메뉴 건너뛰기




Volumn 5 MAY, Issue , 2014, Pages

PIP2 regulation of KCNQ channels: Biophysical and molecular mechanisms for lipid modulation of voltage-dependent gating

Author keywords

Ion channel; KCNQ; Lipid modulations; Voltage gating

Indexed keywords

LARGE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; POTASSIUM CHANNEL KCNE1; POTASSIUM CHANNEL KCNQ; POTASSIUM CHANNEL KCNQ1; POTASSIUM CHANNEL KCNQ2; POTASSIUM CHANNEL KCNQ3; POTASSIUM CHANNEL KV1.2; SHAB POTASSIUM CHANNEL;

EID: 84904311415     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2014.00195     Document Type: Review
Times cited : (103)

References (115)
  • 2
    • 84868108814 scopus 로고    scopus 로고
    • Surface expression and subunit specific control of steady protein levels by the Kv7.2 helix A-B linker
    • e47263. doi: 10.1371/journal.pone.0047263
    • Aivar, P., Fernández-Orth, J., Gomis-Perez, C., Alberdi, A., Alaimo, A., Rodríguez, M. S., et al. (2012). Surface expression and subunit specific control of steady protein levels by the Kv7.2 helix A-B linker. PLoS ONE 7:e47263. doi: 10.1371/journal.pone.0047263.
    • (2012) PLoS ONE , vol.7
    • Aivar, P.1    Fernández-Orth, J.2    Gomis-Perez, C.3    Alberdi, A.4    Alaimo, A.5    Rodríguez, M.S.6
  • 3
    • 78649475177 scopus 로고    scopus 로고
    • Molecular mechanism of allosteric modification of voltage-dependent sodium channels by local anesthetics
    • doi: 10.1085/jgp.201010438
    • Arcisio-Miranda, M., Muroi, Y., Chowdhury, S., and Chanda, B. (2010). Molecular mechanism of allosteric modification of voltage-dependent sodium channels by local anesthetics. J. Gen. Physiol. 136, 541-554. doi: 10.1085/jgp.201010438.
    • (2010) J. Gen. Physiol. , vol.136 , pp. 541-554
    • Arcisio-Miranda, M.1    Muroi, Y.2    Chowdhury, S.3    Chanda, B.4
  • 4
    • 84874698159 scopus 로고    scopus 로고
    • The voltage-sensing domain of a phosphatase gates the pore of a potassium channel
    • doi: 10.1085/jgp.201210940
    • Arrigoni, C., Schroeder, I., Romani, G., Van Etten, J. L., Thiel, G., and Moroni, A. (2013). The voltage-sensing domain of a phosphatase gates the pore of a potassium channel. J. Gen. Physiol. 141, 389-395. doi: 10.1085/jgp.201210940.
    • (2013) J. Gen. Physiol. , vol.141 , pp. 389-395
    • Arrigoni, C.1    Schroeder, I.2    Romani, G.3    Van Etten, J.L.4    Thiel, G.5    Moroni, A.6
  • 5
    • 0029952101 scopus 로고    scopus 로고
    • K(V)LQT1 and lsK (minK) proteins associate to form the I(Ks) cardiac potassium current
    • doi: 10.1038/384078a0
    • Barhanin, J., Lesage, F., Guillemare, E., Fink, M., Lazdunski, M., and Romey, G. (1996). K(V)LQT1 and lsK (minK) proteins associate to form the I(Ks) cardiac potassium current. Nature 384, 78-80. doi: 10.1038/384078a0.
    • (1996) Nature , vol.384 , pp. 78-80
    • Barhanin, J.1    Lesage, F.2    Guillemare, E.3    Fink, M.4    Lazdunski, M.5    Romey, G.6
  • 6
    • 41149095488 scopus 로고    scopus 로고
    • How membrane proteins sense voltage
    • doi: 10.1038/nrm2376
    • Bezanilla, F. (2008). How membrane proteins sense voltage. Nat. Rev. Mol. Cell Biol. 9, 323-332. doi: 10.1038/nrm2376.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 323-332
    • Bezanilla, F.1
  • 7
    • 0035824896 scopus 로고    scopus 로고
    • HERG K(+) channel activity is regulated by changes in phosphatidyl inositol 4,5-bisphosphate
    • doi: 10.1161/hh2401.101375
    • Bian, J., Cui, J., and McDonald, T. V. (2001). HERG K(+) channel activity is regulated by changes in phosphatidyl inositol 4,5-bisphosphate. Circ. Res. 89, 1168-1176. doi: 10.1161/hh2401.101375.
    • (2001) Circ. Res. , vol.89 , pp. 1168-1176
    • Bian, J.1    Cui, J.2    McDonald, T.V.3
  • 8
    • 34547102989 scopus 로고    scopus 로고
    • Regulation of M(Kv7.2/7.3) channels in neurons by PIP2 and products Of PIP2 hydrolysis: significance for receptor-mediated inhibition
    • doi: 10.1113/jphysiol.2007.132498
    • Brown, D. A., Hughes, S. A., Marsh, S. J., and Tinker, A. (2007). Regulation of M(Kv7.2/7.3) channels in neurons by PIP2 and products Of PIP2 hydrolysis: significance for receptor-mediated inhibition. J. Physiol. 582(Pt 3), 917-925. doi: 10.1113/jphysiol.2007.132498.
    • (2007) J. Physiol. , vol.582 , Issue.PART 3 , pp. 917-925
    • Brown, D.A.1    Hughes, S.A.2    Marsh, S.J.3    Tinker, A.4
  • 9
    • 77957924708 scopus 로고    scopus 로고
    • Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP
    • doi: 10.1016/j.jmb.2010.09.012
    • Butterwick, J. A., and MacKinnon, R. (2010). Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP. J. Mol. Biol. 403, 591-606. doi: 10.1016/j.jmb.2010.09.012.
    • (2010) J. Mol. Biol. , vol.403 , pp. 591-606
    • Butterwick, J.A.1    MacKinnon, R.2
  • 10
    • 84871020065 scopus 로고    scopus 로고
    • Thermodynamics of electromechanical coupling in voltage-gated ion channels
    • doi: 10.1085/jgp.201210840
    • Chowdhury, S., and Chanda, B. (2012). Thermodynamics of electromechanical coupling in voltage-gated ion channels. J. Gen. Physiol. 140, 10. doi: 10.1085/jgp.201210840.
    • (2012) J. Gen. Physiol. , vol.140 , pp. 10
    • Chowdhury, S.1    Chanda, B.2
  • 11
    • 0032199006 scopus 로고    scopus 로고
    • Binding, gating, affinity and efficacy: the interpretation of structure-activity relationships for agonists and of the effects of mutating receptors
    • doi: 10.1038/sj.bjp.0702164
    • Colquhoun, D. (1998). Binding, gating, affinity and efficacy: the interpretation of structure-activity relationships for agonists and of the effects of mutating receptors. Br. J. Pharmacol. 125, 923-947. doi: 10.1038/sj.bjp.0702164.
