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Volumn 1, Issue , 2011, Pages

Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; NICOTINIC RECEPTOR;

EID: 84860158205     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep00069     Document Type: Article
Times cited : (189)

References (44)
  • 1
    • 69949159308 scopus 로고    scopus 로고
    • Nicotinic receptors: Allosteric transitions and therapeutic targets in the nervous system
    • Taly, A., Corringer, P. J., Guedin, D., Lestage, P., & Changeux, J. P. Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system. Nat. Rev Drug Discov. 8, 733-750 (2009).
    • (2009) Nat. Rev Drug Discov. , vol.8 , pp. 733-750
    • Taly, A.1    Corringer, P.J.2    Guedin, D.3    Lestage, P.4    Changeux, J.P.5
  • 2
    • 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
    • Barrantes, F. J. Structural basis for lipid modulation of nicotinic acetylcholine receptor function. Brain Res. Brain Res. Rev. 47, 71-95 (2004). (Pubitemid 39574312)
    • (2004) Brain Research Reviews , vol.47 , Issue.1-3 , pp. 71-95
    • Barrantes, F.J.1
  • 3
    • 77952302051 scopus 로고    scopus 로고
    • Cholesterol effects on nicotinic acetylcholine receptor: Cellular aspects
    • Barrantes, F. J. Cholesterol effects on nicotinic acetylcholine receptor: cellular aspects. Subcell. Biochem. 51, 467-487 (2010).
    • (2010) Subcell. Biochem. , vol.51 , pp. 467-487
    • Barrantes, F.J.1
  • 4
    • 0021152857 scopus 로고
    • Functional properties of the acetylcholine receptor incorporated in model lipid membranes. Differential effects of chain length and head group of phospholipids on receptor affinity states and receptor-mediated ion translocation
    • Criado, M., Eibl, H., & Barrantes, F. J. Functional properties of the acetylcholine receptor incorporated in model lipid membranes. Differential effects of chain length and head group of phospholipids on receptor affinity states and receptormediated ion translocation. J Biol. Chem. 259, 9188-9198 (1984). (Pubitemid 14098904)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.14 , pp. 9188-9198
    • Criado, M.1    Eibl, H.2    Barrantes, F.J.3
  • 5
    • 33847068682 scopus 로고    scopus 로고
    • Cholesterol depletion activates rapid internalization of submicron-sized acetylcholine receptor domains at the cell membrane
    • Borroni, V. et al. Cholesterol depletion activates rapid internalization of submicron-sized acetylcholine receptor domains at the cell membrane. Mol. Membr. Biol. 24, 1-15 (2007).
    • (2007) Mol. Membr. Biol. , vol.24 , pp. 1-15
    • Borroni, V.1
  • 6
    • 0027273911 scopus 로고
    • Labeling of the nicotinic acetylcholine receptor by a photoactivatable steroid probe: Effects of cholesterol and cholinergic ligands
    • DOI 10.1016/0005-2736(93)90034-W
    • Fernandez, A. M., Fernandez-Ballester, G., Ferragut, J. A., & Gonzalez-Ros, J. M. Labeling of the nicotinic acetylcholine receptor by a photoactivatable steroid probe: effects of cholesterol and cholinergic ligands. Biochim. Biophys. Acta 1149, 135-144 (1993). (Pubitemid 23186313)
    • (1993) Biochimica et Biophysica Acta - Biomembranes , vol.1149 , Issue.1 , pp. 135-144
    • Fernandez, A.M.1    Fernandez-Ballester, G.2    Ferragut, J.A.3    Gonzales-Ros, J.M.4
  • 7
    • 0023124272 scopus 로고
    • Identification of subunits of acetylcholine receptor that interact with a cholesterol photoaffinity probe
