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Volumn 1808, Issue 10, 2011, Pages 2527-2533

Cholesterol regulates prokaryotic Kir channel by direct binding to channel protein

Author keywords

Cholesterol; Ion channel; KirBac1.1; Lipid bilayer; Lipid protein interaction

Indexed keywords

ANDROSTENEDIOL; CHOLESTEROL; INWARDLY RECTIFYING POTASSIUM CHANNEL; KIRBAC1.1 CHANNEL PROTEIN; TRIFLUOPERAZINE; UNCLASSIFIED DRUG;

EID: 79961116868     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.07.006     Document Type: Article
Times cited : (43)

References (39)
  • 1
    • 32444447144 scopus 로고    scopus 로고
    • Involvement of lipid rafts and caveolae in cardiac ion channel function
    • DOI 10.1016/j.cardiores.2005.11.013, PII S0008636305005250
    • A. Maguy, T.E. Hebert, and S. Nattel Involvement of lipid rafts and caveolae in cardiac ion channel function Cardiovasc. Res. 69 2006 798 807 (Pubitemid 43227978)
    • (2006) Cardiovascular Research , vol.69 , Issue.4 , pp. 798-807
    • Maguy, A.1    Hebert, T.E.2    Nattel, S.3
  • 3
    • 0034697041 scopus 로고    scopus 로고
    • Assembly of Trp1 in a signaling complex associated with caveolin- scaffolding lipid raft domains
    • DOI 10.1074/jbc.275.16.11934
    • T.P. Lockwich, X. Liu, B.B. Singh, J. Jadlowiec, S. Weiland, and I.S. Ambudkar Assembly of Trp1 in a signaling complex associated with caveolin-scaffolding lipid raft domains J. Biol. Chem. 275 2000 11934 11942 (Pubitemid 30237764)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.16 , pp. 11934-11942
    • Lockwich, T.P.1    Liu, X.2    Singh, B.B.3    Jadlowiec, J.4    Weiland, S.5    Ambudkar, I.S.6
  • 5
    • 2342466825 scopus 로고    scopus 로고
    • Plasma membrane localization of TRPC channels: Role of caveolar lipid rafts
    • discussion 70-64, 98-102, 263-106
    • I.S. Ambudkar, S.C. Brazer, X. Liu, T. Lockwich, and B. Singh Plasma membrane localization of TRPC channels: role of caveolar lipid rafts Novartis Found. Symp. 258 2004 63 70 discussion 70-64, 98-102, 263-106
    • (2004) Novartis Found. Symp. , vol.258 , pp. 63-70
    • Ambudkar, I.S.1    Brazer, S.C.2    Liu, X.3    Lockwich, T.4    Singh, B.5
  • 6
    • 0346655136 scopus 로고    scopus 로고
    • V channels to lipid rafts
    • DOI 10.1016/j.tips.2003.11.007
    • J.R. Martens, K. O'Connell, and M. Tamkun Targeting of ion channels to membrane microdomains: localization of KV channels to lipid rafts Trends Pharmacol. Sci. 25 2004 16 21 (Pubitemid 38076952)
    • (2004) Trends in Pharmacological Sciences , vol.25 , Issue.1 , pp. 16-21
    • Martens, J.R.1    O'Connell, K.2    Tamkun, M.3
  • 7
    • 47749119542 scopus 로고    scopus 로고
    • Lipid rafts determine clustering of STIM1 in endoplasmic reticulum-plasma membrane junctions and regulation of store-operated Ca2+ entry (SOCE)
    • B. Pani, H.L. Ong, X. Liu, K. Rauser, I.S. Ambudkar, and B.B. Singh Lipid rafts determine clustering of STIM1 in endoplasmic reticulum-plasma membrane junctions and regulation of store-operated Ca2+ entry (SOCE) J. Biol. Chem. 283 2008 17333 17340
    • (2008) J. Biol. Chem. , vol.283 , pp. 17333-17340
    • Pani, B.1    Ong, H.L.2    Liu, X.3    Rauser, K.4    Ambudkar, I.S.5    Singh, B.B.6
  • 8