    • (1998) Br. J. Pharmacol. , vol.125 , pp. 923-947
    • Colquhoun, D.1
  • 12
    • 67650516762 scopus 로고    scopus 로고
    • A lipid-dependent uncoupled conformation of the acetylcholine receptor
    • doi: 10.1074/jbc.M900030200
    • daCosta, C. J. B., and Baenziger, J. E. (2009). A lipid-dependent uncoupled conformation of the acetylcholine receptor. J. Biol. Chem. 284, 17819-17825. doi: 10.1074/jbc.M900030200.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17819-17825
    • daCosta, C.J.B.1    Baenziger, J.E.2
  • 13
    • 71749098387 scopus 로고    scopus 로고
    • Anionic lipids allosterically modulate multiple nicotinic acetylcholine receptor conformational equilibria
    • doi: 10.1074/jbc.M109.048280
    • daCosta, C. J. B., Medaglia, S. A., Lavigne, N., Wang, S., Carswell, C. L., and Baenziger, J. E. (2009). Anionic lipids allosterically modulate multiple nicotinic acetylcholine receptor conformational equilibria. J. Biol. Chem. 284, 33841-33849. doi: 10.1074/jbc.M109.048280.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33841-33849
    • daCosta, C.J.B.1    Medaglia, S.A.2    Lavigne, N.3    Wang, S.4    Carswell, C.L.5    Baenziger, J.E.6
  • 14
    • 79954991393 scopus 로고    scopus 로고
    • Intermediate states of the Kv1.2 voltage sensor from atomistic molecular dynamics simulations
    • doi: 10.1073/pnas.1102724108
    • Delemotte, L., Tarek, M., Klein, M. L., Amaral, C., and Treptow, W. (2011). Intermediate states of the Kv1.2 voltage sensor from atomistic molecular dynamics simulations. Proc. Natl. Acad. Sci. U.S.A. 108, 6109. doi: 10.1073/pnas.1102724108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 6109
    • Delemotte, L.1    Tarek, M.2    Klein, M.L.3    Amaral, C.4    Treptow, W.5
  • 15
    • 27644518764 scopus 로고    scopus 로고
    • Pathways modulating neural KCNQ/M (Kv7) potassium channels
    • doi: 10.1038/nrn1785
    • Delmas, P., and Brown, D. A. (2005). Pathways modulating neural KCNQ/M (Kv7) potassium channels. Nat. Rev. Neurosci. 6, 850-862. doi: 10.1038/nrn1785.
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 850-862
    • Delmas, P.1    Brown, D.A.2
  • 16
    • 75749085243 scopus 로고    scopus 로고
    • Kinetics of PIP2 metabolism and KCNQ2/3 channel regulation studied with a voltage-sensitive phosphatase in living cells
    • doi: 10.1085/jgp.200910345
    • Falkenburger, B. H., Jensen, J. B., and Hille, B. (2010). Kinetics of PIP2 metabolism and KCNQ2/3 channel regulation studied with a voltage-sensitive phosphatase in living cells. J. Gen. Physiol. 135, 99-114. doi: 10.1085/jgp.200910345.
    • (2010) J. Gen. Physiol. , vol.135 , pp. 99-114
    • Falkenburger, B.H.1    Jensen, J.B.2    Hille, B.3
  • 17
    • 27244444569 scopus 로고    scopus 로고
    • From the cover: interface connections of a transmembrane voltage sensor
    • doi: 10.1073/pnas.0507618102
    • Freites, J. A. (2005). From the cover: interface connections of a transmembrane voltage sensor. Proc. Natl. Acad. Sci. U.S.A. 102, 15059-15064. doi: 10.1073/pnas.0507618102.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15059-15064
    • Freites, J.A.1
  • 19
    • 33846694346 scopus 로고    scopus 로고
    • Structure prediction for the down state of a potassium channel voltage sensor
    • doi: 10.1038/nature05494
    • Grabe, M., Lai, H. C., Jain, M., Nung Jan, Y., and Yeh Jan, L. (2007). Structure prediction for the down state of a potassium channel voltage sensor. Nature 445, 550-553. doi: 10.1038/nature05494.
    • (2007) Nature , vol.445 , pp. 550-553
    • Grabe, M.1    Lai, H.C.2    Jain, M.3    Nung Jan, Y.4    Yeh Jan, L.5
  • 20
    • 79956125732 scopus 로고    scopus 로고
    • + channels is caused by energetic coupling to the pore domain
    • doi: 10.1085/jgp.201010573
    • + channels is caused by energetic coupling to the pore domain. J. Gen. Physiol. 137, 455-472. doi: 10.1085/jgp.201010573.
    • (2011) J. Gen. Physiol. , vol.137 , pp. 455-472
    • Haddad, G.A.1    Blunck, R.2
  • 21
  • 22
    • 0031780332 scopus 로고    scopus 로고
    • + channel
    • doi: 10.1085/jgp.111.6.741
    • + channel. J. Gen. Physiol. 111, 741-749. doi: 10.1085/jgp.111.6.741.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 741-749
    • Heginbotham, L.1
  • 24
    • 84866307068 scopus 로고    scopus 로고
    • Fitting KV potassium channels into the PIP2 puzzle: Hille group connects dots between illustrious HH groups
    • doi: 10.1085/jgp.201210874
    • Hilgemann, D. W. (2012). Fitting KV potassium channels into the PIP2 puzzle: Hille group connects dots between illustrious HH groups. J. Gen. Physiol. 140, 245-248. doi: 10.1085/jgp.201210874.
    • (2012) J. Gen. Physiol. , vol.140 , pp. 245-248
    • Hilgemann, D.W.1
  • 25
    • 0029831984 scopus 로고    scopus 로고
    • 2+ exchange and KATP potassium channels by PIP2
    • doi: 10.1126/science.273.5277.956
    • 2+ exchange and KATP potassium channels by PIP2. Science 273, 956-959. doi: 10.1126/science.273.5277.956.
    • (1996) Science , vol.273 , pp. 956-959
    • Hilgemann, D.W.1    Ball, R.2
  • 26
    • 0035808040 scopus 로고    scopus 로고
    • The complex and intriguing lives of PIP2 with Ion channels and transporters
    • doi: 10.1126/stke.2001.111.re19
    • Hilgemann, D. W., Feng, S., and Nasuhoglu, C. (2001). The complex and intriguing lives of PIP2 with Ion channels and transporters. Sci. STKE 2001, re19. doi: 10.1126/stke.2001.111.re19.
    • (2001) Sci. STKE , vol.2001
    • Hilgemann, D.W.1    Feng, S.2    Nasuhoglu, C.3
  • 27
    • 0032771042 scopus 로고    scopus 로고
    • Allosteric voltage gating of potassium channels II. Mslo channel gating charge movement in the absence of Ca(2+)
    • doi: 10.1085/jgp.114.2.305
    • Horrigan, F. T., and Aldrich, R. W. (1999). Allosteric voltage gating of potassium channels II. Mslo channel gating charge movement in the absence of Ca(2+). J. Gen. Physiol. 114, 305-336. doi: 10.1085/jgp.114.2.305.
    • (1999) J. Gen. Physiol. , vol.114 , pp. 305-336
    • Horrigan, F.T.1    Aldrich, R.W.2
  • 28
    • 0032811552 scopus 로고    scopus 로고
    • Allosteric voltage gating of potassium channels I. Mslo ionic currents in the absence of Ca(2+)
    • doi: 10.1085/jgp.114.2.277
    • Horrigan, F. T., Cui, J., and Aldrich, R. W. (1999). Allosteric voltage gating of potassium channels I. Mslo ionic currents in the absence of Ca(2+). J. Gen. Physiol. 114, 277-304. doi: 10.1085/jgp.114.2.277.
