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Volumn 12, Issue 10, 2004, Pages 1909-1918

Structural dynamics of the M4 transmembrane segment during acetylcholine receptor gating

Author keywords

[No Author keywords available]

Indexed keywords

CHOLINERGIC RECEPTOR; MEMBRANE PROTEIN;

EID: 4644289077     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2004.08.004     Document Type: Article
Times cited : (84)

References (47)
  • 1
    • 0029859799 scopus 로고    scopus 로고
    • Binding sites contribute unequally to the gating of mouse nicotinic alpha D200N acetylcholine receptors
    • Akk G., Sine S., Auerbach A. Binding sites contribute unequally to the gating of mouse nicotinic alpha D200N acetylcholine receptors. J. Physiol. 496:1996;185-196
    • (1996) J. Physiol. , vol.496 , pp. 185-196
    • Akk, G.1    Sine, S.2    Auerbach, A.3
  • 2
    • 0038149197 scopus 로고    scopus 로고
    • Life at the top: The transition state of AChR gating
    • Auerbach, A. (2003). Life at the top: the transition state of AChR gating. Sci. STKE 2003, re11.
    • (2003) Sci. STKE , vol.2003
    • Auerbach, A.1
  • 3
    • 0036821982 scopus 로고    scopus 로고
    • Lipid matters: Nicotinic acetylcholine receptor-lipid interactions (Review)
    • Barrantes F.J. Lipid matters. nicotinic acetylcholine receptor-lipid interactions (Review) Mol. Membr. Biol. 19:2002;277-284
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 277-284
    • Barrantes, F.J.1
  • 4
    • 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. Dev. 6:2003;620-632
    • (2003) Curr. Opin. Drug Discov. Dev. , vol.6 , pp. 620-632
    • Barrantes, F.J.1
  • 5
    • 0026654217 scopus 로고
    • Mapping the lipid-exposed regions in the Torpedo californica nicotinic acetylcholine receptor
    • Blanton M.P., Cohen J.B. Mapping the lipid-exposed regions in the Torpedo californica nicotinic acetylcholine receptor. Biochemistry. 31:1992;3738-3750
    • (1992) Biochemistry , vol.31 , pp. 3738-3750
    • Blanton, M.P.1    Cohen, J.B.2
  • 6
    • 0028326435 scopus 로고
    • Identifying the lipid-protein interface of the Torpedo nicotinic acetylcholine receptor: Secondary structure implications
    • Blanton M.P., Cohen J.B. Identifying the lipid-protein interface of the Torpedo nicotinic acetylcholine receptor. secondary structure implications Biochemistry. 33:1994;2859-2872
    • (1994) Biochemistry , vol.33 , pp. 2859-2872
    • Blanton, M.P.1    Cohen, J.B.2
  • 7
    • 0024725677 scopus 로고
    • Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptor
    • Blount P., Merlie J.P. Molecular basis of the two nonequivalent ligand binding sites of the muscle nicotinic acetylcholine receptor. Neuron. 3:1989;349-357
    • (1989) Neuron , vol.3 , pp. 349-357
    • Blount, P.1    Merlie, J.P.2
  • 8
    • 0031595748 scopus 로고    scopus 로고
    • Mutations at lipid-exposed residues of the acetylcholine receptor affect its gating kinetics
    • Bouzat C., Roccamo A.M., Garbus I., Barrantes F.J. Mutations at lipid-exposed residues of the acetylcholine receptor affect its gating kinetics. Mol. Pharmacol. 54:1998;146-153
    • (1998) Mol. Pharmacol. , vol.54 , pp. 146-153
    • Bouzat, C.1    Roccamo, A.M.2    Garbus, I.3    Barrantes, F.J.4
  • 9
    • 0034059664 scopus 로고    scopus 로고
    • Nicotinic receptor fourth transmembrane domain: Hydrogen bonding by conserved threonine contributes to channel gating kinetics
    • Bouzat C., Barrantes F., Sine S. Nicotinic receptor fourth transmembrane domain. hydrogen bonding by conserved threonine contributes to channel gating kinetics J. Gen. Physiol. 115:2000;663-672
    • (2000) J. Gen. Physiol. , vol.115 , pp. 663-672
    • Bouzat, C.1    Barrantes, F.2    Sine, S.3
  • 10
    • 0036221142 scopus 로고    scopus 로고
    • Subunit-selective contribution to channel gating of the M4 domain of the nicotinic receptor
