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Volumn 4 JAN, Issue , 2014, Pages

Phosphoinositide regulation of inward rectifier potassium (Kir) channels

Author keywords

Inward rectifier potassium channels; Ion channel; Ion channel gating; Kir channel; Ligand gated ion channels; Lipid protein interactions; Phosphoinositides

Indexed keywords


EID: 84893630211     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2013.00404     Document Type: Review
Times cited : (30)

References (71)
  • 1
    • 0032491319 scopus 로고    scopus 로고
    • PIP2 and PIP as determinants for ATP inhibition of KATP channels
    • doi: 10.1126/science.282.5391.1141
    • Baukrowitz, T., Schulte, U., Oliver, D., Herlitze, S., Krauter, T., Tucker, S. J., et al. (1998). PIP2 and PIP as determinants for ATP inhibition of KATP channels. Science 282, 1141-1144. doi: 10.1126/science.282.5391.1141.
    • (1998) Science , vol.282 , pp. 1141-1144
    • Baukrowitz, T.1    Schulte, U.2    Oliver, D.3    Herlitze, S.4    Krauter, T.5    Tucker, S.J.6
  • 2
    • 84856691589 scopus 로고    scopus 로고
    • Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating
    • doi: 10.1038/nsmb.2208
    • Bavro, V. N., De Zorzi, R., Schmidt, M. R., Muniz, J. R., Zubcevic, L., Sansom, M. S., et al. (2012). Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating. Nat. Struct. Mol. Biol. 19, 158-163. doi: 10.1038/nsmb.2208.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 158-163
    • Bavro, V.N.1    De Zorzi, R.2    Schmidt, M.R.3    Muniz, J.R.4    Zubcevic, L.5    Sansom, M.S.6
  • 3
    • 0014751652 scopus 로고
    • Voltage clamp experiments on ventricular myocarial fibres
    • Beeler, G. W. Jr., and Reuter, H. (1970). Voltage clamp experiments on ventricular myocarial fibres. J. Physiol. 207, 165-190.
    • (1970) J. Physiol. , vol.207 , pp. 165-190
    • Beeler Jr., G.W.1    Reuter, H.2
  • 4
    • 79551678672 scopus 로고    scopus 로고
    • Dual-Mode phospholipid regulation of human inward rectifying potassium channels
    • doi: 10.1016/j.bpj.2010.12.3724
    • Cheng, W. W., D'Avanzo, N., Doyle, D. A., and Nichols, C. G. (2011). Dual-Mode phospholipid regulation of human inward rectifying potassium channels. Biophys. J. 100, 620-628. doi: 10.1016/j.bpj.2010.12.3724.
    • (2011) Biophys. J. , vol.100 , pp. 620-628
    • Cheng, W.W.1    D'Avanzo, N.2    Doyle, D.A.3    Nichols, C.G.4
  • 5
    • 64549098161 scopus 로고    scopus 로고
    • KirBac1.1: it's an inward rectifying potassium channel
    • doi: 10.1085/jgp.200810125
    • Cheng, W. W., Enkvetchakul, D., and Nichols, C. G. (2009). KirBac1.1: it's an inward rectifying potassium channel. J. Gen. Physiol. 133, 295-305. doi: 10.1085/jgp.200810125.
    • (2009) J. Gen. Physiol. , vol.133 , pp. 295-305
    • Cheng, W.W.1    Enkvetchakul, D.2    Nichols, C.G.3
  • 6
    • 0036707499 scopus 로고    scopus 로고
    • 2-terminal positive charges in the activity of inward rectifier KATP channels
    • doi: 10.1085/jgp.20028621
    • 2-terminal positive charges in the activity of inward rectifier KATP channels. J. Gen. Physiol. 120, 437-446. doi: 10.1085/jgp.20028621.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 437-446
    • Cukras, C.A.1    Jeliazkova, I.2    Nichols, C.G.3
  • 7
    • 78549271737 scopus 로고    scopus 로고
    • Direct modulation of human inward rectifier K+ channels by membrane phosphatidylinositol 4,5-bisphosphate
    • doi: 10.1074/jbc.C110.186692
    • D'Avanzo, N., Cheng, W. W., Doyle, D. A., and Nichols, C. G. (2010a). Direct modulation of human inward rectifier K+ channels by membrane phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 285, 37129-37132. doi: 10.1074/jbc.C110.186692.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37129-37132
    • D'Avanzo, N.1    Cheng, W.W.2    Doyle, D.A.3    Nichols, C.G.4
  • 8
    • 77953903075 scopus 로고    scopus 로고
    • Lipids driving protein structure? Evolutionary adaptations in Kir channels
    • doi: 10.4161/chan.4.3.12129
    • D'Avanzo, N., Cheng, W. W., Wang, S., Enkvetchakul, D., and Nichols, C. G. (2010b). Lipids driving protein structure? Evolutionary adaptations in Kir channels. Channels (Austin) 4, 139-141. doi: 10.4161/chan.4.3.12129.