    • (1999) J. Gen. Physiol. , vol.114 , pp. 277-304
    • Horrigan, F.T.1    Cui, J.2    Aldrich, R.W.3
  • 29
    • 0032693966 scopus 로고    scopus 로고
    • Voltage sensitivity and gating charge in shaker and shab family potassium channels
    • doi: 10.1085/jgp.114.5.723
    • Islas, L. D., and Sigworth, F. J. (1999). Voltage sensitivity and gating charge in shaker and shab family potassium channels. J. Gen. Physiol. 114, 723. doi: 10.1085/jgp.114.5.723.
    • (1999) J. Gen. Physiol. , vol.114 , pp. 723
    • Islas, L.D.1    Sigworth, F.J.2
  • 30
    • 80052787583 scopus 로고    scopus 로고
    • Alpha-1 adrenergic receptors: targets for agonist drugs to treat heart failure
    • doi: 10.1016/j.yjmcc.2010.11.014
    • Jensen, B. C., O'Connell, T. D., and Simpson, P. C. (2011). Alpha-1 adrenergic receptors: targets for agonist drugs to treat heart failure. J. Mol. Cell. Cardiol. 51, 229-233. doi: 10.1016/j.yjmcc.2010.11.014.
    • (2011) J. Mol. Cell. Cardiol. , vol.51 , pp. 229-233
    • Jensen, B.C.1    O'Connell, T.D.2    Simpson, P.C.3
  • 31
    • 84859651420 scopus 로고    scopus 로고
    • Mechanism of voltage gating in potassium channels
    • doi: 10.1126/science.1216533
    • Jensen, M. O., Jogini, V., Borhani, D. W., Leffler, A. E., Dror, R. O., and Shaw, D. E. (2012). Mechanism of voltage gating in potassium channels. Science 336, 229-233. doi: 10.1126/science.1216533.
    • (2012) Science , vol.336 , pp. 229-233
    • Jensen, M.O.1    Jogini, V.2    Borhani, D.W.3    Leffler, A.E.4    Dror, R.O.5    Shaw, D.E.6
  • 32
    • 42949108787 scopus 로고    scopus 로고
    • Ion channels as drug targets: the next GPSCRs
    • doi: 10.1085/jgp.200709946
    • Kaczorowski, G. J., McManus, O. B., Priest, B. T., and Garcia, M. L. (2008). Ion channels as drug targets: the next GPSCRs. J. Gen. Physiol. 131, 399-405. doi: 10.1085/jgp.200709946.
    • (2008) J. Gen. Physiol. , vol.131 , pp. 399-405
    • Kaczorowski, G.J.1    McManus, O.B.2    Priest, B.T.3    Garcia, M.L.4
  • 33
    • 77951278810 scopus 로고    scopus 로고
    • Electrochemical coupling in the voltage-dependent phosphatase Ci-VSP
    • doi: 10.1038/nchembio.349
    • Kohout, S. C., Bell, S. C., Liu, L., Xu, Q., Minor, D. L., and Isacoff, E. Y. (2010). Electrochemical coupling in the voltage-dependent phosphatase Ci-VSP. Nat. Chem. Biol. 6, 369-375. doi: 10.1038/nchembio.349.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 369-375
    • Kohout, S.C.1    Bell, S.C.2    Liu, L.3    Xu, Q.4    Minor, D.L.5    Isacoff, E.Y.6
  • 34
    • 84866146025 scopus 로고    scopus 로고
    • Regulation of voltage-gated potassium channels by PI(4,5)P2
    • doi: 10.1085/jgp.201210806
    • Kruse, M., Hammond, G. R. V., and Hille, B. (2012). Regulation of voltage-gated potassium channels by PI(4,5)P2. J. Gen. Physiol. 140, 189-205. doi: 10.1085/jgp.201210806.
    • (2012) J. Gen. Physiol. , vol.140 , pp. 189-205
    • Kruse, M.1    Hammond, G.R.V.2    Hille, B.3
  • 35
    • 0032894433 scopus 로고    scopus 로고
    • Mutations in the S4 region isolate the final voltage-dependent cooperative step in potassium channel activation
    • doi: 10.1085/jgp.113.3.389
    • Ledwell, J. L., and Aldrich, R. W. (1999). Mutations in the S4 region isolate the final voltage-dependent cooperative step in potassium channel activation. J. Gen. Physiol. 113, 389-414. doi: 10.1085/jgp.113.3.389.
    • (1999) J. Gen. Physiol. , vol.113 , pp. 389-414
    • Ledwell, J.L.1    Aldrich, R.W.2
  • 36
    • 66149157329 scopus 로고    scopus 로고
    • Two separate interfaces between the voltage sensor and pore are required for the function of voltage-dependent K(+) channels
    • e47. doi: 10.1371/journal.pbio.1000047
    • Lee, S.-Y., Banerjee, A., and MacKinnon, R. (2009). Two separate interfaces between the voltage sensor and pore are required for the function of voltage-dependent K(+) channels. PLoS Biol. 7:e47. doi: 10.1371/journal.pbio.1000047.
    • (2009) PLoS Biol. , vol.7
    • Lee, S.-Y.1    Banerjee, A.2    MacKinnon, R.3
  • 37
    • 27344432813 scopus 로고    scopus 로고
    • + channel open probability by phosphatidylinositol 4,5-bisphosphate
    • doi: 10.1523/JNEUROSCI.2597-05.2005
    • + channel open probability by phosphatidylinositol 4,5-bisphosphate. J. Neurosci. 25, 9825-9835. doi: 10.1523/JNEUROSCI.2597-05.2005.
    • (2005) J. Neurosci. , vol.25 , pp. 9825-9835
    • Li, Y.1    Gamper, N.2    Hilgemann, D.W.3    Shapiro, M.S.4
  • 39
    • 79959352977 scopus 로고    scopus 로고
    • KCNE1 enhances phosphatidylinositol 4,5-bisphosphate (PIP2) sensitivity of IKs to modulate channel activity
    • doi: 10.1073/pnas.1100872108
    • Li, Y., Zaydman, M. A., Wu, D., Shi, J., Guan, M., Virgin-Downey, B., et al. (2011). KCNE1 enhances phosphatidylinositol 4,5-bisphosphate (PIP2) sensitivity of IKs to modulate channel activity. Proc. Natl. Acad. Sci. U.S.A. 108, 9095-9100. doi: 10.1073/pnas.1100872108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 9095-9100
    • Li, Y.1    Zaydman, M.A.2    Wu, D.3    Shi, J.4    Guan, M.5    Virgin-Downey, B.6
  • 40
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • doi: 10.1126/science.1174621
    • Lingwood, D., and Simons, K. (2009). Lipid rafts as a membrane-organizing principle. Science 327, 46-50. doi: 10.1126/science.1174621.
    • (2009) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 41
    • 77955583928 scopus 로고    scopus 로고
    • Channelopathies linked to plasma membrane phosphoinositides
    • doi: 10.1007/s00424-010-0828-y
    • Logothetis, D. E., Petrou, V. I., Adney, S. K., and Mahajan, R. (2010). Channelopathies linked to plasma membrane phosphoinositides. Pflügers Arch. 460, 321-341. doi: 10.1007/s00424-010-0828-y.
