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Volumn 109, Issue 2, 1997, Pages 191-199

Role of the S3-S4 linker in Shaker potassium channel activation

Author keywords

mutagenesis; potassium channel; protein sequence; voltage clamp

Indexed keywords

CALCIUM CHANNEL; MEMBRANE PROTEIN; POTASSIUM CHANNEL;

EID: 0031041645     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.109.2.191     Document Type: Article
Times cited : (56)

References (34)
  • 2
    • 0017796425 scopus 로고
    • Gating currents and charge movements in excitable membranes
    • Almers, W. 1978. Gating currents and charge movements in excitable membranes. Rev. Physiol. Biochem. Pharmacol. 82:96-190.
    • (1978) Rev. Physiol. Biochem. Pharmacol. , vol.82 , pp. 96-190
    • Almers, W.1
  • 3
    • 0017697163 scopus 로고
    • Inactivation of the sodium channel. I. Sodium current experiments
    • Bezanilla, F., and C.M. Armstrong. 1977. Inactivation of the sodium channel. I. Sodium current experiments. J Gen. Physiol. 70:549-566.
    • (1977) J Gen. Physiol. , vol.70 , pp. 549-566
    • Bezanilla, F.1    Armstrong, C.M.2
  • 4
    • 0026525699 scopus 로고
    • Modulation by cAMP of a slowly activating potassium channel expressed in Xenopus oocytes
    • Blumenthal, E.M., and L.K. Kaczmarek. 1992. Modulation by cAMP of a slowly activating potassium channel expressed in Xenopus oocytes. J. Neurosci. 12:290-296.
    • (1992) J. Neurosci. , vol.12 , pp. 290-296
    • Blumenthal, E.M.1    Kaczmarek, L.K.2
  • 5
    • 0025299805 scopus 로고
    • Shal, Shab and Shaw. three genes encoding potassium channels in Drosophila
    • Butler, A., A. Wei, and L. Salkoff. 1990. Shal, Shab and Shaw. three genes encoding potassium channels in Drosophila. Nucleic Acids Res. 18:2173-2174.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 2173-2174
    • Butler, A.1    Wei, A.2    Salkoff, L.3
  • 6
    • 0022555877 scopus 로고
    • Molecular properties of voltage-sensitive sodium channels
    • Catteral, W.A. 1986. Molecular properties of voltage-sensitive sodium channels. Annu. Rev. Biochem. 55:953-985.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 953-985
    • Catteral, W.A.1
  • 8
    • 0026601458 scopus 로고
    • Site-directed mutagenesis of virtually any plasmid by eliminating a unique site
    • Deng, W.P., and J.A. Nickoloff. 1992. Site-directed mutagenesis of virtually any plasmid by eliminating a unique site. Anal. Biochem. 200:81-88.
    • (1992) Anal. Biochem. , vol.200 , pp. 81-88
    • Deng, W.P.1    Nickoloff, J.A.2
  • 9
    • 0026773754 scopus 로고
    • Atomic scale structure and functional models of voltage-gated potassium channels
    • Durell, S.R., and H.R. Guy. 1992. Atomic scale structure and functional models of voltage-gated potassium channels. Biophys. J. 62: 238-247.
    • (1992) Biophys. J. , vol.62 , pp. 238-247
    • Durell, S.R.1    Guy, H.R.2
  • 10
    • 0002785854 scopus 로고
    • Voltage-gated sodium channels
    • R.A. North, editor. CRC Press, Boca Raton, FL
    • Goldin, A. 1995. Voltage-gated sodium channels. In Ligand- and Voltage-gated Ion Channels. R.A. North, editor. CRC Press, Boca Raton, FL. 73-111.
    • (1995) Ligand- and Voltage-gated Ion Channels , pp. 73-111
    • Goldin, A.1
  • 11
    • 0025334586 scopus 로고
    • Pursuing the structure and function of voltage-gated channels
    • Guy, H.R., and F. Conti. 1990. Pursuing the structure and function of voltage-gated channels. Trends Neurosci. 13:201-206.
    • (1990) Trends Neurosci. , vol.13 , pp. 201-206
    • Guy, H.R.1    Conti, F.2
  • 12
    • 0029610155 scopus 로고
    • Transfer of twelve charges is needed to open skeletal muscle Na channels