    • (2010) Channels (Austin) , vol.4 , pp. 139-141
    • D'Avanzo, N.1    Cheng, W.W.2    Wang, S.3    Enkvetchakul, D.4    Nichols, C.G.5
  • 9
    • 79955756236 scopus 로고    scopus 로고
    • Enantioselective protein-sterol interactions mediate regulation of both prokaryotic and eukaryotic inward rectifier K+ channels by cholesterol
    • doi: 10.1371/journal.pone.0019393
    • D'Avanzo, N., Hyrc, K., Enkvetchakul, D., Covey, D. F., and Nichols, C. G. (2011). Enantioselective protein-sterol interactions mediate regulation of both prokaryotic and eukaryotic inward rectifier K+ channels by cholesterol. PLoS ONE 6:e19393. doi: 10.1371/journal.pone.0019393.
    • (2011) PLoS ONE , vol.6
    • D'Avanzo, N.1    Hyrc, K.2    Enkvetchakul, D.3    Covey, D.F.4    Nichols, C.G.5
  • 10
    • 84878754753 scopus 로고    scopus 로고
    • Energetics and location of phosphoinositide binding in human Kir2.1 channels
    • doi: 10.1074/jbc.M113.452540
    • D'Avanzo, N., Lee, S. J., Cheng, W. W., and Nichols, C. G. (2013). Energetics and location of phosphoinositide binding in human Kir2.1 channels. J. Biol. Chem. 288, 16726-16737. doi: 10.1074/jbc.M113.452540.
    • (2013) J. Biol. Chem. , vol.288 , pp. 16726-16737
    • D'Avanzo, N.1    Lee, S.J.2    Cheng, W.W.3    Nichols, C.G.4
  • 11
    • 34547770295 scopus 로고    scopus 로고
    • Impaired interaction between the slide helix and the C-terminus of Kir2.1: a novel mechanism of Andersen syndrome
    • doi: 10.1016/j.cardiores.2007.05.010
    • Decher, N., Renigunta, V., Zuzarte, M., Soom, M., Heinemann, S. H., Timothy, K. W., et al. (2007). Impaired interaction between the slide helix and the C-terminus of Kir2.1: a novel mechanism of Andersen syndrome. Cardiovasc. Res. 75, 748-757. doi: 10.1016/j.cardiores.2007.05.010.
    • (2007) Cardiovasc. Res. , vol.75 , pp. 748-757
    • Decher, N.1    Renigunta, V.2    Zuzarte, M.3    Soom, M.4    Heinemann, S.H.5    Timothy, K.W.6
  • 12
    • 0037777713 scopus 로고    scopus 로고
    • PIP2 binding residues of Kir2.1 are common targets of mutations causing Andersen syndrome
    • doi: 10.1212/01.WNL.0000072261.14060.47
    • Donaldson, M. R., Jensen, J. L., Tristani-Firouzi, M., Tawil, R., Bendahhou, S., Suarez, W. A., et al. (2003). PIP2 binding residues of Kir2.1 are common targets of mutations causing Andersen syndrome. Neurology 60, 1811-1816. doi: 10.1212/01.WNL.0000072261.14060.47.
    • (2003) Neurology , vol.60 , pp. 1811-1816
    • Donaldson, M.R.1    Jensen, J.L.2    Tristani-Firouzi, M.3    Tawil, R.4    Bendahhou, S.5    Suarez, W.A.6
  • 13
    • 27744586089 scopus 로고    scopus 로고
    • Direct modulation of Kir channel gating by membrane phosphatidylinositol 4,5-bisphosphate
    • doi: 10.1074/jbc.C500355200
    • Enkvetchakul, D., Jeliazkova, I., and Nichols, C. G. (2005). Direct modulation of Kir channel gating by membrane phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 280, 35785-35788. doi: 10.1074/jbc.C500355200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35785-35788
    • Enkvetchakul, D.1    Jeliazkova, I.2    Nichols, C.G.3
  • 14
    • 0034027490 scopus 로고    scopus 로고
    • The kinetic and physical basis of K(ATP) channel gating: toward a unified molecular understanding
    • doi: 10.1016/S0006-3495(00)76779-8
    • Enkvetchakul, D., Loussouarn, G., Makhina, E., Shyng, S. L., and Nichols, C. G. (2000). The kinetic and physical basis of K(ATP) channel gating: toward a unified molecular understanding. Biophys. J. 78, 2334-2348. doi: 10.1016/S0006-3495(00)76779-8.