    • (2010) Pflügers Arch. , vol.460 , pp. 321-341
    • Logothetis, D.E.1    Petrou, V.I.2    Adney, S.K.3    Mahajan, R.4
  • 42
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: structural basis of electromechanical coupling
    • doi: 10.1126/science.1116270
    • Long, S. B. (2005). Voltage sensor of Kv1.2: structural basis of electromechanical coupling. Science 309, 903-908. doi: 10.1126/science.1116270.
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1
  • 44
    • 36248982122 scopus 로고    scopus 로고
    • + channel in a lipid membrane-like environment
    • doi: 10.1038/nature06265
    • + channel in a lipid membrane-like environment. Nature 450, 376-382. doi: 10.1038/nature06265.
    • (2007) Nature , vol.450 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 46
    • 0035950089 scopus 로고    scopus 로고
    • Ion conduction pore is conserved among potassium channels
    • doi: 10.1038/35101535
    • Lu, Z., Klem, A. M., and Ramu, Y. (2001). Ion conduction pore is conserved among potassium channels. Nature 413, 809-813. doi: 10.1038/35101535.
    • (2001) Nature , vol.413 , pp. 809-813
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 48
    • 79951841829 scopus 로고    scopus 로고
    • Allosteric features of KCNQ1 gating revealed by alanine scanning mutagenesis
    • doi: 10.1016/j.bpj.2010.12.3726
    • Ma, L.-J., Ohmert, I., and Vardanyan, V. (2011). Allosteric features of KCNQ1 gating revealed by alanine scanning mutagenesis. Biophys. J. 100, 885-894. doi: 10.1016/j.bpj.2010.12.3726.
    • (2011) Biophys. J. , vol.100 , pp. 885-894
    • Ma, L.-J.1    Ohmert, I.2    Vardanyan, V.3
  • 49
    • 0030048243 scopus 로고    scopus 로고
    • Direct physical measure of conformational rearrangement underlying potassium channel gating
    • doi: 10.1126/science.271.5246.213
    • Mannuzzu, L. M., Moronne, M. M., and Isacoff, E. Y. (1996). Direct physical measure of conformational rearrangement underlying potassium channel gating. Science 271, 213-216. doi: 10.1126/science.271.5246.213.
    • (1996) Science , vol.271 , pp. 213-216
    • Mannuzzu, L.M.1    Moronne, M.M.2    Isacoff, E.Y.3
  • 50
    • 63349094727 scopus 로고    scopus 로고
    • PKC activation and PIP2 depletion underlie biphasic regulation of IKs by Gq-coupled receptors
    • doi: 10.1016/j.yjmcc.2009.02.006
    • Matavel, A., and Lopes, C. M. B. (2009). PKC activation and PIP2 depletion underlie biphasic regulation of IKs by Gq-coupled receptors. J. Mol. Cell. Cardiol. 46, 704-712. doi: 10.1016/j.yjmcc.2009.02.006.
    • (2009) J. Mol. Cell. Cardiol. , vol.46 , pp. 704-712
    • Matavel, A.1    Lopes, C.M.B.2
  • 51
    • 85044710038 scopus 로고    scopus 로고
    • PKA and PKC partially rescue Long QT type 1 phenotype by restoring channel-PIP2 interactions
    • doi: 10.4161/chan.4.1.10227
    • Matavel, A., Medei, E., and Lopes, C. M. B. (2010). PKA and PKC partially rescue Long QT type 1 phenotype by restoring channel-PIP2 interactions. Channels 4, 3-11. doi: 10.4161/chan.4.1.10227.
    • (2010) Channels , vol.4 , pp. 3-11
    • Matavel, A.1    Medei, E.2    Lopes, C.M.B.3
  • 52
    • 0036082665 scopus 로고    scopus 로고
    • PIP(2) and proteins: interactions, organization, and information flow
    • doi: 10.1146/annurev.biophys.31.082901.134259
    • McLaughlin, S., Wang, J., Gambhir, A., and Murray, D. (2002). PIP(2) and proteins: interactions, organization, and information flow. Annu. Rev. Biophys. Biomol. Struct. 31, 151-175. doi: 10.1146/annurev.biophys.31.082901.134259.
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 151-175
    • McLaughlin, S.1    Wang, J.2    Gambhir, A.3    Murray, D.4
  • 53
    • 84867238397 scopus 로고    scopus 로고
    • KCNQ1 channels do not undergo concerted but sequential gating transitions in both the absence and the presence of KCNE1 protein
    • doi: 10.1074/jbc.M112.364901
    • Meisel, E., Meidan, D., Haitin, Y., Giladi, M., Peretz, A., and Attali, B. (2012). KCNQ1 channels do not undergo concerted but sequential gating transitions in both the absence and the presence of KCNE1 protein. J. Biol. Chem. 287, 34212-34224. doi: 10.1074/jbc.M112.364901.
    • (2012) J. Biol. Chem. , vol.287 , pp. 34212-34224
    • Meisel, E.1    Meidan, D.2    Haitin, Y.3    Giladi, M.4    Peretz, A.5    Attali, B.6
  • 54
    • 70349840420 scopus 로고    scopus 로고
    • Interactions between lipids and voltage sensor paddles detected with tarantula toxins
    • doi: 10.1038/nsmb.1679
    • Milescu, M., Bosmans, F., Lee, S., Alabi, A. A., Kim, J. I., and Swartz, K. J. (2009). Interactions between lipids and voltage sensor paddles detected with tarantula toxins. Nat. Struct. Mol. Biol. 16, 1080-1085. doi: 10.1038/nsmb.1679.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1080-1085
    • Milescu, M.1    Bosmans, F.2    Lee, S.3    Alabi, A.A.4    Kim, J.I.5    Swartz, K.J.6
  • 55
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • doi: 10.1038/nature03650
    • Murata, Y., Iwasaki, H., Sasaki, M., Inaba, K., and Okamura, Y. (2005). Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. Nature 435, 1239-1243. doi: 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
  • 56
    • 34548725637 scopus 로고    scopus 로고
    • Depolarization activates the phosphoinositide phosphatase Ci-VSP, as detected in Xenopus oocytes coexpressing sensors of PIP2
    • doi: 10.1113/jphysiol.2007.134775
    • Murata, Y., and Okamura, Y. (2007). Depolarization activates the phosphoinositide phosphatase Ci-VSP, as detected in Xenopus oocytes coexpressing sensors of PIP2. J. Physiol. 583, 875-889. doi: 10.1113/jphysiol.2007.134775.
    • (2007) J. Physiol. , vol.583 , pp. 875-889
    • Murata, Y.1    Okamura, Y.2
  • 57
    • 28244433447 scopus 로고    scopus 로고
    • Protein kinase C shifts the voltage dependence of KCNQ/M channels expressed in Xenopus oocytes
    • doi: 10.1113/jphysiol.2005.094995
    • Nakajo, K., and Kubo, Y. (2005). Protein kinase C shifts the voltage dependence of KCNQ/M channels expressed in Xenopus oocytes. J. Physiol. 569, 59-74. doi: 10.1113/jphysiol.2005.094995.
