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Volumn 1838, Issue 5, 2014, Pages 1322-1331

Voltage-gated ion channel modulation by lipids: Insights from molecular dynamics simulations

Author keywords

Ceramide; Kv1.2; PIP2; Shaker; Sphingomyelin

Indexed keywords

LIPID; POTASSIUM CHANNEL KV1.2; SPHINGOMYELIN PHOSPHODIESTERASE; TRIPHOSPHOINOSITIDE;

EID: 84894553015     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2014.01.024     Document Type: Article
Times cited : (32)

References (64)
  • 1
    • 0034017867 scopus 로고    scopus 로고
    • The voltage sensor in voltage-dependent ion channels
    • F. Bezanilla The voltage sensor in voltage-dependent ion channels Physiol. Rev. 80 2000 555 592
    • (2000) Physiol. Rev. , vol.80 , pp. 555-592
    • Bezanilla, F.1
  • 2
    • 77956996917 scopus 로고    scopus 로고
    • Ion channel voltage sensors: Structure, function, and pathophysiology
    • W.A. Catterall Ion channel voltage sensors: structure, function, and pathophysiology Neuron 67 2010 915 928
    • (2010) Neuron , vol.67 , pp. 915-928
    • Catterall, W.A.1
  • 3
    • 16544379913 scopus 로고    scopus 로고
    • Structural biology. Voltage sensor meets lipid membrane
    • R. Mackinnon Structural biology. Voltage sensor meets lipid membrane Science 306 2004 1304 1305
    • (2004) Science , vol.306 , pp. 1304-1305
    • Mackinnon, R.1
  • 4
    • 84890652414 scopus 로고    scopus 로고
    • Omega currents in voltage-gated ion channels: What can we learn from uncovering the voltage-sensing mechanism using MD simulations?
    • M. Tarek, and L. Delemotte Omega currents in voltage-gated ion channels: what can we learn from uncovering the voltage-sensing mechanism using MD simulations? Acc. Chem. Res. 46 2013 2755 2762
    • (2013) Acc. Chem. Res. , vol.46 , pp. 2755-2762
    • Tarek, M.1    Delemotte, L.2
  • 9
    • 3142580385 scopus 로고    scopus 로고
    • A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom
    • S.-Y. Lee, and R. MacKinnon A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom Nature 430 2004 232 235
    • (2004) Nature , vol.430 , pp. 232-235
    • Lee, S.-Y.1    Mackinnon, R.2
  • 10
    • 61449172924 scopus 로고    scopus 로고
    • Conformational changes and slow dynamics through microsecond polarized atomistic molecular simulation of an integral Kv1.2 ion channel
    • P. Bjelkmar, P.S. Niemelä, I. Vattulainen, and E. Lindahl Conformational changes and slow dynamics through microsecond polarized atomistic molecular simulation of an integral Kv1.2 ion channel PLoS Comput. Biol. 5 2009 e1000289
    • (2009) PLoS Comput. Biol. , vol.5 , pp. 1000289
    • Bjelkmar, P.1    Niemelä, P.S.2    Vattulainen, I.3    Lindahl, E.4
  • 12
    • 34547628129 scopus 로고    scopus 로고
    • + channel in a membrane environment
    • + channel in a membrane environment Biophys. J. 93 2007 3070 3082
    • (2007) Biophys. J. , vol.93 , pp. 3070-3082
    • Jogini, V.1    Roux, B.2
  • 13
    • 33846785439 scopus 로고    scopus 로고
    • How does a voltage sensor interact with a lipid bilayer? Simulations of a potassium channel domain