    • (2000) Biophys. J. , vol.78 , pp. 2334-2348
    • Enkvetchakul, D.1    Loussouarn, G.2    Makhina, E.3    Shyng, S.L.4    Nichols, C.G.5
  • 16
    • 0031055885 scopus 로고    scopus 로고
    • Anionic phospholipids activate ATP-sensitive potassium channels
    • doi: 10.1074/jbc.272.9.5388
    • Fan, Z., and Makielski, J. C. (1997). Anionic phospholipids activate ATP-sensitive potassium channels. J. Biol. Chem. 272, 5388-9535. doi: 10.1074/jbc.272.9.5388.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5388-9535
    • Fan, Z.1    Makielski, J.C.2
  • 17
    • 0024552339 scopus 로고
    • Low-conductance K channels in apical membrane of rat cortical collecting tubule
    • Frindt, G., and Palmer, L. G. (1989). Low-conductance K channels in apical membrane of rat cortical collecting tubule. Am. J. Physiol. 256, F143-F151.
    • (1989) Am. J. Physiol. , vol.256
    • Frindt, G.1    Palmer, L.G.2
  • 18
    • 0022034475 scopus 로고
    • + current in voltage-clamped CA3 pyramidal cells in hippocampal cultures
    • doi: 10.1073/pnas.82.5.1558
    • + current in voltage-clamped CA3 pyramidal cells in hippocampal cultures. Proc. Natl. Acad. Sci. U.S.A. 82, 1558-1562. doi: 10.1073/pnas.82.5.1558.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 1558-1562
    • Gahwiler, B.H.1    Brown, D.A.2
  • 19
    • 0023147731 scopus 로고
    • Abnormal myocardial lipid composition in an infant with type II glutaric aciduria
    • Galloway, J. H., Cartwright, I. J., and Bennett, M. J. (1987). Abnormal myocardial lipid composition in an infant with type II glutaric aciduria. J. Lipid Res. 28, 279-284.
    • (1987) J. Lipid Res. , vol.28 , pp. 279-284
    • Galloway, J.H.1    Cartwright, I.J.2    Bennett, M.J.3
  • 20
    • 33947709389 scopus 로고    scopus 로고
    • Molecular dynamics simulations of inwardly rectifying (Kir) potassium channels: a comparative study
    • doi: 10.1021/bi062210f
    • Haider, S., Khalid, S., Tucker, S. J., Ashcroft, F. M., and Sansom, M. S. (2007a). Molecular dynamics simulations of inwardly rectifying (Kir) potassium channels: a comparative study. Biochemistry 46, 3643-3652. doi: 10.1021/bi062210f.
    • (2007) Biochemistry , vol.46 , pp. 3643-3652
    • Haider, S.1    Khalid, S.2    Tucker, S.J.3    Ashcroft, F.M.4    Sansom, M.S.5
  • 21
    • 34548097260 scopus 로고    scopus 로고
    • Identification of the PIP2-binding site on Kir6.2 by molecular modelling and functional analysis
    • doi: 10.1038/sj.emboj.7601809
    • Haider, S., Tarasov, A. I., Craig, T. J., Sansom, M. S., and Ashcroft, F. M. (2007b). Identification of the PIP2-binding site on Kir6.2 by molecular modelling and functional analysis. EMBO J. 26, 3749-3759. doi: 10.1038/sj.emboj.7601809.
    • (2007) EMBO J. , vol.26 , pp. 3749-3759
    • Haider, S.1    Tarasov, A.I.2    Craig, T.J.3    Sansom, M.S.4    Ashcroft, F.M.5
  • 22
    • 8444238620 scopus 로고    scopus 로고
    • Phospholipid composition of myocardium in children with normoxemic and hypoxemic congenital heart diseases
    • Hamplova, B., Pelouch, V., Novakova, O., Skovranek, J., Hucin, B., and Novak, F. (2004). Phospholipid composition of myocardium in children with normoxemic and hypoxemic congenital heart diseases. Physiol. Res. 53, 557-560.
    • (2004) Physiol. Res. , vol.53 , pp. 557-560
    • Hamplova, B.1    Pelouch, V.2    Novakova, O.3    Skovranek, J.4    Hucin, B.5    Novak, F.6
  • 23
    • 80053131218 scopus 로고    scopus 로고
    • Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2
    • doi: 10.1038/nature10370
    • Hansen, S. B., Tao, X., and MacKinnon, R. (2011). Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2. Nature 477, 495-498. doi: 10.1038/nature10370.
    • (2011) Nature , vol.477 , pp. 495-498
    • Hansen, S.B.1    Tao, X.2    MacKinnon, R.3
  • 24
    • 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
  • 25
    • 0027537268 scopus 로고
    • Cloning and expression of an inwardly rectifying ATP-regulated potassium channel
    • doi: 10.1038/362031a0
    • Ho, K., Nichols, C. G., Lederer, W. J., Lytton, J., Vassilev, P. M., Kanazirska, M. V., et al. (1993). Cloning and expression of an inwardly rectifying ATP-regulated potassium channel. Nature 362, 31-38. doi: 10.1038/362031a0.
    • (1993) Nature , vol.362 , pp. 31-38
    • Ho, K.1    Nichols, C.G.2    Lederer, W.J.3    Lytton, J.4    Vassilev, P.M.5    Kanazirska, M.V.6
  • 26
    • 0032546013 scopus 로고    scopus 로고
    • Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gbetagamma
    • doi: 10.1038/35882
    • Huang, C. L., Feng, S., and Hilgemann, D. W. (1998). Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gbetagamma. Nature 391, 803-806. doi: 10.1038/35882.