    • (2005) J. Physiol. , vol.569 , pp. 59-74
    • Nakajo, K.1    Kubo, Y.2
  • 58
    • 0029015694 scopus 로고
    • A wortmannin-sensitive phosphatidylinositol 4-kinase that regulates hormone-sensitive pools of inositolphospholipids
    • doi: 10.1073/pnas.92.12.5317
    • Nakanishi, S., Catt, K. J., and Balla, T. (1995). A wortmannin-sensitive phosphatidylinositol 4-kinase that regulates hormone-sensitive pools of inositolphospholipids. Proc. Natl. Acad. Sci. U.S.A. 92, 5317. doi: 10.1073/pnas.92.12.5317.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5317
    • Nakanishi, S.1    Catt, K.J.2    Balla, T.3
  • 60
    • 0031054075 scopus 로고    scopus 로고
    • A novel mutation in the potassium channel gene KVLQT1 causes the Jervell and Lange-Nielsen cardioauditory syndrome
    • doi: 10.1038/ng0297-186
    • Neyroud, N., Tesson, F., Denjoy, I., Leibovici, M., Donger, C., Barhanin, J., et al. (1997). A novel mutation in the potassium channel gene KVLQT1 causes the Jervell and Lange-Nielsen cardioauditory syndrome. Nat. Genet. 15, 186-189. doi: 10.1038/ng0297-186.
    • (1997) Nat. Genet. , vol.15 , pp. 186-189
    • Neyroud, N.1    Tesson, F.2    Denjoy, I.3    Leibovici, M.4    Donger, C.5    Barhanin, J.6
  • 61
    • 59649119224 scopus 로고    scopus 로고
    • Voltage-sensing phosphatase: actions and potentials
    • doi: 10.1113/jphysiol.2008.163097
    • Okamura, Y., Murata, Y., and Iwasaki, H. (2009). Voltage-sensing phosphatase: actions and potentials. J. Physiol. 587, 513-520. doi: 10.1113/jphysiol.2008.163097.
    • (2009) J. Physiol. , vol.587 , pp. 513-520
    • Okamura, Y.1    Murata, Y.2    Iwasaki, H.3
  • 63
    • 84860802371 scopus 로고    scopus 로고
    • Allosteric gating mechanism underlies the flexible gating of KCNQ1 potassium channels
    • doi: 10.1073/pnas.1201582109
    • Osteen, J. D., Barro-Soria, R., Robey, S., Sampson, K. J., Kass, R. S., and Larsson, H. P. (2012). Allosteric gating mechanism underlies the flexible gating of KCNQ1 potassium channels. Proc. Natl. Acad. Sci. U.S.A. 109, 7103-7108. doi: 10.1073/pnas.1201582109.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 7103-7108
    • Osteen, J.D.1    Barro-Soria, R.2    Robey, S.3    Sampson, K.J.4    Kass, R.S.5    Larsson, H.P.6
  • 64
    • 78651087721 scopus 로고    scopus 로고
    • KCNE1 alters the voltage sensor movements necessary to open the KCNQ1 channel gate
    • doi: 10.1073/pnas.1016300108
    • Osteen, J. D., Gonzalez, C., Sampson, K. J., Iyer, V., Rebolledo, S., Larsson, H. P., et al. (2010). KCNE1 alters the voltage sensor movements necessary to open the KCNQ1 channel gate. Proc. Natl. Acad. Sci. U.S.A. 107, 22710-22715. doi: 10.1073/pnas.1016300108.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 22710-22715
    • Osteen, J.D.1    Gonzalez, C.2    Sampson, K.J.3    Iyer, V.4    Rebolledo, S.5    Larsson, H.P.6
  • 65
    • 17644388821 scopus 로고    scopus 로고
    • Impaired KCNQ1-KCNE1 and phosphatidylinositol-4,5-bisphosphate interaction underlies the long QT syndrome
    • doi: 10.1161/01.RES.0000161451.04649.a8
    • Park, K.-H., Piron, J., Dahimene, S., Merot, J., Baro, I., Escande, D., et al. (2005). Impaired KCNQ1-KCNE1 and phosphatidylinositol-4,5-bisphosphate interaction underlies the long QT syndrome. Circ. Res. 96, 730-739. doi: 10.1161/01.RES.0000161451.04649.a8.
    • (2005) Circ. Res. , vol.96 , pp. 730-739
    • Park, K.-H.1    Piron, J.2    Dahimene, S.3    Merot, J.4    Baro, I.5    Escande, D.6
  • 66
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • doi: 10.1038/nature10238
    • Payandeh, J., Scheuer, T., Zheng, N., and Catterall, W. A. (2011). The crystal structure of a voltage-gated sodium channel. Nature 475, 353-358. doi: 10.1038/nature10238.
    • (2011) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 67
    • 33750499977 scopus 로고    scopus 로고
    • Regulation of gating and rundown of HCN hyperpolarization-activated channels by exogenous and endogenous PIP2
    • doi: 10.1085/jgp.200609648
    • Pian, P., Bucchi, A., Robinson, R. B., and Siegelbaum, S. A. (2006). Regulation of gating and rundown of HCN hyperpolarization-activated channels by exogenous and endogenous PIP2. J. Gen. Physiol. 128, 593-604. doi: 10.1085/jgp.200609648.
    • (2006) J. Gen. Physiol. , vol.128 , pp. 593-604
    • Pian, P.1    Bucchi, A.2    Robinson, R.B.3    Siegelbaum, S.A.4
  • 69
    • 0031848480 scopus 로고    scopus 로고
    • Activation and inactivation of homomeric KvLQT1 potassium channels
    • doi: 10.1016/S0006-3495(98)77568-X
    • Pusch, M., Magrassi, R., Wollnik, B., and Conti, F. (1998). Activation and inactivation of homomeric KvLQT1 potassium channels. Biophys. J. 75, 785-792. doi: 10.1016/S0006-3495(98)77568-X.
    • (1998) Biophys. J. , vol.75 , pp. 785-792
    • Pusch, M.1    Magrassi, R.2    Wollnik, B.3    Conti, F.4
  • 70
    • 33646358260 scopus 로고    scopus 로고
    • A voltage-gated proton-selective channel lacking the pore domain
    • doi: 10.1038/nature04700
    • Ramsey, I. S., Moran, M. M., Chong, J. A., and Clapham, D. E. (2006). A voltage-gated proton-selective channel lacking the pore domain. Nature 440, 1213-1216. doi: 10.1038/nature04700.
    • (2006) Nature , vol.440 , pp. 1213-1216
    • Ramsey, I.S.1    Moran, M.M.2    Chong, J.A.3    Clapham, D.E.4
  • 71
    • 33747062707 scopus 로고    scopus 로고
    • Enzymatic activation of voltage-gated potassium channels
    • doi: 10.1038/nature04880
    • Ramu, Y., Xu, Y., and Lu, Z. (2006). Enzymatic activation of voltage-gated potassium channels. Nature 442, 696-699. doi: 10.1038/nature04880.
    • (2006) Nature , vol.442 , pp. 696-699
    • Ramu, Y.1    Xu, Y.2    Lu, Z.3
  • 73
    • 34548614145 scopus 로고    scopus 로고
    • Molecular characteristics of phosphoinositide binding
    • doi: 10.1007/s00424-007-0291-6
    • Rosenhouse-Dantsker, A., and Logothetis, D. E. (2007). Molecular characteristics of phosphoinositide binding. Pflugers Arch. 455, 45-53. doi: 10.1007/s00424-007-0291-6.
    • (2007) Pflugers Arch. , vol.455 , pp. 45-53
    • Rosenhouse-Dantsker, A.1    Logothetis, D.E.2
  • 74
    • 33645274673 scopus 로고    scopus 로고
    • Analyzing phosphoinositides and their interacting proteins
    • doi: 10.1038/nmeth867
    • Rusten, T. E., and Stenmark, H. (2006). Analyzing phosphoinositides and their interacting proteins. Nat. Methods 3, 251-258. doi: 10.1038/nmeth867.