    • DOI 10.1021/bi00379a003
    • Middlemas, D. S. & Raftery, M. A. Identification of subunits of acetylcholine receptor that interact with a cholesterol photoaffinity probe. Biochemistry 26, 1219-1223 (1987). (Pubitemid 17045848)
    • (1987) Biochemistry , vol.26 , Issue.5 , pp. 1219-1223
    • Middlemas, D.S.1    Raftery, M.A.2
  • 8
    • 0033046008 scopus 로고    scopus 로고
    • The steroid promegestone is a noncompetitive antagonist of the Torpedo nicotinic acetylcholine receptor that interacts with the lipid-protein interface
    • Blanton, M. P., Xie, Y., Dangott, L. J., & Cohen, J. B. The steroid promegestone is a noncompetitive antagonist of the Torpedo nicotinic acetylcholine receptor that interacts with the lipid-protein interface. Mol. Pharmacol. 55, 269-278 (1999). (Pubitemid 29076023)
    • (1999) Molecular Pharmacology , vol.55 , Issue.2 , pp. 269-278
    • Blanton, M.P.1    Xie, Y.2    Dangott, L.J.3    Cohen, J.B.4
  • 9
    • 0032508916 scopus 로고    scopus 로고
    • 125I]azido-cholesterol
    • DOI 10.1016/S0005-2736(98)00153-9, PII S0005273698001539
    • Corbin, J., Wang, H. H., & Blanton, M. P. Identifying the cholesterol binding domain in the nicotinic acetylcholine receptor with [125I]azido-cholesterol. Biochim. Biophys. Acta 1414, 65-74 (1998). (Pubitemid 28511040)
    • (1998) Biochimica et Biophysica Acta - Biomembranes , vol.1414 , Issue.1-2 , pp. 65-74
    • Corbin, J.1    Wang, H.H.2    Blanton, M.P.3
  • 10
    • 31044432386 scopus 로고    scopus 로고
    • 3H]azichoiesterol
    • DOI 10.1021/bi051978h
    • Hamouda, A. K., Chiara, D. C., Sauls, D., Cohen, J. B., & Blanton, M. P. Cholesterol interacts with transmembrane alpha-helices M1, M3, and M4 of the Torpedo nicotinic acetylcholine receptor: photolabeling studies using [3H]Azicholesterol. Biochemistry 45, 976-986 (2006). (Pubitemid 43122261)
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 976-986
    • Hamouda, A.K.1    Chiara, D.C.2    Sauls, D.3    Cohen, J.B.4    Blanton, M.P.5
  • 11
    • 0031755752 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern
    • Li, H. & Papadopoulos, V. Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern. Endocrinology 139, 4991-4997 (1998). (Pubitemid 28533447)
    • (1998) Endocrinology , vol.139 , Issue.12 , pp. 4991-4997
    • Li, H.1    Papadopoulos, V.2
  • 12
    • 0035970108 scopus 로고    scopus 로고
    • Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide
    • DOI 10.1073/pnas.031461598
    • Li, H., Yao, Z., Degenhardt, B., Teper, G., & Papadopoulos, V. Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide. Proc. Natl. Acad. Sci. U. S. A 98, 1267-1272 (2001). (Pubitemid 32121221)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.3 , pp. 1267-1272
    • Li, H.1    Yao, Z.-X.2    Degenhardt, B.3    Teper, G.4    Papadopoulos, V.5
  • 13
    • 45449105538 scopus 로고    scopus 로고
    • Proteins and cholesterol-rich domains
    • Epand, R. M. Proteins and cholesterol-rich domains. Biochim. Biophys. Acta 1778, 1576-1582 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1576-1582
    • Epand, R.M.1
  • 14
    • 77952305288 scopus 로고    scopus 로고
    • Cholesterol interaction with proteins that partition into membrane domains: An overview
    • Epand, R. M., Thomas, A., Brasseur, R., & Epand, R. F. Cholesterol interaction with proteins that partition into membrane domains: an overview. Subcell. Biochem. 51, 253-278 (2010).
