메뉴 건너뛰기




Volumn 141, Issue 2, 2013, Pages 151-160

C-type inactivation of voltage-gated K+ channels: Pore constriction or dilation?

Author keywords

[No Author keywords available]

Indexed keywords

POTASSIUM; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 84874678833     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201210888     Document Type: Note
Times cited : (114)

References (63)
  • 1
    • 0029560754 scopus 로고
    • Episodic ataxia results from voltage-dependent potassium channels with altered functions
    • Adelman, J.P., C.T. Bond, M. Pessia, and J. Maylie. 1995. Episodic ataxia results from voltage-dependent potassium channels with altered functions. Neuron. 15:1449-1454. http://dx.doi.org/10.1016/0896-6273(95)90022-5.
    • (1995) Neuron , vol.15 , pp. 1449-1454
    • Adelman, J.P.1    Bond, C.T.2    Pessia, M.3    Maylie, J.4
  • 2
    • 0018657466 scopus 로고
    • Mechanism of frequency-dependent broadening of molluscan neurone soma spikes
    • Aldrich, R.W., Jr., P.A. Getting, and S.H. Thompson. 1979. Mechanism of frequency-dependent broadening of molluscan neurone soma spikes. J. Physiol. 291:531-544.
    • (1979) J. Physiol , vol.291 , pp. 531-544
    • Aldrich Jr., R.W.1    Getting, P.A.2    Thompson, S.H.3
  • 4
    • 77957245574 scopus 로고    scopus 로고
    • Probing the transition state of the allosteric pathway of the Shaker Kv channel pore by linear free-energy relations
    • Azaria, R., O. Irit, Y. Ben-Abu, and O. Yifrach. 2010. Probing the transition state of the allosteric pathway of the Shaker Kv channel pore by linear free-energy relations. J. Mol. Biol. 403:167-173. http://dx.doi.org/10.1016/j.jmb.2010.08.041.
    • (2010) J. Mol. Biol. , vol.403 , pp. 167-173
    • Azaria, R.1    Irit, O.2    Ben-Abu, Y.3    Yifrach, O.4
  • 5
    • 0028793256 scopus 로고
    • +]: a tale of two inactivation mechanisms
    • +]: a tale of two inactivation mechanisms. Neuron. 15:951-960. http://dx.doi.org/10.1016/0896-6273(95)90185-X.
    • (1995) Neuron , vol.15 , pp. 951-960
    • Baukrowitz, T.1    Yellen, G.2
  • 7
    • 0015424492 scopus 로고
    • Negative conductance caused by entry of sodium and cesium ions into the potassium channels of squid axons
    • Bezanilla, F., and C.M. Armstrong. 1972. Negative conductance caused by entry of sodium and cesium ions into the potassium channels of squid axons. J. Gen. Physiol. 60:588-608. http://dx.doi.org/10.1085/jgp.60.5.588.
    • (1972) J. Gen. Physiol , vol.60 , pp. 588-608
    • Bezanilla, F.1    Armstrong, C.M.2
  • 8
    • 35649011561 scopus 로고    scopus 로고
    • A quantitative description of KcsA gating II: Single-channel currents
    • Chakrapani, S., J.F. Cordero-Morales, and E. Perozo. 2007. A quantitative description of KcsA gating II: Single-channel currents. J. Gen. Physiol. 130:479-496. http://dx.doi.org/10.1085/jgp.200709844.
    • (2007) J. Gen. Physiol , vol.130 , pp. 479-496
    • Chakrapani, S.1    Cordero-Morales, J.F.2    Perozo, E.3
  • 9
    • 0014902326 scopus 로고
    • Sodium and potassium currents in squid axons perfused with fluoride solutions
    • Chandler, W.K., and H. Meves. 1970. Sodium and potassium currents in squid axons perfused with fluoride solutions. J. Physiol. 211:623-652.
    • (1970) J. Physiol , vol.211 , pp. 623-652
    • Chandler, W.K.1    Meves, H.2
  • 11
    • 49649114605 scopus 로고    scopus 로고
    • Protein structure modeling with MODELLER
    • Eswar, N., D. Eramian, B. Webb, M.Y. Shen, and A. Sali. 2008. Protein structure modeling with MODELLER. Methods Mol. Biol. 426:145-159. http://dx.doi.org/10.1007/978-1-60327-058-8_8.
