메뉴 건너뛰기




Volumn 141, Issue 3, 2013, Pages 389-395

The voltage-sensing domain of a phosphatase gates the pore of a potassium channel

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; PHOSPHATASE; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 84874698159     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201210940     Document Type: Article
Times cited : (47)

References (21)
  • 2
    • 36248946187 scopus 로고    scopus 로고
    • Portability of paddle motif function and pharmacology in voltage sensors
    • Alabi, A.A., M.I. Bahamonde, H.J. Jung, J.I. Kim, and K.J. Swartz. 2007. Portability of paddle motif function and pharmacology in voltage sensors. Nature. 450:370-375. http://dx.doi.org/10.1038/nature06266
    • (2007) Nature. , vol.450 , pp. 370-375
    • Alabi, A.A.1    Bahamonde, M.I.2    Jung, H.J.3    Kim, J.I.4    Swartz, K.J.5
  • 3
    • 58149262941 scopus 로고    scopus 로고
    • Inverse coupling in leak and voltage-activated K+ channel gates underlies distinct roles in electrical signaling
    • Ben-Abu, Y., Y. Zhou, N. Zilberberg, and O. Yifrach. 2009. Inverse coupling in leak and voltage-activated K+ channel gates underlies distinct roles in electrical signaling. Nat. Struct. Mol. Biol. 16:71-79. http://dx.doi.org/10.1038/nsmb.1525
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 71-79
    • Ben-Abu, Y.1    Zhou, Y.2    Zilberberg, N.3    Yifrach, O.4
  • 4
    • 56249091754 scopus 로고    scopus 로고
    • Deconstructing voltage sensor function and pharmacology in sodium channels
    • Bosmans, F., M.F. Martin-Eauclaire, and K.J. Swartz. 2008. Deconstructing voltage sensor function and pharmacology in sodium channels. Nature. 456:202-208. http://dx.doi.org/10.1038/nature07473
    • (2008) Nature. , vol.456 , pp. 202-208
    • Bosmans, F.1    Martin-Eauclaire, M.F.2    Swartz, K.J.3
  • 5
    • 0035877755 scopus 로고    scopus 로고
    • Structural compatibility between the putative voltage sensor of voltage-gated K+ channels and the prokaryotic KcsA channel
    • Caprini, M., S. Ferroni, R. Planells-Cases, J. Rueda, C. Rapisarda, A. Ferrer-Montiel, and M. Montal. 2001. Structural compatibility between the putative voltage sensor of voltage-gated K+ channels and the prokaryotic KcsA channel. J. Biol. Chem. 276:21070-21076. http://dx.doi.org/10.1074/jbc.M100487200
    • (2001) J. Biol. Chem. , vol.276 , pp. 21070-21076
    • Caprini, M.1    Ferroni, S.2    Planells-Cases, R.3    Rueda, J.4    Rapisarda, C.5    Ferrer-Montiel, A.6    Montal, M.7
  • 6
    • 38749112951 scopus 로고    scopus 로고
    • A common pathway for charge transport through voltage-sensing domains
    • Chanda, B., and F. Bezanilla. 2008. A common pathway for charge transport through voltage-sensing domains. Neuron. 57:345-351. http://dx.doi.org/10.1016/j.neuron.2008.01.015
    • (2008) Neuron. , vol.57 , pp. 345-351
    • Chanda, B.1    Bezanilla, F.2
  • 7
    • 70449372669 scopus 로고    scopus 로고
    • Selection of inhibitor-resistant viral potassium channels identifies a selectivity filter site that affects barium and amantadine block
    • Chatelain, F.C., S. Gazzarrini, Y. Fujiwara, C. Arrigoni, C. Domigan, G. Ferrara, C. Pantoja, G. Thiel, A. Moroni, and D.L. Minor Jr. 2009. Selection of inhibitor-resistant viral potassium channels identifies a selectivity filter site that affects barium and amantadine block. PLoS ONE. 4:e7496. http://dx.doi.org/10.1371/journal.pone.0007496
    • (2009) PLoS ONE , vol.4
    • Chatelain, F.C.1    Gazzarrini, S.2    Fujiwara, Y.3    Arrigoni, C.4    Domigan, C.5    Ferrara, G.6    Pantoja, C.7    Thiel, G.8    Moroni, A.9    Minor, D.L.10
  • 8
    • 3142655365 scopus 로고    scopus 로고
    • Long distance interactions within the potassium channel pore are revealed by molecular diversity of viral proteins
    • Gazzarrini, S., M. Kang, J.L. Van Etten, S. Tayefeh, S.M. Kast, D. DiFrancesco, G. Thiel, and A. Moroni. 2004. Long distance interactions within the potassium channel pore are revealed by molecular diversity of viral proteins. J. Biol. Chem. 279:28443-28449. http://dx.doi.org/10.1074/jbc.M401184200