    • (England)
    • Z.A. Sands, and M.S.P. Sansom How does a voltage sensor interact with a lipid bilayer? Simulations of a potassium channel domain Structure 1993 15 2007 235 244 (England)
    • (2007) Structure , vol.1993 , Issue.15 , pp. 235-244
    • Sands, Z.A.1    Sansom, M.S.P.2
  • 14
    • 33646135082 scopus 로고    scopus 로고
    • Environment of the gating charges in the Kv1.2 Shaker potassium channel
    • W. Treptow, and M. Tarek Environment of the gating charges in the Kv1.2 Shaker potassium channel Biophys. J. 90 2006 L64 L66
    • (2006) Biophys. J. , vol.90
    • Treptow, W.1    Tarek, M.2
  • 15
    • 1942532321 scopus 로고    scopus 로고
    • Computer simulation of the KvAP voltage-gated potassium channel: Steered molecular dynamics of the voltage sensor
    • L. Monticelli, K.M. Robertson, J.L. MacCallum, and D.P. Tieleman Computer simulation of the KvAP voltage-gated potassium channel: steered molecular dynamics of the voltage sensor FEBS Lett. 564 2004 325 332
    • (2004) FEBS Lett. , vol.564 , pp. 325-332
    • Monticelli, L.1    Robertson, K.M.2    Maccallum, J.L.3    Tieleman, D.P.4
  • 17
    • 84871004046 scopus 로고    scopus 로고
    • An emerging consensus on voltage-dependent gating from computational modeling and molecular dynamics simulations
    • E. Vargas, V. Yarov-Yarovoy, F. Khalili-Araghi, W.A. Catterall, M.L. Klein, and M. Tarek et al. An emerging consensus on voltage-dependent gating from computational modeling and molecular dynamics simulations J. Gen. Physiol. 140 2012 587 594
    • (2012) J. Gen. Physiol. , vol.140 , pp. 587-594
    • Vargas, E.1    Yarov-Yarovoy, V.2    Khalili-Araghi, F.3    Catterall, W.A.4    Klein, M.L.5    Tarek, M.6
  • 18
    • 79954991393 scopus 로고    scopus 로고
    • Intermediate states of the Kv1.2 voltage sensor from atomistic molecular dynamics simulations
    • L. Delemotte, M. Tarek, M.L. Klein, C. Amaral, and W. Treptow Intermediate states of the Kv1.2 voltage sensor from atomistic molecular dynamics simulations Proc. Natl. Acad. Sci. U. S. A. 108 2011 6109 6114
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 6109-6114
    • Delemotte, L.1    Tarek, M.2    Klein, M.L.3    Amaral, C.4    Treptow, W.5
  • 20
    • 84866023433 scopus 로고    scopus 로고
    • Molecular dynamics simulations of voltage-gated cation channels: Insights on voltage-sensor domain function and modulation
    • L. Delemotte, M.L. Klein, and M. Tarek Molecular dynamics simulations of voltage-gated cation channels: insights on voltage-sensor domain function and modulation Front. Pharmacol. 3 2012 97
    • (2012) Front. Pharmacol. , vol.3 , pp. 97
    • Delemotte, L.1    Klein, M.L.2    Tarek, M.3
  • 21
    • 33845637597 scopus 로고    scopus 로고
    • Phospholipids and the origin of cationic gating charges in voltage sensors
    • D. Schmidt, Q.-X. Jiang, and R. MacKinnon Phospholipids and the origin of cationic gating charges in voltage sensors Nature 444 2006 775 779
    • (2006) Nature , vol.444 , pp. 775-779
    • Schmidt, D.1    Jiang, Q.-X.2    Mackinnon, R.3