    • (2006) Nat. Methods , vol.3 , pp. 251-258
    • Rusten, T.E.1    Stenmark, H.2
  • 75
    • 84870776387 scopus 로고    scopus 로고
    • Charge movement in gating-locked HCN channels reveals weak coupling of voltage sensors and gate
    • doi: 10.1085/jgp.201210850
    • Ryu, S., and Yellen, G. (2012). Charge movement in gating-locked HCN channels reveals weak coupling of voltage sensors and gate. J. Gen. Physiol. 140, 469-479. doi: 10.1085/jgp.201210850.
    • (2012) J. Gen. Physiol. , vol.140 , pp. 469-479
    • Ryu, S.1    Yellen, G.2
  • 76
    • 0029854263 scopus 로고    scopus 로고
    • Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks) potassium channel
    • doi: 10.1038/384080a0
    • Sanguinetti, M. C., Curran, M. E., Zou, A., Shen, J., Spector, P. S., Atkinson, D. L., et al. (1996). Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks) potassium channel. Nature 384, 80-83. doi: 10.1038/384080a0.
    • (1996) Nature , vol.384 , pp. 80-83
    • Sanguinetti, M.C.1    Curran, M.E.2    Zou, A.3    Shen, J.4    Spector, P.S.5    Atkinson, D.L.6
  • 78
    • 59649113542 scopus 로고    scopus 로고
    • + channel. III. Functional reconstitution of a sensorless pore module from a prokaryotic Kv channel
    • doi: 10.1085/jgp.200810077
    • + channel. III. Functional reconstitution of a sensorless pore module from a prokaryotic Kv channel. J. Gen. Physiol. 132, 651-666. doi: 10.1085/jgp.200810077.
    • (2008) J. Gen. Physiol. , vol.132 , pp. 651-666
    • Santos, J.S.1    Grigoriev, S.M.2    Montal, M.3
  • 79
    • 33646229810 scopus 로고    scopus 로고
    • A voltage sensor-domain protein is a voltage-gated proton channel
    • doi: 10.1126/science.1122352
    • Sasaki, M. (2006). A voltage sensor-domain protein is a voltage-gated proton channel. Science 312, 589-592. doi: 10.1126/science.1122352.
    • (2006) Science , vol.312 , pp. 589-592
    • Sasaki, M.1
  • 80
    • 33845637597 scopus 로고    scopus 로고
    • Phospholipids and the origin of cationic gating charges in voltage sensors
    • doi: 10.1038/nature05416
    • Schmidt, D., Jiang, Q.-X., and MacKinnon, R. (2006). Phospholipids and the origin of cationic gating charges in voltage sensors. Nature 444, 775-779. doi: 10.1038/nature05416.
    • (2006) Nature , vol.444 , pp. 775-779
    • Schmidt, D.1    Jiang, Q.-X.2    MacKinnon, R.3
  • 81
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant shaker potassium channels
    • doi: 10.1126/science.1553560
    • Schoppa, N. E., McCormack, K., Tanouye, M. A., and Sigworth, F. J. (1992). The size of gating charge in wild-type and mutant shaker potassium channels. Science 255, 1712-1715. doi: 10.1126/science.1553560.
    • (1992) Science , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1    McCormack, K.2    Tanouye, M.A.3    Sigworth, F.J.4
  • 83
    • 79961050460 scopus 로고    scopus 로고
    • Voltage-gated sodium channel (NaV) protein dissection creates a set of functional pore-only proteins
    • doi: 10.1073/pnas.1106811108
    • Shaya, D., Kreir, M., Robbins, R. A., Wong, S., Hammon, J., Brüggemann, A., et al. (2011). Voltage-gated sodium channel (NaV) protein dissection creates a set of functional pore-only proteins. Proc. Natl. Acad. Sci. U.S.A. 108, 12313-12318. doi: 10.1073/pnas.1106811108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 12313-12318
    • Shaya, D.1    Kreir, M.2    Robbins, R.A.3    Wong, S.4    Hammon, J.5    Brüggemann, A.6
  • 84
    • 23744452789 scopus 로고    scopus 로고
    • Cholinergic suppression of KCNQ channel currents enhances excitability of striatal medium spiny neurons
    • doi: 10.1523/JNEUROSCI.1381-05.2005
    • Shen, W. (2005). Cholinergic suppression of KCNQ channel currents enhances excitability of striatal medium spiny neurons. J. Neurosci. 25, 7449-7458. doi: 10.1523/JNEUROSCI.1381-05.2005.
    • (2005) J. Neurosci. , vol.25 , pp. 7449-7458
    • Shen, W.1
  • 85
    • 37049009981 scopus 로고    scopus 로고
    • Structural models for the KCNQ1 voltage-gated potassium channel
    • doi: 10.1021/bi701597s
    • Smith, J., Vanoye, C. G., George, A. L. Jr., Meiler, J., and Sanders, C. R. (2007). Structural models for the KCNQ1 voltage-gated potassium channel. Biochemistry 46, 14141-14152. doi: 10.1021/bi701597s.
    • (2007) Biochemistry , vol.46 , pp. 14141-14152
    • Smith, J.1    Vanoye, C.G.2    George Jr., A.L.3    Meiler, J.4    Sanders, C.R.5
  • 86
    • 33750975638 scopus 로고    scopus 로고
    • Functional interactions at the interface between voltage-sensing and pore domains in the Shaker K(v) channel
    • doi: 10.1016/j.neuron.2006.10.005
    • Soler-Llavina, G. J., Chang, T.-H., and Swartz, K. J. (2006). Functional interactions at the interface between voltage-sensing and pore domains in the Shaker K(v) channel. Neuron 52, 623-634. doi: 10.1016/j.neuron.2006.10.005.
    • (2006) Neuron , vol.52 , pp. 623-634
    • Soler-Llavina, G.J.1    Chang, T.-H.2    Swartz, K.J.3
  • 87
    • 0036683972 scopus 로고    scopus 로고
    • Recovery from muscarinic modulation of M current chanels requires phosphatidyinositol 4,5-bisphosphate
    • doi: 10.1016/S0896-6273(02)00790-0
    • Suh, B.-C., and Hille, B. (2002). Recovery from muscarinic modulation of M current chanels requires phosphatidyinositol 4,5-bisphosphate. Neuron 35, 507-520. doi: 10.1016/S0896-6273(02)00790-0.
    • (2002) Neuron , vol.35 , pp. 507-520
    • Suh, B.-C.1    Hille, B.2
  • 88
    • 20444428008 scopus 로고    scopus 로고
    • Regulation of ion channels by phosphatidylinositol 4,5-bisphosphate
    • doi: 10.1016/j.conb.2005.05.005
    • Suh, B.-C., and Hille, B. (2005). Regulation of ion channels by phosphatidylinositol 4,5-bisphosphate. Curr. Opin. Neurobiol. 15, 370-378. doi: 10.1016/j.conb.2005.05.005.
    • (2005) Curr. Opin. Neurobiol. , vol.15 , pp. 370-378
    • Suh, B.-C.1    Hille, B.2
  • 89
    • 34547101694 scopus 로고    scopus 로고
    • Regulation of KCNQ channels by manipulation of phosphoinositides
    • doi: 10.1113/jphysiol.2007.132647
    • Suh, B.-C., and Hille, B. (2007a). Regulation of KCNQ channels by manipulation of phosphoinositides. J. Physiol. 582(Pt 3), 911-916. doi: 10.1113/jphysiol.2007.132647.