    • (2004) J. Biol. Chem. , vol.279 , pp. 28443-28449
    • Gazzarrini, S.1    Kang, M.2    Van Etten, J.L.3    Tayefeh, S.4    Kast, S.M.5    DiFrancesco, D.6    Thiel, G.7    Moroni, A.8
  • 9
    • 34447129759 scopus 로고    scopus 로고
    • Electrokinetics of miniature K+ channel: open-state V sensitivity and inhibition by K+ driving force
    • Gazzarrini, S., A. Abenavoli, D. Gradmann, G. Thiel, and A. Moroni. 2006. Electrokinetics of miniature K+ channel: open-state V sensitivity and inhibition by K+ driving force. J. Membr. Biol. 214:9-17. http://dx.doi.org/10.1007/s00232-006-0024-3
    • (2006) J. Membr. Biol. , vol.214 , pp. 9-17
    • Gazzarrini, S.1    Abenavoli, A.2    Gradmann, D.3    Thiel, G.4    Moroni, A.5
  • 11
    • 66149157329 scopus 로고    scopus 로고
    • Two separate interfaces between the voltage sensor and pore are required for the function of voltage-dependent K(+) channels
    • Lee, S.Y., A. Banerjee, and R. MacKinnon. 2009. Two separate interfaces between the voltage sensor and pore are required for the function of voltage-dependent K(+) channels. PLoS Biol. 7:e47. http://dx.doi.org/10.1371/journal.pbio.1000047
    • (2009) PLoS Biol , vol.7
    • Lee, S.Y.1    Banerjee, A.2    MacKinnon, R.3
  • 12
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: structural basis of electromechanical coupling
    • Long, S.B., E.B. Campbell, and R. Mackinnon. 2005. Voltage sensor of Kv1.2: structural basis of electromechanical coupling. Science. 309:903-908. http://dx.doi.org/10.1126/science.1116270
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 13
    • 0035950089 scopus 로고    scopus 로고
    • Ion conduction pore is conserved among potassium channels
    • Lu, Z., A.M. Klem, and Y. Ramu. 2001. Ion conduction pore is conserved among potassium channels. Nature. 413:809-813. http://dx.doi.org/10.1038/35101535
    • (2001) Nature , vol.413 , pp. 809-813
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 15
    • 34548725637 scopus 로고    scopus 로고
    • Depolarization activates the phosphoinositide phosphatase Ci-VSP, as detected in Xenopus oocytes coexpressing sensors of PIP2
    • Murata, Y., and Y. Okamura. 2007. Depolarization activates the phosphoinositide phosphatase Ci-VSP, as detected in Xenopus oocytes coexpressing sensors of PIP2. J. Physiol. 583:875-889. http://dx.doi.org/10.1113/jphysiol.2007.134775
    • (2007) J. Physiol. , vol.583 , pp. 875-889
    • Murata, Y.1    Okamura, Y.2
  • 16
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • Murata, Y., H. Iwasaki, M. Sasaki, K. Inaba, and Y. Okamura. 2005. Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. Nature. 435:1239-1243. http://dx.doi.org/10.1038/nature03650
    • (2005) Nature , vol.435 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 17
    • 33846627734 scopus 로고    scopus 로고
    • Molecular properties of Kcv, a virus encoded K+ channel
    • Pagliuca, C., T.A. Goetze, R. Wagner, G. Thiel, A. Moroni, and D. Parcej. 2007. Molecular properties of Kcv, a virus encoded K+ channel. Biochemistry. 46:1079-1090. http://dx.doi.org/10.1021/bi061530w
    • (2007) Biochemistry. , vol.46 , pp. 1079-1090
    • Pagliuca, C.1    Goetze, T.A.2    Wagner, R.3    Thiel, G.4    Moroni, A.5    Parcej, D.6
  • 19
    • 59649113542 scopus 로고    scopus 로고
    • Molecular template for a voltage sensor in a novel K+ channel
    • III. Functional reconstitution of a sensorless pore module from a prokaryotic Kv channel
    • Santos, J.S., S.M. Grigoriev, and M. Montal. 2008. Molecular template for a voltage sensor in a novel K+ channel. III. Functional reconstitution of a sensorless pore module from a prokaryotic Kv channel. J. Gen. Physiol. 132:651-666. http://dx.doi.org/10.1085/jgp.200810077
    • (2008) J. Gen. Physiol. , vol.132 , pp. 651-666
    • Santos, J.S.1    Grigoriev, S.M.2    Montal, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.