    • 77956277183 scopus 로고    scopus 로고
    • Lipid microdomains and the regulation of ion channel function
    • C. Dart Lipid microdomains and the regulation of ion channel function J. Physiol. 588 2010 3169 3178
    • (2010) J. Physiol. , vol.588 , pp. 3169-3178
    • Dart, C.1
  • 9
    • 9644294471 scopus 로고    scopus 로고
    • Structural basis for lipid modulation of nicotinic acetylcholine receptor function
    • DOI 10.1016/j.brainresrev.2004.06.008, PII S0165017304000815, Chemical and Electrical Synapses
    • F.J. Barrantes Structural basis for lipid modulation of nicotinic acetylcholine receptor function Brain Res. Brain Res. Rev. 47 2004 71 95 (Pubitemid 39574312)
    • (2004) Brain Research Reviews , vol.47 , Issue.1-3 , pp. 71-95
    • Barrantes, F.J.1
  • 12
    • 0344861820 scopus 로고    scopus 로고
    • + channels
    • D. Bichet, F.A. Haass, and L.Y. Jan Merging functional studies with structures of inward-rectifier K(+) channels Nat. Rev. Neurosci. 4 2003 957 967 (Pubitemid 37486672)
    • (2003) Nature Reviews Neuroscience , vol.4 , Issue.12 , pp. 957-967
    • Bichet, D.1    Haass, F.A.2    Jan, L.Y.3
  • 14
    • 74949143771 scopus 로고    scopus 로고
    • Inwardly rectifying potassium channels: Their structure, function, and physiological roles
    • H. Hibino, A. Inanobe, K. Furutani, S. Murakami, I. Findlay, and Y. Kurachi Inwardly rectifying potassium channels: their structure, function, and physiological roles Physiol. Rev. 90 2010 291 366
    • (2010) Physiol. Rev. , vol.90 , pp. 291-366
    • Hibino, H.1    Inanobe, A.2    Furutani, K.3    Murakami, S.4    Findlay, I.5    Kurachi, Y.6
  • 15
    • 70149094646 scopus 로고    scopus 로고
    • Cholesterol and Kir channels
    • I. Levitan Cholesterol and Kir channels IUBMB Life 61 2009 781 790
    • (2009) IUBMB Life , vol.61 , pp. 781-790
    • Levitan, I.1
  • 16
    • 0036924104 scopus 로고    scopus 로고
    • + current by optical isomers of cholesterol
    • V.G. Romanenko, G.H. Rothblat, and I. Levitan Modulation of endothelial inward-rectifier K+ current by optical isomers of cholesterol Biophys. J. 83 2002 3211 3222 (Pubitemid 36041940)
    • (2002) Biophysical Journal , vol.83 , Issue.6 , pp. 3211-3222
    • Romanenko, V.G.1    Rothblat, G.H.2    Levitan, I.3
  • 19
    • 34547220490 scopus 로고    scopus 로고
    • Relationship between Kir2.1/Kir2.3 activity and their distributions between cholesterol-rich and cholesterol-poor membrane domains
    • S. Tikku, Y. Epshtein, H. Collins, A.J. Travis, G.H. Rothblat, and I. Levitan Relationship between Kir2.1/Kir2.3 activity and their distributions between cholesterol-rich and cholesterol-poor membrane domains Am. J. Physiol. Cell Physiol. 293 2007 C440 C450
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293
    • Tikku, S.1    Epshtein, Y.2    Collins, H.3    Travis, A.J.4    Rothblat, G.H.5    Levitan, I.6
  • 24
    • 78751684522 scopus 로고    scopus 로고
    • Cholesterol sensitivity of KIR2.1 is controlled by a belt of residues around the cytosolic pore
    • A. Rosenhouse-Dantsker, D.E. Logothetis, and I. Levitan Cholesterol sensitivity of KIR2.1 is controlled by a belt of residues around the cytosolic pore Biophys. J. 100 2011 381 389
    • (2011) Biophys. J. , vol.100 , pp. 381-389