    • (2008) Methods Mol. Biol. , vol.426 , pp. 145-159
    • Eswar, N.1    Eramian, D.2    Webb, B.3    Shen, M.Y.4    Sali, A.5
  • 13
    • 0344717874 scopus 로고    scopus 로고
    • + ions: a remarkably stable non-conducting state produced by membrane depolarizations
    • + solutions lacking K+ ions: a remarkably stable non-conducting state produced by membrane depolarizations. J. Physiol. 499:3-15.
    • (1997) J. Physiol , vol.499 , pp. 3-15
    • Gómez-Lagunas, F.1
  • 14
    • 84859963646 scopus 로고    scopus 로고
    • Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystals
    • USA.
    • Gonzalez-Gutierrez, G., T. Lukk, V. Agarwal, D. Papke, S.K. Nair, and C. Grosman. 2012. Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystals. Proc. Natl. Acad. Sci. USA. 109:6331-6336. http://dx.doi.org/10.1073/pnas.1119268109.
    • (2012) Proc. Natl. Acad. Sci. , vol.109 , pp. 6331-6336
    • Gonzalez-Gutierrez, G.1    Lukk, T.2    Agarwal, V.3    Papke, D.4    Nair, S.K.5    Grosman, C.6
  • 15
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi, T., W.N. Zagotta, and R.W. Aldrich. 1990. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science. 250:533-538. http://dx.doi.org/10.1126/science.2122519.
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 16
    • 0026049511 scopus 로고
    • + channels: effects of alterations in the carboxy-terminal region
    • + channels: effects of alterations in the carboxy-terminal region. Neuron. 7:547-556. http://dx.doi.org/10.1016/0896-6273(91)90367-9.
    • (1991) Neuron , vol.7 , pp. 547-556
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 18
    • 0035936798 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of cardiac arrhythmias
    • Keating, M.T., and M.C. Sanguinetti. 2001. Molecular and cellular mechanisms of cardiac arrhythmias. Cell. 104:569-580. http://dx.doi.org/10.1016/S0092-8674(01)00243-4.
    • (2001) Cell , vol.104 , pp. 569-580
    • Keating, M.T.1    Sanguinetti, M.C.2
  • 19
    • 0031897384 scopus 로고    scopus 로고
    • + at the potassium channel selectivity filter
    • + at the potassium channel selectivity filter. Biophys. J. 74:1840-1849. http://dx.doi.org/10.1016/S0006-3495(98)77894-4.
    • (1998) Biophys. J. , vol.74 , pp. 1840-1849
    • Kiss, L.1    Korn, S.J.2
  • 20
    • 33745216690 scopus 로고    scopus 로고
    • A structural interpretation of voltage-gated potassium channel inactivation
    • Kurata, H.T., and D. Fedida. 2006. A structural interpretation of voltage-gated potassium channel inactivation. Prog. Biophys. Mol. Biol. 92:185-208. http://dx.doi.org/10.1016/j.pbiomolbio.2005.10.001.
    • (2006) Prog. Biophys. Mol. Biol. , vol.92 , pp. 185-208
    • Kurata, H.T.1    Fedida, D.2
  • 21
    • 0033681165 scopus 로고    scopus 로고
    • + channels
    • + channels. Neuron. 27:573-583. http://dx.doi.org/10.1016/S0896-6273(00)00067-2.
    • (2000) Neuron , vol.27 , pp. 573-583
    • Larsson, H.P.1    Elinder, F.2
  • 22
    • 0030071057 scopus 로고    scopus 로고
    • Recovery from C-type inactivation is modulated by extracellular potassium
    • Levy, D.I., and C. Deutsch. 1996. Recovery from C-type inactivation is modulated by extracellular potassium. Biophys. J. 70:798-805. http://dx.doi.org/10.1016/S0006-3495(96)79619-4.
    • (1996) Biophys. J. , vol.70 , pp. 798-805
    • Levy, D.I.1    Deutsch, C.2
  • 23
    • 0029990996 scopus 로고    scopus 로고
    • + channel during gating
    • + channel during gating. Neuron. 16:859-867. http://dx.doi.org/10.1016/S0896-6273(00)80106-3.
    • (1996) Neuron , vol.16 , pp. 859-867
    • Liu, Y.1    Jurman, M.E.2    Yellen, G.3
  • 25
  • 27
    • 0027828292 scopus 로고
    • Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels
    • López-Barneo, J., T. Hoshi, S.H. Heinemann, and R.W. Aldrich. 1993. Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels. Receptors Channels. 1:61-71.