  • 22
    • 79960146268 scopus 로고    scopus 로고
    • Structural dynamics of the S4 voltage-sensor helix in lipid bilayers lacking phosphate groups
    • M. Andersson, J.A. Freites, D.J. Tobias, and S.H. White Structural dynamics of the S4 voltage-sensor helix in lipid bilayers lacking phosphate groups J. Phys. Chem. B 115 2011 8732 8738
    • (2011) J. Phys. Chem. B , vol.115 , pp. 8732-8738
    • Andersson, M.1    Freites, J.A.2    Tobias, D.J.3    White, S.H.4
  • 23
    • 84885455379 scopus 로고    scopus 로고
    • Tuning voltage-gated channel activity and cellular excitability with a sphingomyelinase
    • D.J. Combs, H.-G. Shin, Y. Xu, Y. Ramu, and Z. Lu Tuning voltage-gated channel activity and cellular excitability with a sphingomyelinase J. Gen. Physiol. 142 2013 367 380
    • (2013) J. Gen. Physiol. , vol.142 , pp. 367-380
    • Combs, D.J.1    Shin, H.-G.2    Xu, Y.3    Ramu, Y.4    Lu, Z.5
  • 24
    • 33747062707 scopus 로고    scopus 로고
    • Enzymatic activation of voltage-gated potassium channels
    • Y. Ramu, Y. Xu, and Z. Lu Enzymatic activation of voltage-gated potassium channels Nature 442 2006 696 699
    • (2006) Nature , vol.442 , pp. 696-699
    • Ramu, Y.1    Xu, Y.2    Lu, Z.3
  • 27
    • 79955424191 scopus 로고    scopus 로고
    • Molecular mechanism underlying phosphatidylinositol 4,5-bisphosphate- induced inhibition of SpIH channels
    • G.E. Flynn, and W.N. Zagotta Molecular mechanism underlying phosphatidylinositol 4,5-bisphosphate-induced inhibition of SpIH channels J. Biol. Chem. 286 2011 15535 15542
    • (2011) J. Biol. Chem. , vol.286 , pp. 15535-15542
    • Flynn, G.E.1    Zagotta, W.N.2
  • 29
    • 0032546013 scopus 로고    scopus 로고
    • Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gbetagamma
    • C.L. Huang, S. Feng, and D.W. Hilgemann Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gbetagamma Nature 391 1998 803 806
    • (1998) Nature , vol.391 , pp. 803-806
    • Huang, C.L.1    Feng, S.2    Hilgemann, D.W.3
  • 30
    • 84866146025 scopus 로고    scopus 로고
    • Regulation of voltage-gated potassium channels by PI(4,5)P2
    • M. Kruse, G.R.V. Hammond, and B. Hille Regulation of voltage-gated potassium channels by PI(4,5)P2 J. Gen. Physiol. 140 2012 189 205
    • (2012) J. Gen. Physiol. , vol.140 , pp. 189-205
    • Kruse, M.1    Hammond, G.R.V.2    Hille, B.3
  • 32
    • 77958160884 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5-bisphosphate (PIP(2)) stabilizes the open pore conformation of the Kv11.1 (hERG) channel
    • N. Rodriguez, M.Y. Amarouch, J. Montnach, J. Piron, A.J. Labro, and F. Charpentier et al. Phosphatidylinositol-4,5-bisphosphate (PIP(2)) stabilizes the open pore conformation of the Kv11.1 (hERG) channel Biophys. J. 99 2010 1110 1118
    • (2010) Biophys. J. , vol.99 , pp. 1110-1118
    • Rodriguez, N.1    Amarouch, M.Y.2    Montnach, J.3    Piron, J.4    Labro, A.J.5    Charpentier, F.6
  • 33
    • 48249116482 scopus 로고    scopus 로고
    • PIP2 is a necessary cofactor for ion channel function: How and why?
