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Journal of General Physiology
Volumn 140, Issue 5, 2012, Pages 513-527
Modeling-independent elucidation of inactivation pathways in recombinant and native A-type Kv channels
Author keywords

[No Author keywords available]
Indexed keywords

KV3.4 PROTEIN, RAT; RECOMBINANT PROTEIN; SHAL POTASSIUM CHANNEL; SHAW POTASSIUM CHANNEL;
EID: 84870800619     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201210869     Document Type: Article
Times cited : (21)
References (54)
  • 1
    • 0021000963 scopus 로고
    • Inactivation of open and closed sodium channels determined separately
    • Aldrich, R.W., and C.F. Stevens. 1983. Inactivation of open and closed sodium channels determined separately. Cold Spring Harb. Symp. Quant. Biol. 48:147-153. http://dx.doi.org/10.1101/SQB .1983.048.01.017
    • (1983) Cold Spring Harb. Symp. Quant. Biol. , vol.48 , pp. 147-153
    • Aldrich, R.W.1    Stevens, C.F.2
  • 3
    • 33845212088 scopus 로고    scopus 로고
    • Na channel inactivation from open and closed states
    • Armstrong, C.M. 2006. Na channel inactivation from open and closed states. Proc. Natl. Acad. Sci. USA. 103:17991-17996. http://dx.doi .org/10.1073/pnas.0607603103
    • (2006) Proc. Natl. Acad. Sci. USA. , vol.103 , pp. 17991-17996
    • Armstrong, C.M.1
  • 5
    • 79251536515 scopus 로고    scopus 로고
    • Mechanisms of closed-state inactivation in voltage-gated ion channels
    • Bähring, R., and M. Covarrubias. 2011. Mechanisms of closed-state inactivation in voltage-gated ion channels. J. Physiol. 589:461-479. http://dx.doi.org/10.1113/jphysiol.2010.191965
    • (2011) J. Physiol. , vol.589 , pp. 461-479
    • Bähring, R.1    Covarrubias, M.2
  • 6
    • 0035881095 scopus 로고    scopus 로고
    • Kinetic analysis of open- and closed-state inactivation transitions in human Kv4 2 A-type potassium channels
    • Bähring, R., L.M. Boland, A. Varghese, M. Gebauer, and O. Pongs. 2001. Kinetic analysis of open- and closed-state inactivation transitions in human Kv4.2 A-type potassium channels. J. Physiol. 535:65- 81. http://dx.doi.org/10.1111/j.1469-7793.2001.00065.x
    • (2001) J. Physiol. , vol.535 , pp. 65-81
    • Bähring, R.1    Boland, L.M.2    Varghese, A.3    Gebauer, M.4    Pongs, O.5
  • 7
    • 62349098199 scopus 로고    scopus 로고
    • Dynamic coupling of voltage sensor and gate involved in closed-state inactivation of Kv4 2 channels
    • Barghaan, J., and R. Bähring. 2009. Dynamic coupling of voltage sensor and gate involved in closed-state inactivation of Kv4.2 channels. J. Gen. Physiol. 133:205-224. http://dx.doi.org/10.1085/ jgp.200810073
    • (2009) J. Gen. Physiol. , vol.133 , pp. 205-224
    • Barghaan, J.1    Bähring, R.2
  • 8
    • 38949143719 scopus 로고    scopus 로고
    • Role of N-terminal domain and accessory subunits in controlling deactivation-inactivation coupling of Kv4 2 channels
    • Barghaan, J., M. Tozakidou, H. Ehmke, and R. Bähring. 2008. Role of N-terminal domain and accessory subunits in controlling deactivation-inactivation coupling of Kv4.2 channels. Biophys. J. 94:1276-1294. http://dx.doi.org/10.1529/biophysj.107.111344
    • (2008) Biophys. J. , vol.94 , pp. 1276-1294
    • Barghaan, J.1    Tozakidou, M.2    Ehmke, H.3    Bähring, R.4
  • 9
    • 0019416806 scopus 로고
    • Sodium channel inactivation in the crayfish giant axon Must channels open before inactivating?