    • (1998) Nature , vol.391 , pp. 803-806
    • Huang, C.L.1    Feng, S.2    Hilgemann, D.W.3
  • 27
    • 0028933233 scopus 로고
    • Cloning and functional characterization of a novel ATP-sensitive potassium channel ubiquitously expressed in rat tissues, including pancreatic islets, pituitary, skeletal muscle, and heart
    • doi: 10.1074/jbc.270.11.5691
    • Inagaki, N., Tsuura, Y., Namba, N., Masuda, K., Gonoi, T., Horie, M., et al. (1995). Cloning and functional characterization of a novel ATP-sensitive potassium channel ubiquitously expressed in rat tissues, including pancreatic islets, pituitary, skeletal muscle, and heart. J. Biol. Chem. 270, 5691-5694. doi: 10.1074/jbc.270.11.5691.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5691-5694
    • Inagaki, N.1    Tsuura, Y.2    Namba, N.3    Masuda, K.4    Gonoi, T.5    Horie, M.6
  • 28
    • 78649641632 scopus 로고    scopus 로고
    • A structural determinant for the control of PIP2 sensitivity in G protein-gated inward rectifier K+ channels
    • doi: 10.1074/jbc.M110.161703
    • Inanobe, A., Nakagawa, A., Matsuura, T., and Kurachi, Y. (2010). A structural determinant for the control of PIP2 sensitivity in G protein-gated inward rectifier K+ channels. J. Biol. Chem. 285, 38517-38523. doi: 10.1074/jbc.M110.161703.
    • (2010) J. Biol. Chem. , vol.285 , pp. 38517-38523
    • Inanobe, A.1    Nakagawa, A.2    Matsuura, T.3    Kurachi, Y.4
  • 29
    • 55749104728 scopus 로고    scopus 로고
    • Stoichiometry of Kir channels with phosphatidylinositol bisphosphate
    • doi: 10.4161/chan.2.1.5942
    • Jin, T., Sui, J. L., Rosenhouse-Dantsker, A., Chan, K. W., Jan, L. Y., and Logothetis, D. E. (2008). Stoichiometry of Kir channels with phosphatidylinositol bisphosphate. Channels (Austin) 2, 19-33. doi: 10.4161/chan.2.1.5942.
    • (2008) Channels (Austin) , vol.2 , pp. 19-33
    • Jin, T.1    Sui, J.L.2    Rosenhouse-Dantsker, A.3    Chan, K.W.4    Jan, L.Y.5    Logothetis, D.E.6
  • 30
    • 0027403280 scopus 로고
    • Primary structure and functional expression of a mouse inward rectifier potassium channel
    • doi: 10.1038/362127a0
    • Kubo, Y., Baldwin, T. J., Jan, Y. N., and Jan, L. Y. (1993). Primary structure and functional expression of a mouse inward rectifier potassium channel. Nature 362, 127-133. doi: 10.1038/362127a0.
    • (1993) Nature , vol.362 , pp. 127-133
    • Kubo, Y.1    Baldwin, T.J.2    Jan, Y.N.3    Jan, L.Y.4
  • 31
    • 12444274301 scopus 로고    scopus 로고
    • Crystal structure of the potassium channel KirBac1.1 in the closed state
    • doi: 10.1126/science.1085028
    • Kuo, A., Gulbis, J. M., Antcliff, J. F., Rahman, T., Lowe, E. D., Zimmer, J., et al. (2003). Crystal structure of the potassium channel KirBac1.1 in the closed state. Science 300, 1922-6. doi: 10.1126/science.1085028.
    • (2003) Science , vol.300 , pp. 1922-6
    • Kuo, A.1    Gulbis, J.M.2    Antcliff, J.F.3    Rahman, T.4    Lowe, E.D.5    Zimmer, J.6
  • 32
    • 78650041774 scopus 로고    scopus 로고
    • Gating of a G protein-sensitive mammalian Kir3.1 prokaryotic Kir channel chimera in planar lipid bilayers
    • doi: 10.1074/jbc.M110.151373
    • Leal-Pinto, E., Gomez-Llorente, Y., Sundaram, S., Tang, Q. Y., Ivanova-Nikolova, T., Mahajan, R., et al. (2010). Gating of a G protein-sensitive mammalian Kir3.1 prokaryotic Kir channel chimera in planar lipid bilayers. J. Biol. Chem. 285, 39790-39800. doi: 10.1074/jbc.M110.151373.