    • Bouzat C., Gumilar F., del Carmen Esandi M., Sine S.M. Subunit-selective contribution to channel gating of the M4 domain of the nicotinic receptor. Biophys. J. 82:2002;1920-1929
    • (2002) Biophys. J. , vol.82 , pp. 1920-1929
    • Bouzat, C.1    Gumilar, F.2    Del Carmen Esandi, M.3    Sine, S.M.4
  • 11
    • 0040074444 scopus 로고    scopus 로고
    • The 2.7 a structure of AChBP, homologue of the ligand-binding domain of the nicotinic acetylcholine receptor
    • discussion 29-32, 165-168
    • Brejc K., van Dijk W.J., Smit A.B., Sixma T.K. The 2.7 A structure of AChBP, homologue of the ligand-binding domain of the nicotinic acetylcholine receptor. Novartis Found. Symp. 245:2002;22-29. discussion 29-32, 165-168
    • (2002) Novartis Found. Symp. , vol.245 , pp. 22-29
    • Brejc, K.1    Van Dijk, W.J.2    Smit, A.B.3    Sixma, T.K.4
  • 12
    • 1842475289 scopus 로고    scopus 로고
    • Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures
    • Celie P.H., van Rossum-Fikkert S.E., van Dijk W.J., Brejc K., Smit A.B., Sixma T.K. Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures. Neuron. 41:2004;907-914
    • (2004) Neuron , vol.41 , pp. 907-914
    • Celie, P.H.1    Van Rossum-Fikkert, S.E.2    Van Dijk, W.J.3    Brejc, K.4    Smit, A.B.5    Sixma, T.K.6
  • 13
    • 0242583056 scopus 로고    scopus 로고
    • The role of loop 5 in acetylcholine receptor channel gating
    • Chakrapani S., Bailey T.D., Auerbach A. The role of loop 5 in acetylcholine receptor channel gating. J. Gen. Physiol. 122:2003;521-539
    • (2003) J. Gen. Physiol. , vol.122 , pp. 521-539
    • Chakrapani, S.1    Bailey, T.D.2    Auerbach, A.3
  • 14
    • 1842686239 scopus 로고    scopus 로고
    • Gating dynamics of the acetylcholine receptor extracellular domain
    • Chakrapani S., Bailey T.D., Auerbach A. Gating dynamics of the acetylcholine receptor extracellular domain. J. Gen. Physiol. 123:2004;341-356
    • (2004) J. Gen. Physiol. , vol.123 , pp. 341-356
    • Chakrapani, S.1    Bailey, T.D.2    Auerbach, A.3
  • 15
    • 0032215090 scopus 로고    scopus 로고
    • Allosteric receptors after 30 years
    • Changeux J.P., Edelstein S.J. Allosteric receptors after 30 years. Neuron. 21:1998;959-980
    • (1998) Neuron , vol.21 , pp. 959-980
    • Changeux, J.P.1    Edelstein, S.J.2
  • 16
    • 0031468619 scopus 로고    scopus 로고
    • Identification of amino acids contributing to high and low affinity d-tubocurarine sites in the Torpedo nicotinic acetylcholine receptor
    • Chiara D.C., Cohen J.B. Identification of amino acids contributing to high and low affinity d-tubocurarine sites in the Torpedo nicotinic acetylcholine receptor. J. Biol. Chem. 272:1997;32940-32950
    • (1997) J. Biol. Chem. , vol.272 , pp. 32940-32950
    • Chiara, D.C.1    Cohen, J.B.2
  • 17
    • 0037197654 scopus 로고    scopus 로고
    • Structure of the transition state of gating in the acetylcholine receptor channel pore: A phi-value analysis
    • Cymes G.D., Grosman C., Auerbach A. Structure of the transition state of gating in the acetylcholine receptor channel pore. a phi-value analysis Biochemistry. 41:2002;5548-5555
    • (2002) Biochemistry , vol.41 , pp. 5548-5555
    • Cymes, G.D.1    Grosman, C.2    Auerbach, A.3
  • 18
    • 0034813320 scopus 로고    scopus 로고
    • The kinetics of competitive antagonism by cisatracurium of embryonic and adult nicotinic acetylcholine receptors
    • Demazumder D., Dilger J.P. The kinetics of competitive antagonism by cisatracurium of embryonic and adult nicotinic acetylcholine receptors. Mol. Pharmacol. 60:2001;797-807
    • (2001) Mol. Pharmacol. , vol.60 , pp. 797-807
    • Demazumder, D.1    Dilger, J.P.2
  • 19
    • 0036623799 scopus 로고    scopus 로고
    • Desensitization of diliganded mouse muscle nicotinic acetylcholine receptor channels