    • Bean, B.P. 1981. Sodium channel inactivation in the crayfish giant axon. Must channels open before inactivating? Biophys. J. 35:595- 614. http://dx.doi.org/10.1016/S0006-3495(81)84815-1
    • (1981) Biophys. J. , vol.35 , pp. 595-614
    • Bean, B.P.1
  • 10
    • 0034902244 scopus 로고    scopus 로고
    • Kv4 channels exhibit modulation of closed-state inactivation in inside-out patches
    • Beck, E.J., and M. Covarrubias. 2001. Kv4 channels exhibit modulation of closed-state inactivation in inside-out patches. Biophys. J. 81:867-883. http://dx.doi.org/10.1016/S0006-3495(01)75747-5
    • (2001) Biophys. J. , vol.81 , pp. 867-883
    • Beck, E.J.1    Covarrubias, M.2
  • 11
    • 0036487139 scopus 로고    scopus 로고
    • Remodelling inactivation gating of Kv4 channels by KChIP1, a small-molecular-weight calcium-binding protein
    • Beck, E.J., M. Bowlby, W.F. An, K.J. Rhodes, and M. Covarrubias. 2002. Remodelling inactivation gating of Kv4 channels by KChIP1, a small-molecular-weight calcium-binding protein. J. Physiol. 538:691-706. http://dx.doi.org/10.1113/jphysiol.2001.013127
    • (2002) J. Physiol. , vol.538 , pp. 691-706
    • Beck, E.J.1    Bowlby, M.2    An, W.F.3    Rhodes, K.J.4    Covarrubias, M.5
  • 15
    • 52049105218 scopus 로고    scopus 로고
    • Protein kinase C modulates inactivation of Kv3 3 channels
    • Desai, R., J. Kronengold, J. Mei, S.A. Forman, and L.K. Kaczmarek. 2008. Protein kinase C modulates inactivation of Kv3.3 channels. J. Biol. Chem. 283:22283-22294. http://dx.doi.org/10.1074/jbc .M801663200
    • (2008) J. Biol. Chem. , vol.283 , pp. 22283-22294
    • Desai, R.1    Kronengold, J.2    Mei, J.3    Forman, S.A.4    Kaczmarek, L.K.5
  • 16
    • 33751547752 scopus 로고    scopus 로고
    • A dipeptidyl aminopeptidase- like protein remodels gating charge dynamics in Kv4 2 channels
    • Dougherty, K., and M. Covarrubias. 2006. A dipeptidyl aminopeptidase- like protein remodels gating charge dynamics in Kv4.2 channels. J. Gen. Physiol. 128:745-753. http://dx.doi.org/10.1085/ jgp.200609668
    • (2006) J. Gen. Physiol. , vol.128 , pp. 745-753
    • Dougherty, K.1    Covarrubias, M.2
  • 17
    • 40849114753 scopus 로고    scopus 로고
    • Gating charge immobilization in Kv4 2 channels: the basis of closed-state inactivation
    • Dougherty, K., J.A. De Santiago-Castillo, and M. Covarrubias. 2008. Gating charge immobilization in Kv4.2 channels: the basis of closed-state inactivation. J. Gen. Physiol. 131:257-273. http://dx.doi .org/10.1085/jgp.200709938
    • (2008) J. Gen. Physiol. , vol.131 , pp. 257-273
    • Dougherty, K.1    De Santiago-Castillo, J.A.2    Covarrubias, M.3
  • 18
    • 0003443746 scopus 로고    scopus 로고
    • Third Edition. Sinauer Associates, Inc., Sunderland, MA
    • Hille, B. 2001. Ion Channels of Excitable Membranes. Third Edition. Sinauer Associates, Inc., Sunderland, MA. 814 pp.