    • (2010) J. Biol. Chem. , vol.285 , pp. 39790-39800
    • Leal-Pinto, E.1    Gomez-Llorente, Y.2    Sundaram, S.3    Tang, Q.Y.4    Ivanova-Nikolova, T.5    Mahajan, R.6
  • 33
    • 84893551735 scopus 로고    scopus 로고
    • Secondary anionic phospholipid binding site and gating mechanism in Kir2.1 inward rectifier channels
    • doi: 10.1038/ncomms3786
    • Lee, S. J., Wang, S., Borschel, W., Heyman, S., Gyore, J., and Nichols, C. G. (2013). Secondary anionic phospholipid binding site and gating mechanism in Kir2.1 inward rectifier channels. Nat. Commun. 4, 2786. doi: 10.1038/ncomms3786.
    • (2013) Nat. Commun. , vol.4 , pp. 2786
    • Lee, S.J.1    Wang, S.2    Borschel, W.3    Heyman, S.4    Gyore, J.5    Nichols, C.G.6
  • 34
    • 0038281249 scopus 로고    scopus 로고
    • Phosphoinositide recognition domains
    • doi: 10.1034/j.1600-0854.2004.00071.x
    • Lemmon, M. A. (2003). Phosphoinositide recognition domains. Traffic 4, 201-213. doi: 10.1034/j.1600-0854.2004.00071.x.
    • (2003) Traffic , vol.4 , pp. 201-213
    • Lemmon, M.A.1
  • 35
    • 0034616349 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate and intracellular pH regulate the ROMK1 potassium channel via separate but interrelated mechanisms
    • doi: 10.1074/jbc.275.14.10182
    • Leung, Y. M., Zeng, W. Z., Liou, H. H., Solaro, C. R., and Huang, C. L. (2000). Phosphatidylinositol 4,5-bisphosphate and intracellular pH regulate the ROMK1 potassium channel via separate but interrelated mechanisms. J. Biol. Chem. 275, 10182-10189. doi: 10.1074/jbc.275.14.10182.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10182-10189
    • Leung, Y.M.1    Zeng, W.Z.2    Liou, H.H.3    Solaro, C.R.4    Huang, C.L.5
  • 36
    • 0033545972 scopus 로고    scopus 로고
    • Regulation of ROMK1 channel by protein kinase A via a phosphatidylinositol 4,5-bisphosphate-dependent mechanism
    • doi: 10.1073/pnas.96.10.5820
    • Liou, H. H., Zhou, S. S., and Huang, C. L. (1999). Regulation of ROMK1 channel by protein kinase A via a phosphatidylinositol 4,5-bisphosphate-dependent mechanism. Proc. Natl. Acad. Sci. U.S.A. 96, 5820-5825. doi: 10.1073/pnas.96.10.5820.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 5820-5825
    • Liou, H.H.1    Zhou, S.S.2    Huang, C.L.3
  • 37
    • 0037071897 scopus 로고    scopus 로고
    • Alterations in conserved Kir channel-PIP2 interactions underlie channelopathies
    • doi: 10.1016/S0896-6273(02)00725-0
    • Lopes, C. M., Zhang, H., Rohacs, T., Jin, T., Yang, J., and Logothetis, D. E. (2002). Alterations in conserved Kir channel-PIP2 interactions underlie channelopathies. Neuron 34, 933-944. doi: 10.1016/S0896-6273(02)00725-0.
    • (2002) Neuron , vol.34 , pp. 933-944
    • Lopes, C.M.1    Zhang, H.2    Rohacs, T.3    Jin, T.4    Yang, J.5    Logothetis, D.E.6
  • 38
    • 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
  • 39
    • 0023214019 scopus 로고
    • Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cerevisiae
    • Nikawa, J., Kodaki, T., and Yamashita, S. (1987). Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cerevisiae. J. Biol. Chem. 262, 4876-4881.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4876-4881
    • Nikawa, J.1    Kodaki, T.2    Yamashita, S.3
  • 40
    • 0019980518 scopus 로고
    • Yeast mutant defective in synthesis of phosphatidylinositol. Isolation and characterization of a CDPdiacylglycerol-inositol 3-phosphatidyltransferase Km mutant
    • doi: 10.1111/j.1432-1033.1982.tb06703.x
    • Nikawa, J., and Yamashita, S. (1982). Yeast mutant defective in synthesis of phosphatidylinositol. Isolation and characterization of a CDPdiacylglycerol-inositol 3-phosphatidyltransferase Km mutant. Eur. J. Biochem. 125, 445-451. doi: 10.1111/j.1432-1033.1982.tb06703.x.
    • (1982) Eur. J. Biochem. , vol.125 , pp. 445-451
    • Nikawa, J.1    Yamashita, S.2
  • 41
    • 0031553023 scopus 로고    scopus 로고
    • Phosphatidylinositol synthase from yeast
    • doi: 10.1016/S0005-2760(97)00103-3
    • Nikawa, J., and Yamashita, S. (1997). Phosphatidylinositol synthase from yeast. Biochim. Biophys. Acta 1348, 173-178. doi: 10.1016/S0005-2760(97)00103-3.