    • B.-C. Suh, and B. Hille PIP2 is a necessary cofactor for ion channel function: how and why? Annu. Rev. Biophys. 37 2008 175 195
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 175-195
    • Suh, B.-C.1    Hille, B.2
  • 34
    • 80053485088 scopus 로고    scopus 로고
    • + channel and gating regulation by G proteins, PIP2, and sodium
    • + channel and gating regulation by G proteins, PIP2, and sodium Cell 147 2011 199 208
    • (2011) Cell , vol.147 , pp. 199-208
    • Whorton, M.R.1    Mackinnon, R.2
  • 35
    • 0037468826 scopus 로고    scopus 로고
    • PIP(2) activates KCNQ channels, and its hydrolysis underlies receptor-mediated inhibition of M currents
    • H. Zhang, L.C. Craciun, T. Mirshahi, T. Rohacs, C.M.B. Lopes, and T. Jin et al. PIP(2) activates KCNQ channels, and its hydrolysis underlies receptor-mediated inhibition of M currents Neuron 37 2003 963 975
    • (2003) Neuron , vol.37 , pp. 963-975
    • Zhang, H.1    Craciun, L.C.2    Mirshahi, T.3    Rohacs, T.4    Lopes, C.M.B.5    Jin, T.6
  • 37
    • 0002854502 scopus 로고    scopus 로고
    • Phosphoinositide-3-kinases - Regulation by cell surface receptors and function of 3-phosphorylated lipids
    • S. Cockcroft, Oxford University Press Oxford, UK
    • L. Stephens, A. McGregor, and P. Hawkins Phosphoinositide-3-kinases - regulation by cell surface receptors and function of 3-phosphorylated lipids S. Cockcroft, Biol. Phosphoinositides 2000 Oxford University Press Oxford, UK 32 107
    • (2000) Biol. Phosphoinositides , pp. 32-107
    • Stephens, L.1    McGregor, A.2    Hawkins, P.3
  • 40
    • 84866399905 scopus 로고    scopus 로고
    • Voltage-gated channel mechanosensitivity: Fact or friction?
    • C.E. Morris Voltage-gated channel mechanosensitivity: fact or friction? Front. Physiol. 2 2011 25
    • (2011) Front. Physiol. , vol.2 , pp. 25
    • Morris, C.E.1
  • 41
    • 0036112238 scopus 로고    scopus 로고
    • Membrane stretch accelerates activation and slow inactivation in Shaker channels with S3-S4 linker deletions
    • I.V. Tabarean, and C.E. Morris Membrane stretch accelerates activation and slow inactivation in Shaker channels with S3-S4 linker deletions Biophys. J. 82 2002 2982 2994
    • (2002) Biophys. J. , vol.82 , pp. 2982-2994
    • Tabarean, I.V.1    Morris, C.E.2
  • 42
    • 0842326193 scopus 로고    scopus 로고
    • Membrane tension accelerates rate-limiting voltage-dependent activation and slow inactivation steps in a Shaker channel
    • U. Laitko, and C.E. Morris Membrane tension accelerates rate-limiting voltage-dependent activation and slow inactivation steps in a Shaker channel J. Gen. Physiol. 123 2004 135 154
    • (2004) J. Gen. Physiol. , vol.123 , pp. 135-154
    • Laitko, U.1    Morris, C.E.2
  • 43
    • 69949118458 scopus 로고    scopus 로고
    • PACKMOL: A package for building initial configurations for molecular dynamics simulations
    • L. Martínez, R. Andrade, E.G. Birgin, and J.M. Martínez PACKMOL: a package for building initial configurations for molecular dynamics simulations J. Comput. Chem. 30 2009 2157 2164
    • (2009) J. Comput. Chem. , vol.30 , pp. 2157-2164
    • Martínez, L.1    Andrade, R.2    Birgin, E.G.3    Martínez, J.M.4
  • 44
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • A.D. Mackerell Jr., M. Feig, and C.L. Brooks III Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations J. Comput. Chem. 25 2004 1400 1415
