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Volumn 112, Issue 4, 1998, Pages 377-389

Protein rearrangements underlying slow inactivation of the Shaker K+ channel

Author keywords

Fluorescence; Inactivation; K+ channel; Pore; S4

Indexed keywords

POTASSIUM CHANNEL;

EID: 0031718344     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.112.4.377     Document Type: Article
Times cited : (158)

References (39)
  • 2
    • 0028793256 scopus 로고
    • +]: A tale of two inactivation mechanisms
    • +]: a tale of two inactivation mechanisms. Neuron. 15:951-960.
    • (1995) Neuron , vol.15 , pp. 951-960
    • Baukrowitz, T.1    Yellen, G.2
  • 4
    • 0026315160 scopus 로고
    • Molecular basis of gating charge immobilization in Shaker potassium channels
    • Bezanilla, F., E. Perozo, D. Papazian, and E. Stefani. 1991. Molecular basis of gating charge immobilization in Shaker potassium channels. Science. 254:679-683.
    • (1991) Science , vol.254 , pp. 679-683
    • Bezanilla, F.1    Perozo, E.2    Papazian, D.3    Stefani, E.4
  • 5
    • 0028208966 scopus 로고
    • Cysteines in the Shaker K channel are not essential for channel activity or zinc modulation
    • Boland, L., M. Jurman, and G. Yellen. 1994. Cysteines in the Shaker K channel are not essential for channel activity or zinc modulation. Biophys. J. 66:694-699.
    • (1994) Biophys. J. , vol.66 , pp. 694-699
    • Boland, L.1    Jurman, M.2    Yellen, G.3
  • 6
    • 0030840167 scopus 로고    scopus 로고
    • Characterizing voltage-dependent conformational changes in the Shaker K channel with fluorescence
    • Cha, A., and F. Bezanilla. 1997. Characterizing voltage-dependent conformational changes in the Shaker K channel with fluorescence. Neuron. 19:1127-1140.
    • (1997) Neuron , vol.19 , pp. 1127-1140
    • Cha, A.1    Bezanilla, F.2
  • 9
    • 0030051784 scopus 로고    scopus 로고
    • Agitoxin footprinting the Shaker potassium channel pore
    • Gross, A., and R. MacKinnon. 1996. Agitoxin footprinting the Shaker potassium channel pore. Neuron. 16:399-406.
    • (1996) Neuron , vol.16 , pp. 399-406
    • Gross, A.1    MacKinnon, R.2
  • 12
    • 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.
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 13
    • 0026049511 scopus 로고
    • Two types of inactivation in Shaker K channels: Effect of alterations in the carboxyterminal region
    • Hoshi, T., W. Zagotta, and R. Aldrich. 1991. Two types of inactivation in Shaker K channels: effect of alterations in the carboxyterminal region. Neuron. 7:547-556.
    • (1991) Neuron , vol.7 , pp. 547-556
    • Hoshi, T.1    Zagotta, W.2    Aldrich, R.3
  • 14
    • 0025362581 scopus 로고
    • Evidence for the formation of heteromultimeric potassium channels in Xenopus oocytes
    • Isacoff, E., Y. Jan, and L. Jan. 1990. Evidence for the formation of heteromultimeric potassium channels in Xenopus oocytes. Nature. 345:530-534.
    • (1990) Nature , vol.345 , pp. 530-534
    • Isacoff, E.1    Jan, Y.2    Jan, L.3
  • 15
    • 0025900745 scopus 로고
    • Putative receptor for the cytoplasmic inactivation gate in the Shaker K. channel
    • Isacoff, E., Y. Jan, and L. Jan. 1991. Putative receptor for the cytoplasmic inactivation gate in the Shaker K. channel. Nature. 353:86-90.
    • (1991) Nature , vol.353 , pp. 86-90
    • Isacoff, E.1    Jan, Y.2    Jan, L.3
  • 16
    • 0025482647 scopus 로고
    • The role of the divergent amino and carboxyl domains on the inactivation properties of potassium channels derived from the Shaker gene of Drosophila