    • (2001) Ion Channels of Excitable Membranes , pp. 814
    • Hille, B.1
  • 19
    • 0031571202 scopus 로고    scopus 로고
    • The NEURON simulation environment
    • Hines, M.L., and N.T. Carnevale. 1997. The NEURON simulation environment. Neural Comput. 9:1179-1209. http://dx.doi.org/ 10.1162/neco.1997.9.6.1179
    • (1997) Neural Comput , vol.9 , pp. 1179-1209
    • Hines, M.L.1    Carnevale, N.T.2
  • 20
    • 0030855840 scopus 로고    scopus 로고
    • + channel regulation of signal propagation in dendrites of hippocampal pyramidal neurons
    • + channel regulation of signal propagation in dendrites of hippocampal pyramidal neurons. Nature. 387:869-875.
    • (1997) Nature , vol.387 , pp. 869-875
    • Hoffman, D.A.1    Magee, J.C.2    Colbert, C.M.3    Johnston, D.4
  • 21
    • 0019463825 scopus 로고
    • Sodium channels need not open before they inactivate
    • Horn, R., J. Patlak, and C.F. Stevens. 1981. Sodium channels need not open before they inactivate. Nature. 291:426-427. http://dx .doi.org/10.1038/291426a0
    • (1981) Nature , vol.291 , pp. 426-427
    • Horn, R.1    Patlak, J.2    Stevens, C.F.3
  • 22
    • 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
  • 23
    • 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
  • 24
    • 33646014745 scopus 로고    scopus 로고
    • I.V.The Kv4 2 potassium channel subunit is required for pain plasticity
    • Hu, H.-J., Y. Carrasquillo, F. Karim, W.E. Jung, J.M. Nerbonne, T.L. Schwarz, and R.W. Gereau IV. 2006. The Kv4.2 potassium channel subunit is required for pain plasticity. Neuron. 50:89-100. http:// dx.doi.org/10.1016/j.neuron.2006.03.010
    • (2006) Neuron , vol.50 , pp. 89-100
    • Hu, H.-J.1    Carrasquillo, Y.2    Karim, F.3    Jung, W.E.4    Nerbonne, J.M.5    Schwarz, T.L.6    Gereau, R.W.7
  • 25
    • 9144260644 scopus 로고    scopus 로고
    • Molecular physiology and modulation of somatodendritic A-type potassium channels
    • Jerng, H.H., P.J. Pfaffinger, and M. Covarrubias. 2004. Molecular physiology and modulation of somatodendritic A-type potassium channels. Mol. Cell. Neurosci. 27:343-369. http://dx.doi.org/10.1016/j.mcn.2004.06.011
    • (2004) Mol. Cell. Neurosci. , vol.27 , pp. 343-369
    • Jerng, H.H.1    Pfaffinger, P.J.2    Covarrubias, M.3
  • 26
    • 27844446627 scopus 로고    scopus 로고
    • Multiprotein assembly of Kv4.2 KChIP3 and DPP10 produces ternary channel complexes with ISA-like properties
    • Jerng, H.H., K. Kunjilwar, and P.J. Pfaffinger. 2005. Multiprotein assembly of Kv4.2, KChIP3 and DPP10 produces ternary channel complexes with ISA-like properties. J. Physiol. 568:767-788. http:// dx.doi.org/10.1113/jphysiol.2005.087858
    • (2005) J. Physiol. , vol.568 , pp. 767-788
    • Jerng, H.H.1    Kunjilwar, K.2    Pfaffinger, P.J.3
  • 27
    • 34547493445 scopus 로고    scopus 로고
    • DPP10 splice variants are localized in distinct neuronal populations and act to differentially regulate the inactivation properties of Kv4-based ion channels