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 173-178
    • Nikawa, J.1    Yamashita, S.2
  • 42
    • 34548386717 scopus 로고    scopus 로고
    • Crystal structure of a Kir3.1-prokaryotic Kir channel chimera
    • doi: 10.1038/sj.emboj.7601828
    • Nishida, M., Cadene, M., Chait, B. T., and MacKinnon, R. (2007). Crystal structure of a Kir3.1-prokaryotic Kir channel chimera. EMBO J. 26, 4005-4015. doi: 10.1038/sj.emboj.7601828.
    • (2007) EMBO J. , vol.26 , pp. 4005-4015
    • Nishida, M.1    Cadene, M.2    Chait, B.T.3    MacKinnon, R.4
  • 43
    • 33746047139 scopus 로고    scopus 로고
    • Andersen's syndrome mutation effects on the structure and assembly of the cytoplasmic domains of Kir2.1
    • doi: 10.1021/bi060653d
    • Pegan, S., Arrabit, C., Slesinger, P. A., and Choe, S. (2006). Andersen's syndrome mutation effects on the structure and assembly of the cytoplasmic domains of Kir2.1. Biochemistry 45, 8599-8606. doi: 10.1021/bi060653d.
    • (2006) Biochemistry , vol.45 , pp. 8599-8606
    • Pegan, S.1    Arrabit, C.2    Slesinger, P.A.3    Choe, S.4
  • 44
    • 14544298750 scopus 로고    scopus 로고
    • Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification
    • doi: 10.1038/nn1411
    • Pegan, S., Arrabit, C., Zhou, W., Kwiatkowski, W., Collins, A., Slesinger, P. A., et al. (2005). Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification. Nat. Neurosci. 8, 279-287. doi: 10.1038/nn1411.
    • (2005) Nat. Neurosci. , vol.8 , pp. 279-287
    • Pegan, S.1    Arrabit, C.2    Zhou, W.3    Kwiatkowski, W.4    Collins, A.5    Slesinger, P.A.6
  • 45
    • 0028911094 scopus 로고
    • Organization and function of sarcolemmal phospholipids in control and ischemic/reperfused cardiomyocytes
    • doi: 10.1016/0022-2828(95)90080-2
    • Post, J. A., Verkleij, A. J., and Langer, G. A. (1995). Organization and function of sarcolemmal phospholipids in control and ischemic/reperfused cardiomyocytes. J. Mol. Cell. Cardiol. 27, 749-760. doi: 10.1016/0022-2828(95)90080-2.
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , pp. 749-760
    • Post, J.A.1    Verkleij, A.J.2    Langer, G.A.3
  • 46
    • 59649091228 scopus 로고    scopus 로고
    • Long-pore electrostatics in inward-rectifier potassium channels
    • doi: 10.1085/jgp.200810068
    • Robertson, J. L., Palmer, L. G., and Roux, B. (2008). Long-pore electrostatics in inward-rectifier potassium channels. J. Gen. Physiol. 132, 613-632. doi: 10.1085/jgp.200810068.
    • (2008) J. Gen. Physiol. , vol.132 , pp. 613-632
    • Robertson, J.L.1    Palmer, L.G.2    Roux, B.3
  • 48
    • 0037457882 scopus 로고    scopus 로고
    • Specificity of activation by phosphoinositides determines lipid regulation of Kir channels
    • doi: 10.1073/pnas.0236364100
    • Rohacs, T., Lopes, C. M., Jin, T., Ramdya, P. P., Molnar, Z., and Logothetis, D. E. (2003). Specificity of activation by phosphoinositides determines lipid regulation of Kir channels. Proc. Natl. Acad. Sci. U.S.A. 100, 745-750. doi: 10.1073/pnas.0236364100.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 745-750
    • Rohacs, T.1    Lopes, C.M.2    Jin, T.3    Ramdya, P.P.4    Molnar, Z.5    Logothetis, D.E.6
  • 49
    • 10044242802 scopus 로고    scopus 로고
    • Cholesterol sensitivity and lipid raft targeting of Kir2.1 channels
    • doi: 10.1529/biophysj.104.043273
    • Romanenko, V. G., Fang, Y., Byfield, F., Travis, A. J., Vandenberg, C. A., Rothblat, G. H., et al. (2004). Cholesterol sensitivity and lipid raft targeting of Kir2.1 channels. Biophys. J. 87, 3850-3861. doi: 10.1529/biophysj.104.043273.
    • (2004) Biophys. J. , vol.87 , pp. 3850-3861
    • Romanenko, V.G.1    Fang, Y.2    Byfield, F.3    Travis, A.J.4    Vandenberg, C.A.5    Rothblat, G.H.6
  • 50
    • 0014236250 scopus 로고
    • Voltage clamp experiments on frog atrial heart muscle fibres with the sucrose gap technique
    • doi: 10.1007/BF00362729
    • Rougier, O., Vassort, G., and Stampfli, R. (1968). Voltage clamp experiments on frog atrial heart muscle fibres with the sucrose gap technique. Pflugers Arch. 301, 91-108. doi: 10.1007/BF00362729.