    • (2010) Subcell. Biochem. , vol.51 , pp. 253-278
    • Epand, R.M.1    Thomas, A.2    Brasseur, R.3    Epand, R.F.4
  • 15
    • 16844383101 scopus 로고    scopus 로고
    • The tryptophan-rich region of HIV gp41 and the promotion of cholesterol-rich domains
    • DOI 10.1021/bi0500224
    • Epand, R. F., Sayer, B. G., & Epand, R. M. The tryptophan-rich region of HIV gp41 and the promotion of cholesterol-rich domains. Biochemistry 44, 5525-5531 (2005). (Pubitemid 40489992)
    • (2005) Biochemistry , vol.44 , Issue.14 , pp. 5525-5531
    • Epand, R.F.1    Sayer, B.G.2    Epand, R.M.3
  • 16
    • 33744512299 scopus 로고    scopus 로고
    • Cholesterol and the interaction of proteins with membrane domains
    • DOI 10.1016/j.plipres.2006.02.001, PII S0163782706000154
    • Epand, R. M. Cholesterol and the interaction of proteins with membrane domains. Prog. Lipid Res. 45, 279-294 (2006). (Pubitemid 43818129)
    • (2006) Progress in Lipid Research , vol.45 , Issue.4 , pp. 279-294
    • Epand, R.M.1
  • 17
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • Hilf, R. J. & Dutzler, R. Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel. Nature 457, 115-118 (2009).
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.J.1    Dutzler, R.2
  • 18
    • 58149267953 scopus 로고    scopus 로고
    • X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
    • Bocquet, N. et al. X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation. Nature 457, 111-114 (2009).
    • (2009) Nature , vol.457 , pp. 111-114
    • Bocquet, N.1
  • 19
    • 0036821982 scopus 로고    scopus 로고
    • Lipid matters: Nicotinic acetylcholine receptor-lipid interactions (review)
    • DOI 10.1080/09687680210166226
    • Barrantes, F. J. Lipid matters: nicotinic acetylcholine receptor-lipid interactions (Review). Mol. Membr. Biol. 19, 277-284 (2002). (Pubitemid 36090788)
    • (2002) Molecular Membrane Biology , vol.19 , Issue.4 , pp. 277-284
    • Barrantes, F.J.1
  • 21
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4 A resolution
    • DOI 10.1016/j.jmb.2004.12.031
    • Unwin, N. Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J. Mol. Biol. 346, 967-989 (2005). (Pubitemid 40215523)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.4 , pp. 967-989
    • Unwin, N.1
  • 22
    • 71549116093 scopus 로고    scopus 로고
    • Sphingolipid/cholesterol regulation of neurotransmitter receptor conformation and function
    • Fantini, J. & Barrantes, F. J. Sphingolipid/cholesterol regulation of neurotransmitter receptor conformation and function. Biochim. Biophys. Acta 1788, 2345-2361 (2009).