    • Jerng, H.H., A.D. Lauver, and P.J. Pfaffinger. 2007. DPP10 splice variants are localized in distinct neuronal populations and act to differentially regulate the inactivation properties of Kv4-based ion channels. Mol. Cell. Neurosci. 35:604-624. http://dx.doi.org/ 10.1016/j.mcn.2007.03.008
    • (2007) Mol. Cell. Neurosci. , vol.35 , pp. 604-624
    • Jerng, H.H.1    Lauver, A.D.2    Pfaffinger, P.J.3
  • 28
    • 72449137625 scopus 로고    scopus 로고
    • A novel N-terminal motif of dipeptidyl peptidase-like proteins produces rapid inactivation of Kv4 2 channels by a pore-blocking mechanism
    • Jerng, H.H., K. Dougherty, M. Covarrubias, and P.J. Pfaffinger. 2009. A novel N-terminal motif of dipeptidyl peptidase-like proteins produces rapid inactivation of Kv4.2 channels by a pore-blocking mechanism. Channels (Austin). 3:448-461. http://dx.doi.org/ 10.4161/chan.3.6.10216
    • (2009) Channels (Austin) , vol.3 , pp. 448-461
    • Jerng, H.H.1    Dougherty, K.2    Covarrubias, M.3    Pfaffinger, P.J.4
  • 29
    • 77956269591 scopus 로고    scopus 로고
    • Going native: voltage-gated potassium channels controlling neuronal excitability
    • Johnston, J., I.D. Forsythe, and C. Kopp-Scheinpflug. 2010. Going native: voltage-gated potassium channels controlling neuronal excitability. J. Physiol. 588:3187-3200. http://dx.doi.org/10.1113/ jphysiol.2010.191973
    • (2010) J. Physiol. , vol.588 , pp. 3187-3200
    • Johnston, J.1    Forsythe, I.D.2    Kopp-Scheinpflug, C.3
  • 31
    • 63849134796 scopus 로고    scopus 로고
    • The dipeptidyl-peptidase-like protein DPP6 determines the unitary conductance of neuronal Kv4 2 channels
    • Kaulin, Y.A., J.A. De Santiago-Castillo, C.A. Rocha, M.S. Nadal, B. Rudy, and M. Covarrubias. 2009. The dipeptidyl-peptidase-like protein DPP6 determines the unitary conductance of neuronal Kv4.2 channels. J. Neurosci. 29:3242-3251. http://dx.doi.org/ 10.1523/JNEUROSCI.4767-08.2009
    • (2009) J. Neurosci. , vol.29 , pp. 3242-3251
    • Kaulin, Y.A.1    De Santiago-Castillo, J.A.2    Rocha, C.A.3    Nadal, M.S.4    Rudy, B.5    Covarrubias, M.6
  • 32
    • 0033014674 scopus 로고    scopus 로고
    • Heteromeric assembly of Kv2 1 with Kv9. 3: effect on the state dependence of inactivation
    • Kerschensteiner, D., and M. Stocker. 1999. Heteromeric assembly of Kv2.1 with Kv9.3: effect on the state dependence of inactivation. Biophys. J. 77:248-257. http://dx.doi.org/10.1016/S0006-3495(99) 76886-4
    • (1999) Biophys. J. , vol.77 , pp. 248-257
    • Kerschensteiner, D.1    Stocker, M.2
  • 33
    • 0037705349 scopus 로고    scopus 로고
    • Structural determinants of the regulation of the voltage-gated potassium channel Kv2 1 by the modulatory α-subunit Kv9. 3
    • Kerschensteiner, D., F. Monje, and M. Stocker. 2003. Structural determinants of the regulation of the voltage-gated potassium channel Kv2.1 by the modulatory α-subunit Kv9.3. J. Biol. Chem. 278:18154-18161. http://dx.doi.org/10.1074/jbc.M213117200
    • (2003) J. Biol. Chem. , vol.278 , pp. 18154-18161
    • Kerschensteiner, D.1    Monje, F.2    Stocker, M.3
  • 34