    • Rosenhouse-Dantsker, A.1    Logothetis, D.E.2    Levitan, I.3
  • 26
    • 26444584556 scopus 로고    scopus 로고
    • Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography
    • DOI 10.1016/j.str.2005.07.011, PII S0969212605002704
    • A. Kuo, C. Domene, L.N. Johnson, D.A. Doyle, and C. Venien-Bryan Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography Structure 13 2005 1463 1472 (Pubitemid 41427586)
    • (2005) Structure , vol.13 , Issue.10 , pp. 1463-1472
    • Kuo, A.1    Domene, C.2    Johnson, L.N.3    Doyle, D.A.4    Venien-Bryan, C.5
  • 28
    • 27744586089 scopus 로고    scopus 로고
    • Direct modulation of Kir channel gating by membrane phosphatidylinositol 4,5-bisphosphate
    • DOI 10.1074/jbc.C500355200
    • D. Enkvetchakul, I. Jeliazkova, and C.G. Nichols Direct modulation of Kir channel gating by membrane phosphatidylinositol 4,5-bisphosphate J. Biol. Chem. 280 2005 35785 35788 (Pubitemid 41633843)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.43 , pp. 35785-35788
    • Enkvetchakul, D.1    Jeliazkova, I.2    Nichols, C.G.3
  • 30
    • 3242668095 scopus 로고    scopus 로고
    • Direct binding of cholesterol to the purified membrane region of SCAP: Mechanism for a sterol-sensing domain
    • DOI 10.1016/j.molcel.2004.06.019, PII S1097276504003521
    • A. Radhakrishnan, L.P. Sun, H.J. Kwon, M.S. Brown, and J.L. Goldstein Direct binding of cholesterol to the purified membrane region of SCAP: mechanism for a sterol-sensing domain Mol. Cell 15 2004 259 268 (Pubitemid 38950972)
    • (2004) Molecular Cell , vol.15 , Issue.2 , pp. 259-268
    • Radhakrishnan, A.1    Sun, L.-P.2    Kwon, H.J.3    Brown, M.S.4    Goldstein, J.L.5
  • 31
    • 38149069055 scopus 로고    scopus 로고
    • Purified NPC1 protein. I. Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein
    • R.E. Infante, L. Abi-Mosleh, A. Radhakrishnan, J.D. Dale, M.S. Brown, and J.L. Goldstein Purified NPC1 protein. I. Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein J. Biol. Chem. 283 2008 1052 1063
    • (2008) J. Biol. Chem. , vol.283 , pp. 1052-1063
    • Infante, R.E.1    Abi-Mosleh, L.2    Radhakrishnan, A.3    Dale, J.D.4    Brown, M.S.5    Goldstein, J.L.6
  • 32
    • 55749083068 scopus 로고    scopus 로고
    • NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes
    • R.E. Infante, M.L. Wang, A. Radhakrishnan, H.J. Kwon, M.S. Brown, and J.L. Goldstein NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes Proc. Natl. Acad. Sci. U.S.A. 105 2008 15287 15292
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 15287-15292
    • Infante, R.E.1    Wang, M.L.2    Radhakrishnan, A.3    Kwon, H.J.4    Brown, M.S.5    Goldstein, J.L.6
  • 33
    • 77952313405 scopus 로고    scopus 로고
    • Cholesterol-protein interaction: Methods and cholesterol reporter molecules
    • G. Gimpl Cholesterol-protein interaction: methods and cholesterol reporter molecules Subcell. Biochem. 51 2010 1 45
    • (2010) Subcell. Biochem. , vol.51 , pp. 1-45
    • Gimpl, G.1
  • 34
    • 79955756236 scopus 로고    scopus 로고
    • Enantioselective protein-sterol interactions mediate regulation of both prokaryotic and eukaryotic inward rectifier k channels by cholesterol