    • (1968) Pflugers Arch. , vol.301 , pp. 91-108
    • Rougier, O.1    Vassort, G.2    Stampfli, R.3
  • 51
    • 84872535182 scopus 로고    scopus 로고
    • Simulation-based prediction of phosphatidylinositol 4,5-bisphosphate binding to an ion channel
    • doi: 10.1021/bi301350s
    • Schmidt, M. R., Stansfeld, P. J., Tucker, S. J., and Sansom, M. S. (2013). Simulation-based prediction of phosphatidylinositol 4,5-bisphosphate binding to an ion channel. Biochemistry 52, 279-281. doi: 10.1021/bi301350s.
    • (2013) Biochemistry , vol.52 , pp. 279-281
    • Schmidt, M.R.1    Stansfeld, P.J.2    Tucker, S.J.3    Sansom, M.S.4
  • 52
    • 0033756604 scopus 로고    scopus 로고
    • Structural determinants of PIP(2) regulation of inward rectifier K(ATP) channels
    • doi: 10.1085/jgp.116.5.599
    • Shyng, S. L., Cukras, C. A., Harwood, J., and Nichols, C. G. (2000). Structural determinants of PIP(2) regulation of inward rectifier K(ATP) channels. J. Gen. Physiol. 116, 599-608. doi: 10.1085/jgp.116.5.599.
    • (2000) J. Gen. Physiol. , vol.116 , pp. 599-608
    • Shyng, S.L.1    Cukras, C.A.2    Harwood, J.3    Nichols, C.G.4
  • 53
    • 0032491439 scopus 로고    scopus 로고
    • Membrane phospholipid control of nucleotide sensitivity of KATP channels
    • doi: 10.1126/science.282.5391.1138
    • Shyng, S. L., and Nichols, C. G. (1998). Membrane phospholipid control of nucleotide sensitivity of KATP channels. Science 282, 1138-1141. doi: 10.1126/science.282.5391.1138.
    • (1998) Science , vol.282 , pp. 1138-1141
    • Shyng, S.L.1    Nichols, C.G.2
  • 54
    • 0015259575 scopus 로고
    • The phospholipid composition of human placenta, endometrium and amniotic fluid: a comparative study
    • doi: 10.1007/BF02531265
    • Singh, E. J., and Swartwout, J. R. (1972). The phospholipid composition of human placenta, endometrium and amniotic fluid: a comparative study. Lipids 7, 26-29. doi: 10.1007/BF02531265.
    • (1972) Lipids , vol.7 , pp. 26-29
    • Singh, E.J.1    Swartwout, J.R.2
  • 55
    • 0037352568 scopus 로고    scopus 로고
    • Biosynthesis of phosphatidylcholine in bacteria
    • doi: 10.1016/S0163-7827(02)00050-4
    • Sohlenkamp, C., Lopez-Lara, I. M., and Geiger, O. (2003). Biosynthesis of phosphatidylcholine in bacteria. Prog. Lipid Res. 42, 115-162. doi: 10.1016/S0163-7827(02)00050-4.
    • (2003) Prog. Lipid Res. , vol.42 , pp. 115-162
    • Sohlenkamp, C.1    Lopez-Lara, I.M.2    Geiger, O.3
  • 56
    • 0035830482 scopus 로고    scopus 로고
    • Multiple PIP2 binding sites in Kir2.1 inwardly rectifying potassium channels
    • doi: 10.1016/S0014-5793(01)02136-6
    • Soom, M., Schonherr, R., Kubo, Y., Kirsch, C., Klinger, R., and Heinemann, S. H. (2001). Multiple PIP2 binding sites in Kir2.1 inwardly rectifying potassium channels. FEBS Lett. 490, 49-53. doi: 10.1016/S0014-5793(01)02136-6.
    • (2001) FEBS Lett. , vol.490 , pp. 49-53
    • Soom, M.1    Schonherr, R.2    Kubo, Y.3    Kirsch, C.4    Klinger, R.5    Heinemann, S.H.6
  • 57
    • 72749123748 scopus 로고    scopus 로고
    • PIP(2)-binding site in Kir channels: definition by multiscale biomolecular simulations
    • doi: 10.1021/bi9013193
    • Stansfeld, P. J., Hopkinson, R., Ashcroft, F. M., and Sansom, M. S. (2009). PIP(2)-binding site in Kir channels: definition by multiscale biomolecular simulations. Biochemistry 48, 10926-10933. doi: 10.1021/bi9013193.
    • (2009) Biochemistry , vol.48 , pp. 10926-10933
    • Stansfeld, P.J.1    Hopkinson, R.2    Ashcroft, F.M.3    Sansom, M.S.4
  • 58
    • 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
  • 59
    • 0025262334 scopus 로고
    • Inward rectification in neonatal rat spinal motoneurones
    • Takahashi, T. (1990). Inward rectification in neonatal rat spinal motoneurones. J. Physiol. 423, 47-62.