    • 28244434047 scopus 로고    scopus 로고
    • Kv4 potassium channel subunits control action potential repolarization and frequencydependent broadening in rat hippocampal CA1 pyramidal neurones
    • Kim, J., D.S. Wei, and D.A. Hoffman. 2005. Kv4 potassium channel subunits control action potential repolarization and frequencydependent broadening in rat hippocampal CA1 pyramidal neurones. J. Physiol. 569:41-57. http://dx.doi.org/10.1113/jphysiol .2005.095042
    • (2005) J. Physiol. , vol.569 , pp. 41-57
    • Kim, J.1    Wei, D.S.2    Hoffman, D.A.3
  • 36
    • 0034902362 scopus 로고    scopus 로고
    • U-type inactivation of Kv3 1 and Shaker potassium channels
    • Klemic, K.G., G.E. Kirsch, and S.W. Jones. 2001. U-type inactivation of Kv3.1 and Shaker potassium channels. Biophys. J. 81:814-826. http://dx.doi.org/10.1016/S0006-3495(01)75743-8
    • (2001) Biophys. J. , vol.81 , pp. 814-826
    • Klemic, K.G.1    Kirsch, G.E.2    Jones, S.W.3
  • 37
    • 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
  • 38
    • 57049112014 scopus 로고    scopus 로고
    • + currents in neurons
    • + currents in neurons. J. Physiol. 586:5609-5623. http://dx.doi.org/10.1113/jphysiol .2008.161620
    • (2008) J. Physiol. , vol.586 , pp. 5609-5623
    • Maffie, J.1    Rudy, B.2
  • 39
    • 0032840150 scopus 로고    scopus 로고
    • + conductance in the back-propagation of action potentials in the dendrites of hippocampal pyramidal neurons
    • + conductance in the back-propagation of action potentials in the dendrites of hippocampal pyramidal neurons. J. Comput. Neurosci. 7:5-15. http://dx.doi.org/10.1023/ A:1008906225285
    • (1999) J. Comput. Neurosci. , vol.7 , pp. 5-15
    • Migliore, M.1    Hoffman, D.A.2    Magee, J.C.3    Johnston, D.4
  • 40
    • 0027753950 scopus 로고
    • Energetics of Shaker K channels block by inactivation peptides
    • Murrell-Lagnado, R.D., and R.W. Aldrich. 1993. Energetics of Shaker K channels block by inactivation peptides. J. Gen. Physiol. 102:977-1003. http://dx.doi.org/10.1085/jgp.102.6.977
    • (1993) J. Gen. Physiol. , vol.102 , pp. 977-1003
    • Murrell-Lagnado, R.D.1    Aldrich, R.W.2
  • 41
    • 0027968092 scopus 로고
    • Internal block of human heart sodium channels by symmetrical tetra-alkylammoniums
    • O'Leary, M.E., and R. Horn. 1994. Internal block of human heart sodium channels by symmetrical tetra-alkylammoniums. J. Gen. Physiol. 104:507-522. http://dx.doi.org/10.1085/jgp.104.3.507
    • (1994) J. Gen. Physiol. , vol.104 , pp. 507-522
    • O'Leary, M.E.1    Horn, R.2
  • 44
    • 0037062485 scopus 로고    scopus 로고
    • Obligatory heterotetramerization of three previously uncharacterized Kv channel alpha-subunits identified in the human genome
    • Ottschytsch, N., A. Raes, D. Van Hoorick, and D.J. Snyders. 2002. Obligatory heterotetramerization of three previously uncharacterized Kv channel alpha-subunits identified in the human genome. Proc. Natl. Acad. Sci. USA. 99:7986-7991. http://dx.doi .org/10.1073/pnas.122617999
    • (2002) Proc. Natl. Acad. Sci. USA.