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • Mackerell, Jr.A.D.1    Feig, M.2    Brooks III, C.L.3
  • 46
    • 0041694125 scopus 로고    scopus 로고
    • Molecular dynamics simulation of sphingomyelin bilayer
    • M.T. Hyvönen, and P.T. Kovanen Molecular dynamics simulation of sphingomyelin bilayer J. Phys. Chem. B 107 2003 9102 9108
    • (2003) J. Phys. Chem. B , vol.107 , pp. 9102-9108
    • Hyvönen, M.T.1    Kovanen, P.T.2
  • 48
    • 77049117291 scopus 로고    scopus 로고
    • A molecular dynamics investigation of lipid bilayer perturbation by PIP2
    • D. Lupyan, M. Mezei, D.E. Logothetis, and R. Osman A molecular dynamics investigation of lipid bilayer perturbation by PIP2 Biophys. J. 98 2010 240 247
    • (2010) Biophys. J. , vol.98 , pp. 240-247
    • Lupyan, D.1    Mezei, M.2    Logothetis, D.E.3    Osman, R.4
  • 50
    • 43949121752 scopus 로고    scopus 로고
    • Modeling membranes under a transmembrane potential
    • L. Delemotte, F. Dehez, W. Treptow, and M. Tarek Modeling membranes under a transmembrane potential J. Phys. Chem. B 112 2008 5547 5550
    • (2008) J. Phys. Chem. B , vol.112 , pp. 5547-5550
    • Delemotte, L.1    Dehez, F.2    Treptow, W.3    Tarek, M.4
  • 51
    • 67849095786 scopus 로고    scopus 로고
    • Initial response of the potassium channel voltage sensor to a transmembrane potential
    • W. Treptow, M. Tarek, and M.L. Klein Initial response of the potassium channel voltage sensor to a transmembrane potential J. Am. Chem. Soc. 131 2009 2107 2109
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2107-2109
    • Treptow, W.1    Tarek, M.2    Klein, M.L.3
  • 53
    • 0042191762 scopus 로고    scopus 로고
    • Ordering of water molecules between phospholipid bilayers visualized by coherent anti-Stokes Raman scattering microscopy
    • J.-X. Cheng, S. Pautot, D.A. Weitz, and X.S. Xie Ordering of water molecules between phospholipid bilayers visualized by coherent anti-Stokes Raman scattering microscopy Proc. Natl. Acad. Sci. 100 2003 9826 9830
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 9826-9830
    • Cheng, J.-X.1    Pautot, S.2    Weitz, D.A.3    Xie, X.S.4
  • 54
    • 84867841541 scopus 로고    scopus 로고
    • Molecular dynamics simulations of lipid membrane electroporation
    • L. Delemotte, and M. Tarek Molecular dynamics simulations of lipid membrane electroporation J. Membr. Biol. 245 2012 531 543
    • (2012) J. Membr. Biol. , vol.245 , pp. 531-543
    • Delemotte, L.1    Tarek, M.2
  • 55
    • 0026635481 scopus 로고
    • Membrane dipole potentials, hydration forces, and the ordering of water at membrane surfaces
    • K. Gawrisch, D. Ruston, J. Zimmerberg, V.A. Parsegian, R.P. Rand, and N. Fuller Membrane dipole potentials, hydration forces, and the ordering of water at membrane surfaces Biophys. J. 61 1992 1213 1223
    • (1992) Biophys. J. , vol.61 , pp. 1213-1223
    • Gawrisch, K.1    Ruston, D.2    Zimmerberg, J.3    Parsegian, V.A.4    Rand, R.P.5    Fuller, N.6
  • 56
    • 0001765178 scopus 로고    scopus 로고
    • Molecular dynamics study on electrostatic properties of a lipid bilayer: Polarization, electrostatic potential, and the effects on structure and dynamics of water near the interface
    • W. Shinoda, M. Shimizu, and S. Okazaki Molecular dynamics study on electrostatic properties of a lipid bilayer: polarization, electrostatic potential, and the effects on structure and dynamics of water near the interface J. Phys. Chem. B 102 1998 6647 6654