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2345-2361
    • Fantini, J.1    Barrantes, F.J.2
  • 23
    • 0027441795 scopus 로고
    • Protein-lipid interactions and Torpedo californica nicotinic acetylcholine receptor function. 2. Membrane fluidity and ligand-mediated alteration in the accessibility of γ subunit cysteine residues to cholesterol
    • DOI 10.1021/bi00097a021
    • Narayanaswami, V. & McNamee, M. G. Protein-lipid interactions and Torpedo californica nicotinic acetylcholine receptor function. 2. Membrane fluidity and ligand-mediated alteration in the accessibility of gamma subunit cysteine residues to cholesterol. Biochemistry 32, 12420-12427 (1993). (Pubitemid 23357964)
    • (1993) Biochemistry , vol.32 , Issue.46 , pp. 12420-12427
    • Narayanaswami, V.1    McNamee, M.G.2
  • 24
    • 0043166978 scopus 로고    scopus 로고
    • Lipid-protein interactions and effect of local anesthetics in acetylcholine receptor-rich membranes from Torpedo marmorata electric organ
    • DOI 10.1021/bi034485q
    • Mantipragada, S. B. et al. Lipid-protein interactions and effect of local anesthetics in acetylcholine receptor-rich membranes from Torpedo marmorata electric organ. Biochemistry 42, 9167-9175 (2003). (Pubitemid 36935426)
    • (2003) Biochemistry , vol.42 , Issue.30 , pp. 9167-9175
    • Mantipragada, S.B.1    Horvath, L.I.2    Arias, H.R.3    Schwarzmann, G.4    Sandhoff, K.5    Barrantes, F.J.6    Marsh, D.7
  • 25
    • 33847119788 scopus 로고    scopus 로고
    • G protein-coupled receptor signaling complexity in neuronal tissue: Implications for novel therapeutics
    • DOI 10.2174/156720507779939850
    • Maudsley, S., Martin, B., & Luttrell, L. M. G protein-coupled receptor signaling complexity in neuronal tissue: implications for novel therapeutics. Curr. Alzheimer Res. 4, 3-19 (2007). (Pubitemid 46293880)
    • (2007) Current Alzheimer Research , vol.4 , Issue.1 , pp. 3-19
    • Maudsley, S.1    Martin, B.2    Luttrell, L.M.3
  • 26
    • 78751662442 scopus 로고    scopus 로고
    • The role of G protein-coupled receptors in the pathology of Alzheimer's disease
    • Thathiah, A. & De, S. B. The role of G protein-coupled receptors in the pathology of Alzheimer's disease. Nat. Rev. Neurosci. 12, 73-87 (2011).
    • (2011) Nat. Rev. Neurosci. , vol.12 , pp. 73-87
    • Thathiah, A.1    De, S.B.2
  • 27
    • 77951904180 scopus 로고    scopus 로고
    • Neuronal nicotinic acetylcholine receptorcholesterol crosstalk in Alzheimer's disease
    • Barrantes, F. J., Borroni, V., & Valles, S. Neuronal nicotinic acetylcholine receptorcholesterol crosstalk in Alzheimer's disease. FEBS Lett. 584, 1856-1863 (2010).
    • (2010) FEBS Lett. , vol.584 , pp. 1856-1863
    • Barrantes, F.J.1    Borroni, V.2    Valles, S.3
  • 29
    • 0142027322 scopus 로고    scopus 로고
    • Modulation of nicotinic acetylcholine receptor function through the outer and middle rings of transmembrane domains
    • Barrantes, F. J. Modulation of nicotinic acetylcholine receptor function through the outer and middle rings of transmembrane domains. Curr. Opin. Drug Discov. Devel. 6, 620-632 (2003). (Pubitemid 37287931)
    • (2003) Current Opinion in Drug Discovery and Development , vol.6 , Issue.5 , pp. 620-632
    • Barrantes, F.J.1
  • 30
    • 0037070567 scopus 로고    scopus 로고
    • High free energy of lipid/protein interaction in biological membranes
    • DOI 10.1016/S0014-5793(02)02400-6, PII S0014579302024006
    • Sandermann, H., Jr. High free energy of lipid/protein interaction in biological membranes. FEBS Lett. 514, 340-342 (2002). (Pubitemid 34273965)
    • (2002) FEBS Letters , vol.514 , Issue.2-3 , pp. 340-342
    • Sandermann Jr., H.1
  • 31
  • 32
    • 0035834626 scopus 로고    scopus 로고
    • The lipid/protein interface as xenobiotic target site: Kinetic analysis of the nicotinic acetylcholine receptor
    • Walcher, S., Altschuh, J., & Sandermann, H., Jr. The lipid/protein interface as xenobiotic target site: kinetic analysis of the nicotinic acetylcholine receptor. J. Biol. Chem. 276, 42191-42195 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 42191-42195
    • Walcher, S.1    Altschuh, J.2    Sandermann Jr., H.3
  • 33
    • 67650066494 scopus 로고    scopus 로고
    • Anionic lipid and cholesterol interactions with alpha4beta2 nAChR: Insights from MD simulations
    • Cheng, M. H., Xu, Y., & Tang, P. Anionic lipid and cholesterol interactions with alpha4beta2 nAChR: insights from MD simulations. J. Phys. Chem. B 113, 6964-6970 (2009).