    • (1990) J. Physiol. , vol.423 , pp. 47-62
    • Takahashi, T.1
  • 60
    • 72949091450 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic strong inward-rectifier K+ channel Kir2.2 at 3.1 A resolution
    • doi: 10.1126/science.1180310
    • Tao, X., Avalos, J. L., Chen, J., and MacKinnon, R. (2009). Crystal structure of the eukaryotic strong inward-rectifier K+ channel Kir2.2 at 3.1 A resolution. Science 326, 1668-1674. doi: 10.1126/science.1180310.
    • (2009) Science , vol.326 , pp. 1668-1674
    • Tao, X.1    Avalos, J.L.2    Chen, J.3    MacKinnon, R.4
  • 61
    • 15444365811 scopus 로고    scopus 로고
    • MARCKS is a natively unfolded protein with an inaccessible actin-binding site: evidence for long-range intramolecular interactions
    • doi: 10.1074/jbc.M414614200
    • Tapp, H., Al-Naggar, I. M., Yarmola, E. G., Harrison, A., Shaw, G., Edison, A. S., et al. (2005). MARCKS is a natively unfolded protein with an inaccessible actin-binding site: evidence for long-range intramolecular interactions. J. Biol. Chem. 280, 9946-9956. doi: 10.1074/jbc.M414614200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9946-9956
    • Tapp, H.1    Al-Naggar, I.M.2    Yarmola, E.G.3    Harrison, A.4    Shaw, G.5    Edison, A.S.6
  • 62
    • 0037072757 scopus 로고    scopus 로고
    • Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions
    • doi: 10.1074/jbc.M203954200
    • Wang, J., Gambhir, A., Hangyas-Mihalyne, G., Murray, D., Golebiewska, U., and McLaughlin, S. (2002a). Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions. J. Biol. Chem. 277, 34401-34412. doi: 10.1074/jbc.M203954200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34401-34412
    • Wang, J.1    Gambhir, A.2    Hangyas-Mihalyne, G.3    Murray, D.4    Golebiewska, U.5    McLaughlin, S.6
  • 64
    • 84863032002 scopus 로고    scopus 로고
    • Structural rearrangements underlying ligand-gating in Kir channels
    • doi: 10.1038/ncomms1625
    • Wang, S., Lee, S. J., Heyman, S., Enkvetchakul, D., and Nichols, C. G. (2012). Structural rearrangements underlying ligand-gating in Kir channels. Nat. Commun. 3, 617. doi: 10.1038/ncomms1625.
    • (2012) Nat. Commun. , vol.3 , pp. 617
    • Wang, S.1    Lee, S.J.2    Heyman, S.3    Enkvetchakul, D.4    Nichols, C.G.5
  • 65
  • 66
    • 0013803871 scopus 로고
    • Lipid composition of heart muscle homogenate
    • Wheeldon, L. W., Schumert, Z., and Turner, D. A. (1965). Lipid composition of heart muscle homogenate. J. Lipid Res. 6, 481-489.
    • (1965) J. Lipid Res. , vol.6 , pp. 481-489
    • Wheeldon, L.W.1    Schumert, Z.2    Turner, D.A.3
  • 67
    • 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
  • 68
    • 84878996278 scopus 로고    scopus 로고
    • X-ray structure of the mammalian GIRK2-betagamma G-protein complex
    • doi: 10.1038/nature12241
    • Whorton, M. R., and MacKinnon, R. (2013). X-ray structure of the mammalian GIRK2-betagamma G-protein complex. Nature 498, 190-197. doi: 10.1038/nature12241.
    • (2013) Nature , vol.498 , pp. 190-197
    • Whorton, M.R.1    MacKinnon, R.2
  • 69
    • 45549098736 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5-bisphosphate (PIP2) regulation of strong inward rectifier Kir2.1 channels: multilevel positive cooperativity
    • doi: 10.1113/jphysiol.2007.147868
    • Xie, L. H., John, S. A., Ribalet, B., and Weiss, J. N. (2008). Phosphatidylinositol-4,5-bisphosphate (PIP2) regulation of strong inward rectifier Kir2.1 channels: multilevel positive cooperativity. J. Physiol. 586, 1833-1848. doi: 10.1113/jphysiol.2007.147868.
    • (2008) J. Physiol. , vol.586 , pp. 1833-1848
    • Xie, L.H.1    John, S.A.2    Ribalet, B.3    Weiss, J.N.4
  • 70
    • 0036084087 scopus 로고    scopus 로고
    • Structural determinants and specificities for ROMK1-phosphoinositide interaction
    • doi: 10.1152/ajprenal.00300.2001
    • Zeng, W. Z., Liou, H. H., Krishna, U. M., Falck, J. R., and Huang, C. L. (2002). Structural determinants and specificities for ROMK1-phosphoinositide interaction. Am. J. Physiol. Renal Physiol. 282, F826-F834. doi: 10.1152/ajprenal.00300.2001.
    • (2002) Am. J. Physiol. Renal Physiol. , vol.282
    • Zeng, W.Z.1    Liou, H.H.2    Krishna, U.M.3    Falck, J.R.4    Huang, C.L.5


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