    • Iverson, L.E., and B. Rudy. 1990. The role of the divergent amino and carboxyl domains on the inactivation properties of potassium channels derived from the Shaker gene of Drosophila. J. Neurosci. 10:2903-2916.
    • (1990) J. Neurosci. , vol.10 , pp. 2903-2916
    • Iverson, L.E.1    Rudy, B.2
  • 17
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A. 1985. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA. 82:488-492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 18
    • 0028941130 scopus 로고
    • Side-chain accessibilities in the pore of a K channel probed by sulfhydryl-specific reagents after cysteine-scanning mutagenesis
    • Kurz, L., R.D. Zuhlke, H. Zhang, and R. Joho. 1995. Side-chain accessibilities in the pore of a K channel probed by sulfhydryl-specific reagents after cysteine-scanning mutagenesis. Biophys. J. 68: 900-905.
    • (1995) Biophys. J. , vol.68 , pp. 900-905
    • Kurz, L.1    Zuhlke, R.D.2    Zhang, H.3    Joho, R.4
  • 20
    • 0030071057 scopus 로고    scopus 로고
    • Recovery from c-type inactivation is modulated by extracellular potassium
    • Levy, D., and C. Deutsch. 1996. Recovery from c-type inactivation is modulated by extracellular potassium. Biophys. J. 70:798-805.
    • (1996) Biophys. J. , vol.70 , pp. 798-805
    • Levy, D.1    Deutsch, C.2
  • 21
    • 0027828292 scopus 로고
    • Effects of external cations and mutations in the pore region on c-type inactivation of Shaker potassium channels
    • Lopez-Barneo, J., T. Hoshi, S. Heinemann, and R. 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
    • Lopez-Barneo, J.1    Hoshi, T.2    Heinemann, S.3    Aldrich, R.4
  • 22
    • 0029990996 scopus 로고    scopus 로고
    • Dynamic rearrangement of the outer mouth of a K channel during gating
    • Liu, Y., M. Jurman, and G. Yellen. 1996. Dynamic rearrangement of the outer mouth of a K channel during gating. Neuron. 16:859-867.
    • (1996) Neuron , vol.16 , pp. 859-867
    • Liu, Y.1    Jurman, M.2    Yellen, G.3
  • 23
    • 0028960949 scopus 로고
    • Silver as a probe of pore-forming residues in a potassium channel
    • Lu, Q., and C. Miller. 1995. Silver as a probe of pore-forming residues in a potassium channel. Nature. 268:304-307.
    • (1995) Nature , vol.268 , pp. 304-307
    • Lu, Q.1    Miller, C.2
  • 24
    • 0032478696 scopus 로고    scopus 로고
    • Structural conservation in prokaryotic and eukaryotic potassium channels
    • MacKinnon, R., S.L. Cohen, A. Kuo, A. Lee, and B.T. Chait. 1998. Structural conservation in prokaryotic and eukaryotic potassium channels. Science. 280:106-109.
    • (1998) Science , vol.280 , pp. 106-109
    • MacKinnon, R.1    Cohen, S.L.2    Kuo, A.3    Lee, A.4    Chait, B.T.5
  • 25
    • 0030059224 scopus 로고    scopus 로고
    • Direct physical measure of conformational rearrangement underlying potassium channel gating
    • Mannuzzu, L., M. Moronne, and E.Y. Isacoff. 1996. Direct physical measure of conformational rearrangement underlying potassium channel gating. Science. 271:213-216.
    • (1996) Science , vol.271 , pp. 213-216
    • Mannuzzu, L.1    Moronne, M.2    Isacoff, E.Y.3
  • 26
    • 0028136017 scopus 로고
    • State-dependent inactivation of the Kv3 potassium channel
    • Marom, S., and I. Levitan. 1994. State-dependent inactivation of the Kv3 potassium channel. Biophys. J. 67:579-589.
    • (1994) Biophys. J. , vol.67 , pp. 579-589
    • Marom, S.1    Levitan, I.2
  • 27
    • 0030044863 scopus 로고    scopus 로고
    • A strongly interacting pair of residues on the contact surface of charybdotoxin and a Shaker K channel