    • (1993) Receptors Channels , vol.1 , pp. 61-71
    • López-Barneo, J.1    Hoshi, T.2    Heinemann, S.H.3    Aldrich, R.W.4
  • 28
    • 0027364807 scopus 로고
    • Functional stoichiometry of Shaker potassium channel inactivation
    • MacKinnon, R., R.W. Aldrich, and A.W. Lee. 1993. Functional stoichiometry of Shaker potassium channel inactivation. Science. 262:757-759. http://dx.doi.org/10.1126/science.7694359.
    • (1993) Science , vol.262 , pp. 757-759
    • MacKinnon, R.1    Aldrich, R.W.2    Lee, A.W.3
  • 29
    • 4644239377 scopus 로고    scopus 로고
    • Metal-substituted derivatives of the rubredoxin from Clostridium pasteurianum
    • Maher, M., M. Cross, M.C. Wilce, J.M. Guss, and A.G. Wedd. 2004. Metal-substituted derivatives of the rubredoxin from Clostridium pasteurianum. Acta Crystallogr. D Biol. Crystallogr. 60:298-303. http://dx.doi.org/10.1107/S090744490302794X.
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 298-303
    • Maher, M.1    Cross, M.2    Wilce, M.C.3    Guss, J.M.4    Wedd, A.G.5
  • 30
    • 0031714063 scopus 로고    scopus 로고
    • + solutions: role of the voltage sensor
    • + solutions: role of the voltage sensor. Biophys. J. 75:1828-1835. http://dx.doi.org/10.1016/S0006-3495(98)77624-6.
    • (1998) Biophys.J. , vol.75 , pp. 1828-1835
    • Melishchuk, A.1    Loboda, A.2    Armstrong, C.M.3
  • 31
    • 0030993829 scopus 로고    scopus 로고
    • + channels distinguish between the sites of tetraethylammonium blockade and C-type inactivation
    • + channels distinguish between the sites of tetraethylammonium blockade and C-type inactivation. J. Physiol. 499:361-367.
    • (1997) J. Physiol , vol.499 , pp. 361-367
    • Molina, A.1    Castellano, A.G.2    López-Barneo, J.3
  • 33
    • 25444529765 scopus 로고    scopus 로고
    • Molecular physiology of cardiac repolarization
    • Nerbonne, J.M., and R.S. Kass. 2005. Molecular physiology of cardiac repolarization. Physiol. Rev. 85:1205-1253. http://dx.doi.org/10.1152/physrev.00002.2005.
    • (2005) Physiol. Rev. , vol.85 , pp. 1205-1253
    • Nerbonne, J.M.1    Kass, R.S.2
  • 34
    • 0032895084 scopus 로고    scopus 로고
    • Functional consequences of a decreased potassium affinity in a potassium channel pore. Ion interactions and C-type inactivation
    • Ogielska, E.M., and R.W. Aldrich. 1999. Functional consequences of a decreased potassium affinity in a potassium channel pore. Ion interactions and C-type inactivation. J. Gen. Physiol. 113:347-358. http://dx.doi.org/10.1085/jgp.113.2.347.
    • (1999) J. Gen. Physiol , vol.113 , pp. 347-358
    • Ogielska, E.M.1    Aldrich, R.W.2
  • 35
    • 0028822993 scopus 로고
    • Cooperative subunit interactions in C-type inactivation of K channels
    • Ogielska, E.M., W.N. Zagotta, T. Hoshi, S.H. Heinemann, J. Haab, and R.W. Aldrich. 1995. Cooperative subunit interactions in C-type inactivation of K channels. Biophys. J. 69:2449-2457. http://dx.doi.org/10.1016/S0006-3495(95)80114-1.
    • (1995) Biophys.J. , vol.69 , pp. 2449-2457
    • Ogielska, E.M.1    Zagotta, W.N.2    Hoshi, T.3    Heinemann, S.H.4    Haab, J.5    Aldrich, R.W.6
  • 37
    • 84855505933 scopus 로고    scopus 로고
    • Thermodynamic coupling between activation and inactivation gating in potassium channels revealed by free energy molecular dynamics simulations
    • Pan, A.C., L.G. Cuello, E. Perozo, and B. Roux. 2011. Thermodynamic coupling between activation and inactivation gating in potassium channels revealed by free energy molecular dynamics simulations. J. Gen. Physiol. 138:571-580. http://dx.doi.org/10.1085/jgp.201110670.