    • (2009) J. Phys. Chem. B , vol.113 , pp. 6964-6970
    • Cheng, M.H.1    Xu, Y.2    Tang, P.3
  • 34
    • 66149092693 scopus 로고    scopus 로고
    • Binding and release of cholesterol in the Osh4 protein of yeast
    • Singh, R. P., Brooks, B. R., & Klauda, J. B. Binding and release of cholesterol in the Osh4 protein of yeast. Proteins 75, 468-477 (2009).
    • (2009) Proteins , vol.75 , pp. 468-477
    • Singh, R.P.1    Brooks, B.R.2    Klauda, J.B.3
  • 36
    • 0038694994 scopus 로고    scopus 로고
    • Snorkeling of lysine side chains in transmembrane helices: How easy can it get?
    • DOI 10.1016/S0014-5793(03)00475-7
    • Strandberg, E. & Killian, J. A. Snorkeling of lysine side chains in transmembrane helices: how easy can it get? FEBS Lett. 544, 69-73 (2003). (Pubitemid 36628038)
    • (2003) FEBS Letters , vol.544 , Issue.1-3 , pp. 69-73
    • Strandberg, E.1    Killian, J.A.2
  • 38
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • DOI 10.1038/nature06717, PII NATURE06717
    • Hilf, R. J. & Dutzler, R. X-ray structure of a prokaryotic pentameric ligand-gated ion channel. Nature 452, 375-379 (2008). (Pubitemid 351430790)
    • (2008) Nature , vol.452 , Issue.7185 , pp. 375-379
    • Hilf, R.J.C.1    Dutzler, R.2
  • 41
    • 38449113609 scopus 로고    scopus 로고
    • Cholesterol effects on nicotinic acetylcholine receptor
    • Barrantes, F. J. Cholesterol effects on nicotinic acetylcholine receptor. J Neurochem. 103 Suppl 1, 72-80 (2007).
    • (2007) J Neurochem. 103 Suppl , vol.1 , pp. 72-80
    • Barrantes, F.J.1
  • 42
    • 77950180614 scopus 로고    scopus 로고
    • Multilevel fragment-based approach (MFBA): ANovel Hybrid Computational method for the study of large molecules
    • Rezác, J. & Salahub, D. R. Multilevel Fragment-Based Approach (MFBA): ANovel Hybrid Computational Method for the Study of Large Molecules. J. Chem. Theory Comput. 6, 91-99 (2010).
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 91-99
    • Rezác, J.1    Salahub, D.R.2
  • 43
    • 77949360652 scopus 로고    scopus 로고
    • How cholesterol constrains glycolipid conformation for optimal recognition of Alzheimer's beta amyloid peptide (Abeta1-40)
    • Yahi, N., Aulas, A., & Fantini, J. How cholesterol constrains glycolipid conformation for optimal recognition of Alzheimer's beta amyloid peptide (Abeta1-40). PLoS. One. 5, e9079 (2010).
    • (2010) PLoS. One. , vol.5
    • Yahi, N.1    Aulas, A.2    Fantini, J.3
  • 44
    • 33744826819 scopus 로고    scopus 로고
    • MolDock: A new technique for high-accuracy molecular docking
    • DOI 10.1021/jm051197e
    • Thomsen, R. & Christensen, M. H. MolDock: a new technique for high-accuracy molecular docking. J. Med. Chem. 49, 3315-3321 (2006). (Pubitemid 43830529)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.11 , pp. 3315-3321
    • Thomsen, R.1    Christensen, M.H.2


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