    • Hirschberg, B., A. Rovner, M. Lieberman, and J. Patlak. 1995. Transfer of twelve charges is needed to open skeletal muscle Na channels. J. Gen. Physiol. 106:1053-1068.
    • (1995) J. Gen. Physiol. , vol.106 , pp. 1053-1068
    • Hirschberg, B.1    Rovner, A.2    Lieberman, M.3    Patlak, J.4
  • 13
    • 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 (Wash. DC). 250:533-538.
    • (1990) Science (Wash. DC) , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 14
    • 0024039181 scopus 로고
    • Multiple products of the Drosophila Shaker gene may contribute to potassium channel diversity
    • Kamb, A., J. Tseng-Crank, and M.A. Tanouye. 1988. Multiple products of the Drosophila Shaker gene may contribute to potassium channel diversity. Neuron. 1:421-430.
    • (1988) Neuron. , vol.1 , pp. 421-430
    • Kamb, A.1    Tseng-Crank, J.2    Tanouye, M.A.3
  • 15
    • 0028950653 scopus 로고
    • Membrane topology of P-glycoprotein as determined by epitope insertion: Transmembrane organization of the N-terminal domain of mdr3
    • Kast, C., V. Canfield, R. Levenson, and P. Gross. 1995. Membrane topology of P-glycoprotein as determined by epitope insertion: transmembrane organization of the N-terminal domain of mdr3. Biochemistry. 34:4402-4411.
    • (1995) Biochemistry , vol.34 , pp. 4402-4411
    • Kast, C.1    Canfield, V.2    Levenson, R.3    Gross, P.4
  • 17
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • MacArthur, M.W., and J.M. Thornton. 1991. Influence of proline residues on protein conformation. J. Mol. Biol. 218:397-412.
    • (1991) J. Mol. Biol. , vol.218 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.M.2
  • 18
    • 0030059224 scopus 로고    scopus 로고
    • Direct physical measure of conformation rearrangement underlying potassium channel gating
    • Mannuzzu, L.M., M.M. Moronne, and E.Y. Isacoff. 1996. Direct physical measure of conformation rearrangement underlying potassium channel gating. Science (Wash. DC). 271:213-216.
    • (1996) Science (Wash. DC) , vol.271 , pp. 213-216
    • Mannuzzu, L.M.1    Moronne, M.M.2    Isacoff, E.Y.3
  • 19
    • 0028063942 scopus 로고
    • Critical roles of the S3 segment and S3-S4 linker of repeat I in activation of L-type calcium channels
    • Nakai, J., B.A. Adams, K. Imoto, and K.G. Beam. 1994. Critical roles of the S3 segment and S3-S4 linker of repeat I in activation of L-type calcium channels. Proc. Natl. Acad. Sci. USA. 91:1014-1018.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1014-1018
    • Nakai, J.1    Adams, B.A.2    Imoto, K.3    Beam, K.G.4
  • 20
    • 0025290573 scopus 로고
    • pOEV: A Xenopus oocyte protein expression vector
    • Pfaff, S.L., M.M. Tamkun, and W.L. Taylor. 1990. pOEV: a Xenopus oocyte protein expression vector. Anal. Biochem. 188:192-199.
    • (1990) Anal. Biochem. , vol.188 , pp. 192-199
    • Pfaff, S.L.1    Tamkun, M.M.2    Taylor, W.L.3
  • 21
    • 0029872191 scopus 로고    scopus 로고
    • Major transmembrane movement associated with colicin Ia channel gating
    • J.K.S.
    • Qiu, X.-Q., J.K.S., P.K. Kienker, A. Finkelstein, and S.L. Slatin. 1996. Major transmembrane movement associated with colicin Ia channel gating. J. Gen. Physiol. 107:313-328.
    • (1996) J. Gen. Physiol. , vol.107 , pp. 313-328
    • Qiu, X.-Q.1    Kienker, P.K.2    Finkelstein, A.3    Slatin, S.L.4
  • 22
    • 0026759307 scopus 로고
    • Site-specific mutagenesis of almost any plasmid using a PCR-based version of unique site elimination
    • Ray, F.A., and J.A. Nickoloff. 1992. Site-specific mutagenesis of almost any plasmid using a PCR-based version of unique site elimination. Biotechniques. 13:342-346.
    • (1992) Biotechniques , vol.13 , pp. 342-346