    • (2011) J. Gen. Physiol , vol.138 , pp. 571-580
    • Pan, A.C.1    Cuello, L.G.2    Perozo, E.3    Roux, B.4
  • 38
    • 0029145067 scopus 로고
    • + channel occurs by a cooperative mechanism
    • + channel occurs by a cooperative mechanism. Biophys. J. 69:896-903. http://dx.doi.org/10.1016/S0006-3495 (95)79963-5.
    • (1995) Biophys.J. , vol.69 , pp. 896-903
    • Panyi, G.1    Sheng, Z.2    Deutsch, C.3
  • 42
    • 33746660275 scopus 로고    scopus 로고
    • A trapped intracellular cation modulates K+ channel recovery from slow inactivation
    • Ray, E.C., and C. Deutsch. 2006. A trapped intracellular cation modulates K+ channel recovery from slow inactivation. J. Gen. Physiol. 128:203-217. http://dx.doi.org/10.1085/jgp.200609561.
    • (2006) J. Gen. Physiol , vol.128 , pp. 203-217
    • Ray, E.C.1    Deutsch, C.2
  • 47
    • 33645317063 scopus 로고    scopus 로고
    • hERG potassium channels and cardiac arrhythmia
    • Sanguinetti, M.C., and M. Tristani-Firouzi. 2006. hERG potassium channels and cardiac arrhythmia. Nature. 440:463-469. http://dx.doi.org/10.1038/nature04710.
    • (2006) Nature , vol.440 , pp. 463-469
    • Sanguinetti, M.C.1    Tristani-Firouzi, M.2
  • 48
    • 0029939954 scopus 로고    scopus 로고
    • Modification of C-type inactivating Shaker potassium channels by chloramine- T
    • Schlief, T., R. Schönherr, and S.H. Heinemann. 1996. Modification of C-type inactivating Shaker potassium channels by chloramine- T. Pflügers Arch. 431:483-493. http://dx.doi.org/10.1007/BF02191894.
    • (1996) Pflügers Arch , vol.431 , pp. 483-493
    • Schlief, T.1    Schönherr, R.2    Heinemann, S.H.3
  • 49
    • 0030054878 scopus 로고    scopus 로고
    • Molecular determinants for activation and inactivation of HERG, a human inward rectifier potassium channel
    • Schönherr, R., and S.H. Heinemann. 1996. Molecular determinants for activation and inactivation of HERG, a human inward rectifier potassium channel. J. Physiol. 493:635-642.
    • (1996) J. Physiol , vol.493 , pp. 635-642
    • Schönherr, R.1    Heinemann, S.H.2
  • 50
    • 0031952461 scopus 로고    scopus 로고
    • Activation of Shaker potassium channels. III. An activation gating model for wild-type and V2 mutant channels
    • Schoppa, N.E., and F.J. Sigworth. 1998. Activation of Shaker potassium channels. III. An activation gating model for wild-type and V2 mutant channels. J. Gen. Physiol. 111:313-342. http://dx.doi.org/10.1085/jgp.111.2.313.
    • (1998) J. Gen. Physiol , vol.111 , pp. 313-342
    • Schoppa, N.E.1    Sigworth, F.J.2
  • 51
    • 0030025308 scopus 로고    scopus 로고
    • The inward rectification mechanism of the HERG cardiac potassium channel
    • Smith, P.L., T. Baukrowitz, and G. Yellen. 1996. The inward rectification mechanism of the HERG cardiac potassium channel. Nature. 379:833-836. http://dx.doi.org/10.1038/379833a0.
    • (1996) Nature , vol.379 , pp. 833-836
    • Smith, P.L.1    Baukrowitz, T.2    Yellen, G.3
  • 52
  • 53
    • 0030706134 scopus 로고    scopus 로고
    • Ion conduction through C-type inactivated Shaker channels
    • Starkus, J.G., L. Kuschel, M.D. Rayner, and S.H. Heinemann. 1997. Ion conduction through C-type inactivated Shaker channels. J. Gen. Physiol. 110:539-550. http://dx.doi.org/10.1085/jgp.110.5.539.