    • (2007) J. Physiol. , vol.582 , Issue.PART 3 , pp. 911-916
    • Suh, B.-C.1    Hille, B.2
  • 90
    • 34548813681 scopus 로고    scopus 로고
    • + channels
    • doi: 10.1085/jgp.200709821
    • + channels. J. Gen. Physiol. 130, 241-256. doi: 10.1085/jgp.200709821.
    • (2007) J. Gen. Physiol. , vol.130 , pp. 241-256
    • Suh, B.-C.1    Hille, B.2
  • 91
    • 48249116482 scopus 로고    scopus 로고
    • PIP2 is a necessary cofactor for ion channel function: how and why?
    • doi: 10.1146/annurev.biophys.37.032807.125859
    • Suh, B.-C., and Hille, B. (2008). PIP2 is a necessary cofactor for ion channel function: how and why? Annu. Rev. Biophys. 37, 175-195. doi: 10.1146/annurev.biophys.37.032807.125859.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 175-195
    • Suh, B.-C.1    Hille, B.2
  • 92
    • 33845310879 scopus 로고    scopus 로고
    • Rapid chemically induced changes of ptdins(4,5)P2 gate KCNQ ion channels
    • doi: 10.1126/science.1131163
    • Suh, B.-C., Inoue, T., Meyer, T., and Hille, B. (2006). Rapid chemically induced changes of ptdins(4,5)P2 gate KCNQ ion channels. Sci. Signal. 314, 1454. doi: 10.1126/science.1131163.
    • (2006) Sci. Signal. , vol.314 , pp. 1454
    • Suh, B.-C.1    Inoue, T.2    Meyer, T.3    Hille, B.4
  • 93
    • 77955488732 scopus 로고    scopus 로고
    • Modulation of high-voltage activated Ca(2+) channels by membrane phosphatidylinositol 4,5-bisphosphate
    • doi: 10.1016/j.neuron.2010.07.001
    • Suh, B.-C., Leal, K., and Hille, B. (2010). Modulation of high-voltage activated Ca(2+) channels by membrane phosphatidylinositol 4,5-bisphosphate. Neuron 67, 224-238. doi: 10.1016/j.neuron.2010.07.001.
    • (2010) Neuron , vol.67 , pp. 224-238
    • Suh, B.-C.1    Leal, K.2    Hille, B.3
  • 94
    • 84863997405 scopus 로고    scopus 로고
    • Distinct subunit contributions to the activation of M-type potassium channels by PI(4,5)P2
    • doi: 10.1085/jgp.201210796
    • Telezhkin, V., Brown, D. A., and Gibb, A. J. (2012a). Distinct subunit contributions to the activation of M-type potassium channels by PI(4,5)P2. J. Gen. Physiol. 140, 41-53. doi: 10.1085/jgp.201210796.
    • (2012) J. Gen. Physiol. , vol.140 , pp. 41-53
    • Telezhkin, V.1    Brown, D.A.2    Gibb, A.J.3
  • 95
    • 84858965573 scopus 로고    scopus 로고
    • Structural requirements of membrane phospholipids for M-type potassium channel activation and binding
    • doi: 10.1074/jbc.M111.322552
    • Telezhkin, V., Reilly, J. M., Thomas, A. M., Tinker, A., and Brown, D. A. (2012b). Structural requirements of membrane phospholipids for M-type potassium channel activation and binding. J. Biol. Chem. 287, 10001-10012. doi: 10.1074/jbc.M111.322552.
    • (2012) J. Biol. Chem. , vol.287 , pp. 10001-10012
    • Telezhkin, V.1    Reilly, J.M.2    Thomas, A.M.3    Tinker, A.4    Brown, D.A.5
  • 96
    • 84879845707 scopus 로고    scopus 로고
    • A basic residue in the proximal C-terminus is necessary for efficient activation of the M-channel subunit Kv7.2 by PI(4,5)P2
    • doi: 10.1007/s00424-012-1199-3
    • Telezhkin, V., Thomas, A. M., Harmer, S. C., Tinker, A., and Brown, D. A. (2013). A basic residue in the proximal C-terminus is necessary for efficient activation of the M-channel subunit Kv7.2 by PI(4,5)P2. Pflgers Arch. 465, 945-953. doi: 10.1007/s00424-012-1199-3.
    • (2013) Pflgers Arch. , vol.465 , pp. 945-953
    • Telezhkin, V.1    Thomas, A.M.2    Harmer, S.C.3    Tinker, A.4    Brown, D.A.5
  • 97
    • 78751564282 scopus 로고    scopus 로고
    • Characterization of a binding site for anionic phospholipids on KCNQ1
    • doi: 10.1074/jbc.M110.153551
    • Thomas, A. M., Harmer, S. C., Khambra, T., and Tinker, A. (2011). Characterization of a binding site for anionic phospholipids on KCNQ1. J. Biol. Chem. 286, 2088-2100. doi: 10.1074/jbc.M110.153551.
    • (2011) J. Biol. Chem. , vol.286 , pp. 2088-2100
    • Thomas, A.M.1    Harmer, S.C.2    Khambra, T.3    Tinker, A.4
  • 98
    • 33646135082 scopus 로고    scopus 로고
    • Environment of the gating charges in the Kv1.2 Shaker potassium channel
    • doi: 10.1529/biophysj.106.080754
    • Treptow, W., and Tarek, M. (2006). Environment of the gating charges in the Kv1.2 Shaker potassium channel. Biophys. J. 90, L64-L66. doi: 10.1529/biophysj.106.080754.
    • (2006) Biophys. J. , vol.90
    • Treptow, W.1    Tarek, M.2
  • 100
    • 48749110968 scopus 로고    scopus 로고
    • Direct regulation of BK channels by phosphatidylinositol 4,5-bisphosphate as a novel signaling pathway
    • doi: 10.1085/jgp.200709913
    • Vaithianathan, T., Bukiya, A., Liu, J., Liu, P., Asuncion-Chin, M., Fan, Z., et al. (2008). Direct regulation of BK channels by phosphatidylinositol 4,5-bisphosphate as a novel signaling pathway. J. Gen. Physiol. 132, 13-28. doi: 10.1085/jgp.200709913.
    • (2008) J. Gen. Physiol. , vol.132 , pp. 13-28
    • Vaithianathan, T.1    Bukiya, A.2    Liu, J.3    Liu, P.4    Asuncion-Chin, M.5    Fan, Z.6
  • 102
    • 0032483972 scopus 로고    scopus 로고
    • KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates of the M-channel
    • doi: 10.1126/science.282.5395.1890
    • Wang, H. S., Pan, Z., Shi, W., Brown, B. S., Wymore, R. S., Cohen, I. S., et al. (1998). KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates of the M-channel. Science 282, 1890-1893. doi: 10.1126/science.282.5395.1890.
