352-11357
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 11352-11357
    • Chen, X.1    Wang, Q.2    Ni, F.3    Ma, J.4
  • 40
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., Kutzner, C., van der Spoel, D., and Lindahl, E. (2008) GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 41
    • 5244304444 scopus 로고
    • Efficient estimation of free-energy differences from Monte-Carlo data
    • Bennett, C. H. (1976) Efficient Estimation of Free-Energy Differences from Monte-Carlo Data. J. Comput. Phys. 22, 245-268
    • (1976) J. Comput. Phys. , vol.22 , pp. 245-268
    • Bennett, C.H.1
  • 44
    • 0042736856 scopus 로고    scopus 로고
    • Allosteric switching by mutually exclusive folding of protein domains
    • Radley, T. L., Markowska, A. I., Bettinger, B. T., Ha, J. H., and Loh, S. N. (2003) Allosteric switching by mutually exclusive folding of protein domains. J. Mol. Biol. 332, 529-536
    • (2003) J. Mol. Biol. , vol.332 , pp. 529-536
    • Radley, T.L.1    Markowska, A.I.2    Bettinger, B.T.3    Ha, J.H.4    Loh, S.N.5
  • 45
    • 77955626630 scopus 로고    scopus 로고
    • A shaker K+ channel with a miniature engineered voltage sensor
    • Xu, Y., Ramu, Y., and Lu, Z. (2010) A shaker K+ channel with a miniature engineered voltage sensor. Cell 142, 580-589
    • (2010) Cell , vol.142 , pp. 580-589
    • Xu, Y.1    Ramu, Y.2    Lu, Z.3
  • 46
  • 47
    • 79960189344 scopus 로고    scopus 로고
    • Dynamic allostery: Linkers are not merely flexible
    • Ma, B., Tsai, C. J., Halilogl, T., and Nussinov, R. (2011) Dynamic allostery: linkers are not merely flexible. Structure 19, 907-917
    • (2011) Structure , vol.19 , pp. 907-917
    • Ma, B.1    Tsai, C.J.2    Halilogl, T.3    Nussinov, R.4


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