    • (1997) J. Gen. Physiol , vol.110 , pp. 539-550
    • Starkus, J.G.1    Kuschel, L.2    Rayner, M.D.3    Heinemann, S.H.4
  • 54
    • 0031823743 scopus 로고    scopus 로고
    • Macroscopic Na+ currents in the "nonconducting" Shaker potassium channel mutant W434F
    • Starkus, J.G., L. Kuschel, M.D. Rayner, and S.H. Heinemann. 1998. Macroscopic Na+ currents in the "nonconducting" Shaker potassium channel mutant W434F. J. Gen. Physiol. 112:85-93. http://dx.doi.org/10.1085/jgp.112.1.85.
    • (1998) J. Gen. Physiol , vol.112 , pp. 85-93
    • Starkus, J.G.1    Kuschel, L.2    Rayner, M.D.3    Heinemann, S.H.4
  • 55
    • 0024285845 scopus 로고
    • Expression of functional potassium channels from Shaker cDNA in Xenopus oocytes
    • Timpe, L.C., T.L. Schwarz, B.L. Tempel, D.M. Papazian, Y.N. Jan, and L.Y. Jan. 1988. Expression of functional potassium channels from Shaker cDNA in Xenopus oocytes. Nature. 331:143-145. http://dx.doi.org/10.1038/331143a0.
    • (1988) Nature , vol.331 , pp. 143-145
    • Timpe, L.C.1    Schwarz, T.L.2    Tempel, B.L.3    Papazian, D.M.4    Jan, Y.N.5    Jan, L.Y.6
  • 56
    • 0030906796 scopus 로고    scopus 로고
    • How does the W434F mutation block current in Shaker potassium channels? J
    • Yang, Y., Y. Yan, and F.J. Sigworth. 1997. How does the W434F mutation block current in Shaker potassium channels? J. Gen. Physiol. 109:779-789. http://dx.doi.org/10.1085/jgp.109.6.779.
    • (1997) Gen. Physiol , vol.109 , pp. 779-789
    • Yang, Y.1    Yan, Y.2    Sigworth, F.J.3
  • 58
    • 0032417420 scopus 로고    scopus 로고
    • The moving parts of voltage-gated ion channels
    • Yellen, G. 1998. The moving parts of voltage-gated ion channels. Q. Rev. Biophys. 31:239-295. http://dx.doi.org/10.1017/S0033583598003448.
    • (1998) Q. Rev. Biophys , vol.31 , pp. 239-295
    • Yellen, G.1
  • 59
    • 0028297301 scopus 로고
    • An engineered cysteine in the external mouth of a K+ channel allows inactivation to be modulated by metal binding
    • Yellen, G., D. Sodickson, T.Y. Chen, and M.E. Jurman. 1994. An engineered cysteine in the external mouth of a K+ channel allows inactivation to be modulated by metal binding. Biophys. J. 66:1068-1075. http://dx.doi.org/10.1016/S0006-3495(94)80888-4.
    • (1994) Biophys.J. , vol.66 , pp. 1068-1075
    • Yellen, G.1    Sodickson, D.2    Chen, T.Y.3    Jurman, M.E.4
  • 60
    • 1842317695 scopus 로고
    • Gating of single Shaker potassium channels in Drosophila muscle and in Xenopus oocytes injected with Shaker mRNA
    • USA.
    • Zagotta, W.N., T. Hoshi, and R.W. Aldrich. 1989. Gating of single Shaker potassium channels in Drosophila muscle and in Xenopus oocytes injected with Shaker mRNA. Proc. Natl. Acad. Sci. USA. 86:7243-7247. http://dx.doi.org/10.1073/pnas.86.18.7243.
    • (1989) Proc. Natl. Acad. Sci. , vol.86 , pp. 7243-7247
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, R.W.3
  • 61
    • 0028140472 scopus 로고
    • Shaker potassium channel gating. III: Evaluation of kinetic models for activation
    • Zagotta, W.N., T. Hoshi, and R.W. Aldrich. 1994. Shaker potassium channel gating. III: Evaluation of kinetic models for activation. J. Gen. Physiol. 103:321-362. http://dx.doi.org/10.1085/jgp.103.2.321.
    • (1994) J. Gen. Physiol , vol.103 , pp. 321-362
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, R.W.3
  • 62
    • 0035822048 scopus 로고    scopus 로고
    • Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors
    • Zhou, M., J.H. Morais-Cabral, S. Mann, and R. MacKinnon. 2001. Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors. Nature. 411:657-661. http://dx.doi.org/10.1038/35079500.
    • (2001) Nature , vol.411 , pp. 657-661
    • Zhou, M.1    Morais-Cabral, J.H.2    Mann, S.3    MacKinnon, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.