    • Ottschytsch, N.1    Raes, A.2    Van Hoorick, D.3    Snyders, D.J.4
  • 45
    • 34247562213 scopus 로고    scopus 로고
    • Probing the cavity of the slow inactivated conformation of Shaker potassium channels
    • Panyi, G., and C. Deutsch. 2007. Probing the cavity of the slow inactivated conformation of Shaker potassium channels. J. Gen. Physiol. 129:403-418. http://dx.doi.org/10.1085/jgp.200709758
    • (2007) J. Gen. Physiol. , vol.129 , pp. 403-418
    • Panyi, G.1    Deutsch, C.2
  • 46
    • 0032077264 scopus 로고    scopus 로고
    • Preferential closed-state inactivation of neuronal calcium channels
    • Patil, P.G., D.L. Brody, and D.T. Yue. 1998. Preferential closed-state inactivation of neuronal calcium channels. Neuron. 20:1027-1038. http://dx.doi.org/10.1016/S0896-6273(00)80483-3
    • (1998) Neuron , vol.20 , pp. 1027-1038
    • Patil, P.G.1    Brody, D.L.2    Yue, D.T.3
  • 48
    • 84855165622 scopus 로고    scopus 로고
    • Modulation of Kv3 4 channel N-type inactivation by protein kinase C shapes the action potential in dorsal root ganglion neurons
    • Ritter, D.M., C. Ho, M.E. O'Leary, and M. Covarrubias. 2012. Modulation of Kv3.4 channel N-type inactivation by protein kinase C shapes the action potential in dorsal root ganglion neurons. J. Physiol. 590:145-161.
    • (2012) J. Physiol. , vol.590 , pp. 145-161
    • Ritter, D.M.1    Ho, C.2    O'Leary, M.E.3    Covarrubias, M.4
  • 49
    • 0030968673 scopus 로고    scopus 로고
    • + channel Kv1 4 regulated by Ca2+/calmodulin-dependent protein kinase
    • + channel Kv1.4 regulated by Ca2+/calmodulin-dependent protein kinase. J. Neurosci. 17: 3379-3391.
    • (1997) J. Neurosci. , vol.17 , pp. 3379-3391
    • Roeper, J.1    Lorra, C.2    Pongs, O.3
  • 52
    • 0034212603 scopus 로고    scopus 로고
    • + current mediated by the Kv4 channel regulates the generation of action potential in developing cerebellar granule cells
    • + current mediated by the Kv4 channel regulates the generation of action potential in developing cerebellar granule cells. J. Neurosci. 20:4145-4155.
    • (2000) J. Neurosci. , vol.20 , pp. 4145-4155
    • Shibata, R.1    Nakahira, K.2    Shibasaki, K.3    Wakazono, Y.4    Imoto, K.5    Ikenaka, K.6
  • 53
    • 0025330743 scopus 로고
    • Gating of single non-Shaker A-type potassium channels in larval Drosophila neurons
    • Solc, C.K., and R.W. Aldrich. 1990. Gating of single non-Shaker A-type potassium channels in larval Drosophila neurons. J. Gen. Physiol. 96:135-165. http://dx.doi.org/10.1085/jgp.96.1.135
    • (1990) J. Gen. Physiol. , vol.96 , pp. 135-165
    • Solc, C.K.1    Aldrich, R.W.2
  • 54
    • 80053114545 scopus 로고    scopus 로고
    • + current gradient critical for the regulation of dendritic excitability in CA1 hippocampal neurons
    • + current gradient critical for the regulation of dendritic excitability in CA1 hippocampal neurons. Neuron. 71:1102-1115. http://dx.doi.org/10.1016/ j.neuron.2011.08.008
    • (2011) Neuron , vol.71 , pp. 1102-1115
    • Sun, W.1    Maffie, J.K.2    Lin, L.3    Petralia, R.S.4    Rudy, B.5    Hoffman, D.A.6

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