    • N. D'Avanzo, K. Hyrc, D. Enkvetchakul, D.F. Covey, and C.G. Nichols Enantioselective protein-sterol interactions mediate regulation of both prokaryotic and eukaryotic inward rectifier k channels by cholesterol PLoS One 6 2011 e19393
    • (2011) PLoS One , vol.6 , pp. 19393
    • D'Avanzo, N.1    Hyrc, K.2    Enkvetchakul, D.3    Covey, D.F.4    Nichols, C.G.5
  • 35
    • 33846865571 scopus 로고    scopus 로고
    • Trifluoperazine causes a disturbance in glycerophospholipid monolayers containing phosphatidylserine (PS): Effects of pH, acyl unsaturation, and proportion of PS
    • DOI 10.1021/la061628b
    • A. Broniec, A.U. Gjerde, A.B. Olmheim, and H. Holmsen Trifluoperazine causes a disturbance in glycerophospholipid monolayers containing phosphatidylserine (PS): effects of pH, acyl unsaturation, and proportion of PS Langmuir 23 2007 694 699 (Pubitemid 46226581)
    • (2007) Langmuir , vol.23 , Issue.2 , pp. 694-699
    • Broniec, A.1    Gjerde, A.U.2    Olmheim, A.B.3    Holmsen, H.4
  • 36
    • 34548772913 scopus 로고    scopus 로고
    • Phase separation is induced by phenothiazine derivatives in phospholipid/sphingomyelin/cholesterol mixtures containing low levels of cholesterol and sphingomyelin
    • DOI 10.1016/j.bpc.2007.07.001, PII S030146220700169X
    • A.B. Hendrich, K. Michalak, and O. Wesolowska Phase separation is induced by phenothiazine derivatives in phospholipid/sphingomyelin/cholesterol mixtures containing low levels of cholesterol and sphingomyelin Biophys. Chem. 130 2007 32 40 (Pubitemid 47429870)
    • (2007) Biophysical Chemistry , vol.130 , Issue.1-2 , pp. 32-40
    • Hendrich, A.B.1    Michalak, K.2    Wesolowska, O.3
  • 37
    • 79251575362 scopus 로고    scopus 로고
    • Direct visualization of phase separation induced by phenothiazine-type antipsychotic drugs in model lipid membranes
    • O. Wesolowska, K. Michalak, and A.B. Hendrich Direct visualization of phase separation induced by phenothiazine-type antipsychotic drugs in model lipid membranes Mol. Membr. Biol. 28 2011 103 114
    • (2011) Mol. Membr. Biol. , vol.28 , pp. 103-114
    • Wesolowska, O.1    Michalak, K.2    Hendrich, A.B.3
  • 38
    • 0030992795 scopus 로고    scopus 로고
    • Lipid bilayer electrostatic energy, curvature stress, and assembly of gramicidin channels
    • DOI 10.1021/bi9619841
    • J.A. Lundbaek, A.M. Maer, and O.S. Andersen Lipid bilayer electrostatic energy, curvature stress, and assembly of gramicidin channels Biochemistry 36 1997 5695 5701 (Pubitemid 27214920)
    • (1997) Biochemistry , vol.36 , Issue.19 , pp. 5695-5701
    • Lundbaek, J.A.1    Maer, A.M.2    Andersen, O.S.3
  • 39
    • 34548852630 scopus 로고    scopus 로고
    • Control of inward rectifier K channel activity by lipid tethering of cytoplasmic domains
    • DOI 10.1085/jgp.200709764
    • D. Enkvetchakul, I. Jeliazkova, J. Bhattacharyya, and C.G. Nichols Control of inward rectifier K channel activity by lipid tethering of cytoplasmic domains J. Gen. Physiol. 130 2007 329 334 (Pubitemid 47443293)
    • (2007) Journal of General Physiology , vol.130 , Issue.3 , pp. 329-334
    • Enkvetchakul, D.1    Jeliazkova, I.2    Bhattacharyya, J.3    Nichols, C.G.4


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