    • (1998) Science , vol.282 , pp. 1890-1893
    • Wang, H.S.1    Pan, Z.2    Shi, W.3    Brown, B.S.4    Wymore, R.S.5    Cohen, I.S.6
  • 103
    • 9044240040 scopus 로고    scopus 로고
    • Positional cloning of a novel potassium channel gene: KVLQT1 mutations cause cardiac arrhythmias
    • doi: 10.1038/ng0196-17
    • Wang, Q., Curran, M. E., Splawski, I., Burn, T. C., Millholland, J. M., VanRaay, T. J., et al. (1996). Positional cloning of a novel potassium channel gene: KVLQT1 mutations cause cardiac arrhythmias. Nat. Genet. 12, 17-23. doi: 10.1038/ng0196-17.
    • (1996) Nat. Genet. , vol.12 , pp. 17-23
    • Wang, Q.1    Curran, M.E.2    Splawski, I.3    Burn, T.C.4    Millholland, J.M.5    VanRaay, T.J.6
  • 104
    • 80053485088 scopus 로고    scopus 로고
    • + channel and gating regulation by G proteins, PIP2, and sodium
    • doi: 10.1016/j.cell.2011.07.046
    • + channel and gating regulation by G proteins, PIP2, and sodium. Cell 147, 199-208. doi: 10.1016/j.cell.2011.07.046.
    • (2011) Cell , vol.147 , pp. 199-208
    • Whorton, M.R.1    MacKinnon, R.2
  • 105
    • 0037206832 scopus 로고    scopus 로고
    • Dual regulation of voltage-gated calcium channels by PtdIns(4,5)P2
    • doi: 10.1038/nature01118
    • Wu, L., Bauer, C. S., Zhen, X.-G., Xie, C., and Yang, J. (2002). Dual regulation of voltage-gated calcium channels by PtdIns(4,5)P2. Nature 419, 947-952. doi: 10.1038/nature01118.
    • (2002) Nature , vol.419 , pp. 947-952
    • Wu, L.1    Bauer, C.S.2    Zhen, X.-G.3    Xie, C.4    Yang, J.5
  • 106
    • 39149109885 scopus 로고    scopus 로고
    • + channels
    • doi: 10.1038/nature06618
    • + channels. Nature 451, 826-830. doi: 10.1038/nature06618.
    • (2008) Nature , vol.451 , pp. 826-830
    • Xu, Y.1    Ramu, Y.2    Lu, Z.3
  • 107
    • 0032417420 scopus 로고    scopus 로고
    • The moving parts of voltage-gated ion channels
    • doi: 10.1017/S0033583598003448
    • Yellen, G. (1998). The moving parts of voltage-gated ion channels. Q. Rev. Biophys. 31, 239-295. doi: 10.1017/S0033583598003448.
    • (1998) Q. Rev. Biophys. , vol.31 , pp. 239-295
    • Yellen, G.1
  • 108
    • 0028140472 scopus 로고
    • Shaker potassium channel gating. III: evaluation of kinetic models for activation
    • doi: 10.1085/jgp.103.2.321
    • Zagotta, W. N., Hoshi, T., and Aldrich, R. W. (1994). Shaker potassium channel gating. III: evaluation of kinetic models for activation. J. Gen. Physiol. 103, 321-362. doi: 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
  • 109
    • 84870938851 scopus 로고    scopus 로고
    • Ion channel associated diseases: overview of molecular mechanisms
    • doi: 10.1021/cr300360k
    • Zaydman, M. A., Silva, J. R., and Cui, J. (2012). Ion channel associated diseases: overview of molecular mechanisms. Chem. Rev. 112, 6319-6333. doi: 10.1021/cr300360k.
    • (2012) Chem. Rev. , vol.112 , pp. 6319-6333
    • Zaydman, M.A.1    Silva, J.R.2    Cui, J.3
  • 110
    • 84881428576 scopus 로고    scopus 로고
    • Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening
    • doi: 10.1073/pnas.1305167110
    • Zaydman, M. A., Silva, J. R., Delaloye, K., Li, Y., Liang, H., Larsson, H. P., et al. (2013). Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening. Proc. Natl. Acad. Sci. U.S.A. 110, 13180-13185. doi: 10.1073/pnas.1305167110.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 13180-13185
    • Zaydman, M.A.1    Silva, J.R.2    Delaloye, K.3    Li, Y.4    Liang, H.5    Larsson, H.P.6
  • 111
    • 0037468826 scopus 로고    scopus 로고
    • PIP2 activates KCNQ channels, and its hydrolysis underlies receptor-mediated inhibition of M currents
    • doi: 10.1016/S0896-6273(03)00125-9
    • Zhang, H., Craciun, L., Mirshahi, T., Rohacs, T., Lopes, C., Jin, T., et al. (2003). PIP2 activates KCNQ channels, and its hydrolysis underlies receptor-mediated inhibition of M currents. Neuron 37, 963-975. doi: 10.1016/S0896-6273(03)00125-9.
    • (2003) Neuron , vol.37 , pp. 963-975
    • Zhang, H.1    Craciun, L.2    Mirshahi, T.3    Rohacs, T.4    Lopes, C.5    Jin, T.6
  • 112
    • 84890289929 scopus 로고    scopus 로고
    • 2 interactions with voltage sensor elements contribute to KCNQ2 channel gating
    • doi: 10.1073/pnas.1312483110
    • 2 interactions with voltage sensor elements contribute to KCNQ2 channel gating. Proc. Natl. Acad. Sci. U.S.A. 110, 20093-20098. doi: 10.1073/pnas.1312483110.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 20093-20098
    • Zhang, Q.1    Zhou, P.2    Chen, Z.3    Li, M.4    Jiang, H.5    Gao, Z.6
  • 113
    • 79953236295 scopus 로고    scopus 로고
    • Lipid-dependent gating of a voltage-gated potassium channel
    • doi: 10.1038/ncomms1254
    • Zheng, H., Liu, W., Anderson, L. Y., and Jiang, Q.-X. (2011). Lipid-dependent gating of a voltage-gated potassium channel. Nat. Commun. 2, 250. doi: 10.1038/ncomms1254.
    • (2011) Nat. Commun. , vol.2 , pp. 250
    • Zheng, H.1    Liu, W.2    Anderson, L.Y.3    Jiang, Q.-X.4
  • 114
    • 84878123925 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate alters pharmacological selectivity for epilepsy-causing KCNQ potassium channels
    • doi: 10.1073/pnas.1302167110
    • Zhou, P., Yu, H., Gu, M., Nan, F. J., Gao, Z., and Li, M. (2013). Phosphatidylinositol 4,5-bisphosphate alters pharmacological selectivity for epilepsy-causing KCNQ potassium channels. Proc. Natl. Acad. Sci. U.S.A. 110, 8725-8731. doi: 10.1073/pnas.1302167110.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 8725-8731
    • Zhou, P.1    Yu, H.2    Gu, M.3    Nan, F.J.4    Gao, Z.5    Li, M.6
  • 115
    • 33845438139 scopus 로고    scopus 로고
    • Pacemaking by HCN channels requires interaction with phosphoinositides
    • doi: 10.1016/j.neuron.2006.12.005
    • Zolles, G., Klöcker, N., Wenzel, D., Weisser-Thomas, J., Fleischmann, B. K., Roeper, J., et al. (2006). Pacemaking by HCN channels requires interaction with phosphoinositides. Neuron 52, 1027-1036. doi: 10.1016/j.neuron.2006.12.005.
    • (2006) Neuron , vol.52 , pp. 1027-1036
    • Zolles, G.1    Klöcker, N.2    Wenzel, D.3    Weisser-Thomas, J.4    Fleischmann, B.K.5    Roeper, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.