    • Naranjo, D., and C. Miller. 1996. A strongly interacting pair of residues on the contact surface of charybdotoxin and a Shaker K channel. Neuron. 16:123-130.
    • (1996) Neuron , vol.16 , pp. 123-130
    • Naranjo, D.1    Miller, C.2
  • 30
    • 0029145067 scopus 로고
    • C-type inactivation of a voltage-gated channel occurs by a cooperative mechanism
    • Panyi, G., Z. Sheng, L. Tu, and C. Deutsch. 1995. C-type inactivation of a voltage-gated channel occurs by a cooperative mechanism. Biophys. J. 69:896-903.
    • (1995) Biophys. J. , vol.69 , pp. 896-903
    • Panyi, G.1    Sheng, Z.2    Tu, L.3    Deutsch, C.4
  • 31
    • 0029070117 scopus 로고
    • K pore structure revealed by reporter cysteines at inner and outer surfaces
    • Pascual, J., C. Shieh, G. Kirsch, and A. Brown. 1995. K pore structure revealed by reporter cysteines at inner and outer surfaces. Neuron. 14:1055-1063.
    • (1995) Neuron , vol.14 , pp. 1055-1063
    • Pascual, J.1    Shieh, C.2    Kirsch, G.3    Brown, A.4
  • 33
    • 0030706134 scopus 로고    scopus 로고
    • Ion conduction through c-type inactivated Shaker channels
    • Starkus, J.G., L. Kuschel, M. Rayner, and S. Heinemann. 1997. Ion conduction through c-type inactivated Shaker channels. J. Gen. Physiol. 110:539-550.
    • (1997) J. Gen. Physiol. , vol.110 , pp. 539-550
    • Starkus, J.G.1    Kuschel, L.2    Rayner, M.3    Heinemann, S.4
  • 34
    • 0024093507 scopus 로고
    • Four cDNA clones from the Shaker locus of Drosophila induce kinetically distinct A-type potassium currents in Xenopus oocytes
    • Timpe, L., Y. Jan, and L. Jan. 1988. Four cDNA clones from the Shaker locus of Drosophila induce kinetically distinct A-type potassium currents in Xenopus oocytes. Neuron. 1:659-667.
    • (1988) Neuron , vol.1 , pp. 659-667
    • Timpe, L.1    Jan, Y.2    Jan, L.3
  • 35
    • 0030906796 scopus 로고    scopus 로고
    • How does the W434F mutation block current in the Shaker potassium channels?
    • Yang, Y., Y. Yan, and F. Sigworth. 1997. How does the W434F mutation block current in the Shaker potassium channels? J. Gen. Physiol. 109:779-789.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 779-789
    • Yang, Y.1    Yan, Y.2    Sigworth, F.3
  • 36
    • 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. Chen, and 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.
    • (1994) Biophys. J. , vol.66 , pp. 1068-1075
    • Yellen, G.1    Sodickson, D.2    Chen, T.3    Jurman, E.4
  • 37
    • 0026058182 scopus 로고
    • Alterations of ionic selectivity of a K channel by mutation of the H5 region
    • Yool, A.J., and T.L. Schwarz. 1991. Alterations of ionic selectivity of a K channel by mutation of the H5 region. Nature. 349:700-704.
    • (1991) Nature , vol.349 , pp. 700-704
    • Yool, A.J.1    Schwarz, T.L.2
  • 38
    • 0029845542 scopus 로고    scopus 로고
    • Measurement of the movement of the S4 segment during the activation of a voltage-gated potassium channel
    • Yusaf, S.P., D. Wray, and A. Sivaprasadarao. 1996. Measurement of the movement of the S4 segment during the activation of a voltage-gated potassium channel. Pflügers Arch. 433:91-97.
    • (1996) Pflügers Arch. , vol.433 , pp. 91-97
    • Yusaf, S.P.1    Wray, D.2    Sivaprasadarao, A.3
  • 39
    • 0025245612 scopus 로고
    • Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB
    • Zagotta, W.N., T. Hoshi, and W. Aldrich. 1990. Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB. Science. 250:568-571.
    • (1990) Science , vol.250 , pp. 568-571
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.