    • (1998) J. Phys. Chem. B , vol.102 , pp. 6647-6654
    • Shinoda, W.1    Shimizu, M.2    Okazaki, S.3
  • 57
    • 85029334138 scopus 로고    scopus 로고
    • Electroporation of lipid membranes
    • A. Pakhomov, D. Miklavcic, M. Markov, Taylor and Francis/CRC Press
    • L. Delemotte, and M. Tarek Electroporation of lipid membranes A. Pakhomov, D. Miklavcic, M. Markov, Adv. Electroporation Tech. Biol. Med 2010 Taylor and Francis/CRC Press 141 160
    • (2010) Adv. Electroporation Tech. Biol. Med , pp. 141-160
    • Delemotte, L.1    Tarek, M.2
  • 58
    • 33646416475 scopus 로고    scopus 로고
    • Aqueous solutions next to phospholipid membrane surfaces: Insights from simulations
    • M.L. Berkowitz, D.L. Bostick, and S. Pandit Aqueous solutions next to phospholipid membrane surfaces: insights from simulations Chem. Rev. 106 2006 1527 1539
    • (2006) Chem. Rev. , vol.106 , pp. 1527-1539
    • Berkowitz, M.L.1    Bostick, D.L.2    Pandit, S.3
  • 59
    • 0035201782 scopus 로고    scopus 로고
    • Molecular simulation of dioleoylphosphatidylcholine lipid bilayers at differing levels of hydration
    • R.J. Mashl, H.L. Scott, S. Subramaniam, and E. Jakobsson Molecular simulation of dioleoylphosphatidylcholine lipid bilayers at differing levels of hydration Biophys. J. 81 2001 3005 3015
    • (2001) Biophys. J. , vol.81 , pp. 3005-3015
    • Mashl, R.J.1    Scott, H.L.2    Subramaniam, S.3    Jakobsson, E.4
  • 60
    • 11144342719 scopus 로고    scopus 로고
    • Atomistic simulations of biologically realistic transmembrane potential gradients
    • J.N. Sachs, P.S. Crozier, and T.B. Woolf Atomistic simulations of biologically realistic transmembrane potential gradients J. Chem. Phys. 121 2004 10847 10851
    • (2004) J. Chem. Phys. , vol.121 , pp. 10847-10851
    • Sachs, J.N.1    Crozier, P.S.2    Woolf, T.B.3
  • 61
    • 0032863720 scopus 로고    scopus 로고
    • Structure of dipalmitoylphosphatidylcholine/cholesterol bilayer at low and high cholesterol concentrations: Molecular dynamics simulation
    • A.M. Smondyrev, and M.L. Berkowitz Structure of dipalmitoylphosphatidylcholine/cholesterol bilayer at low and high cholesterol concentrations: molecular dynamics simulation Biophys. J. 77 1999 2075 2089
    • (1999) Biophys. J. , vol.77 , pp. 2075-2089
    • Smondyrev, A.M.1    Berkowitz, M.L.2
  • 62
    • 78751564282 scopus 로고    scopus 로고
    • Characterization of a binding site for anionic phospholipids on KCNQ1
    • A.M. Thomas, S.C. Harmer, T. Khambra, and A. Tinker Characterization of a binding site for anionic phospholipids on KCNQ1 J. Biol. Chem. 286 2011 2088 2100
    • (2011) J. Biol. Chem. , vol.286 , pp. 2088-2100
    • Thomas, A.M.1    Harmer, S.C.2    Khambra, T.3    Tinker, A.4
  • 63
    • 84872535182 scopus 로고    scopus 로고
    • Simulation-based prediction of phosphatidylinositol 4,5-bisphosphate binding to an ion channel
    • M.R. Schmidt, P.J. Stansfeld, S.J. Tucker, and M.S.P. Sansom Simulation-based prediction of phosphatidylinositol 4,5-bisphosphate binding to an ion channel Biochemistry (Mosc) 52 2013 279 281
    • (2013) Biochemistry (Mosc) , vol.52 , pp. 279-281
    • Schmidt, M.R.1    Stansfeld, P.J.2    Tucker, S.J.3    Sansom, M.S.P.4


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