    • Ray, F.A.1    Nickoloff, J.A.2
  • 23
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant Shaker potassium channels
    • Schoppa, N.E., K. McCormack, M.A. Tanouye, and F.J. Sigworth. 1992. The size of gating charge in wild-type and mutant Shaker potassium channels. Science (Wash. DC). 255:1712-1715.
    • (1992) Science (Wash. DC) , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1    McCormack, K.2    Tanouye, M.A.3    Sigworth, F.J.4
  • 24
    • 0024285862 scopus 로고
    • Multiple potassium-channel components are produced by alternative splicing at the Shaker locus of Drosophila
    • Schwarz, T.L., B.L. Tempel, D.L. Papazian, Y.N. Jan, and L.Y. Jan. 1988. Multiple potassium-channel components are produced by alternative splicing at the Shaker locus of Drosophila. Nature. (Lond.). 331:137-142.
    • (1988) Nature. (Lond.) , vol.331 , pp. 137-142
    • Schwarz, T.L.1    Tempel, B.L.2    Papazian, D.L.3    Jan, Y.N.4    Jan, L.Y.5
  • 26
    • 15644365675 scopus 로고
    • Use of hydrophilic amino acid epitope insertions to probe the topology of the Shaker H4 potassium channel
    • Abstr.
    • Shih, T.M., and A.L. Goldin. 1995. Use of hydrophilic amino acid epitope insertions to probe the topology of the Shaker H4 potassium channel. Biophys. J. 68:266a. (Abstr.).
    • (1995) Biophys. J. , vol.68
    • Shih, T.M.1    Goldin, A.L.2
  • 27
    • 0027971204 scopus 로고
    • Voltage gating of ion channels
    • Sigworth, F.J. 1994. Voltage gating of ion channels. Q. Rev. Biophys. 27:1-40.
    • (1994) Q. Rev. Biophys. , vol.27 , pp. 1-40
    • Sigworth, F.J.1
  • 28
    • 0028100898 scopus 로고
    • Identification of a translocated protein segment in a voltage-dependent channel
    • Slatin, A., X.Q. Qiu, K.S. Jakes, and A. Finkelstein. 1994. Identification of a translocated protein segment in a voltage-dependent channel. Nature (Lond.). 371:158-161.
    • (1994) Nature (Lond.) , vol.371 , pp. 158-161
    • Slatin, A.1    Qiu, X.Q.2    Jakes, K.S.3    Finkelstein, A.4
  • 29
    • 0025782832 scopus 로고
    • Proline kinks in transmembrane alpha helices
    • von Heijne, G. 1991. Proline kinks in transmembrane alpha helices. J. Mol. Biol. 218:499-503.
    • (1991) J. Mol. Biol. , vol.218 , pp. 499-503
    • Von Heijne, G.1
  • 30
    • 0025236345 scopus 로고
    • Factor Xa cleavage of fusion proteins. Elimination of non-specific cleavage by reversible acylation
    • Wearne, S.J. 1990. Factor Xa cleavage of fusion proteins. Elimination of non-specific cleavage by reversible acylation. FEBS Lett. 263:23-26.
    • (1990) FEBS Lett. , vol.263 , pp. 23-26
    • Wearne, S.J.1
  • 32
    • 0030021584 scopus 로고    scopus 로고
    • Molecular basis of charge movement in voltage-gated sodium channels
    • Yang, N., A. George, Jr., and R. Horn. 1996. Molecular basis of charge movement in voltage-gated sodium channels. Neuron. 16: 113-122.
    • (1996) Neuron. , vol.16 , pp. 113-122
    • Yang, N.1    George Jr., A.2    Horn, R.3
  • 33
    • 0028085276 scopus 로고
    • Shaker potassium channel gating. II. Transitions in the activation pathway
    • Zagotta, W.N., T. Hoshi, J. Dittman, and R.W. Aldrich. 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
  • 34
    • 0028918964 scopus 로고
    • A method for probing the topography and interactions of proteins. Footprinting of myoglobin
    • Zhong, M., L. Lin, and N.R. Kallenbach. 1995. A method for probing the topography and interactions of proteins. Footprinting of myoglobin. Proc. Natl. Acad. Sci. USA. 92:2111-2115.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2111-2115
    • Zhong, M.1    Lin, L.2    Kallenbach, N.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.