    • Elenes S., Auerbach A. Desensitization of diliganded mouse muscle nicotinic acetylcholine receptor channels. J. Physiol. 541:2002;367-383
    • (2002) J. Physiol. , vol.541 , pp. 367-383
    • Elenes, S.1    Auerbach, A.2
  • 21
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht A.R., Matouschek A., Serrano L. The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224:1992;771-782
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 22
    • 0036629771 scopus 로고    scopus 로고
    • Identification of threonine 422 in transmembrane domain alpha M4 of the nicotinic acetylcholine receptor as a possible site of interaction with hydrocortisone
    • Garbus I., Roccamo A.M., Barrantes F.J. Identification of threonine 422 in transmembrane domain alpha M4 of the nicotinic acetylcholine receptor as a possible site of interaction with hydrocortisone. Neuropharmacology. 43:2002;65-73
    • (2002) Neuropharmacology , vol.43 , pp. 65-73
    • Garbus, I.1    Roccamo, A.M.2    Barrantes, F.J.3
  • 23
    • 0036040016 scopus 로고    scopus 로고
    • Linear free-energy relationships and the dynamics of gating in the acetylcholine receptor channel - A Phi-value analysis of an allosteric transition at the single-molecule level
    • Grosman C. Linear free-energy relationships and the dynamics of gating in the acetylcholine receptor channel - A Phi-value analysis of an allosteric transition at the single-molecule level. J. Biol. Phys. 28:2002;267-277
    • (2002) J. Biol. Phys. , vol.28 , pp. 267-277
    • Grosman, C.1
  • 24
    • 0346365092 scopus 로고    scopus 로고
    • Free-energy landscapes of ion-channel gating are malleable: Changes in the number of bound ligands are accompanied by changes in the location of the transition state in acetylcholine-receptor channels
    • Grosman C. Free-energy landscapes of ion-channel gating are malleable. changes in the number of bound ligands are accompanied by changes in the location of the transition state in acetylcholine-receptor channels Biochemistry. 42:2003;14977-14987
    • (2003) Biochemistry , vol.42 , pp. 14977-14987
    • Grosman, C.1
  • 25
    • 0034064135 scopus 로고    scopus 로고
    • Asymmetric and independent contribution of the second transmembrane segment 12′ residues to diliganded gating of acetylcholine receptor channels: A single-channel study with choline as the agonist
    • Grosman C., Auerbach A. Asymmetric and independent contribution of the second transmembrane segment 12′ residues to diliganded gating of acetylcholine receptor channels. a single-channel study with choline as the agonist J. Gen. Physiol. 115:2000;637-651
    • (2000) J. Gen. Physiol. , vol.115 , pp. 637-651
    • Grosman, C.1    Auerbach, A.2
  • 26
    • 0033811476 scopus 로고    scopus 로고
    • The extracellular linker of muscle acetylcholine receptor channels is a gating control element
    • a
    • Grosman C., Salamone F.N., Sine S.M., Auerbach A. The extracellular linker of muscle acetylcholine receptor channels is a gating control element. J. Gen. Physiol. 116:2000;327-340. a
    • (2000) J. Gen. Physiol. , vol.116 , pp. 327-340
    • Grosman, C.1    Salamone, F.N.2    Sine, S.M.3    Auerbach, A.4
  • 27
    • 0034677524 scopus 로고    scopus 로고
    • Mapping the conformational wave of acetylcholine receptor channel gating
    • b
    • Grosman C., Zhou M., Auerbach A. Mapping the conformational wave of acetylcholine receptor channel gating. Nature. 403:2000;773-776. b
    • (2000) Nature , vol.403 , pp. 773-776
    • Grosman, C.1    Zhou, M.2    Auerbach, A.3
  • 28
    • 0035042719 scopus 로고    scopus 로고
    • Protein mobility and GABA-induced conformational changes in GABA(A) receptor pore-lining M2 segment
    • Horenstein J., Wagner D.A., Czajkowski C., Akabas M.H. Protein mobility and GABA-induced conformational changes in GABA(A) receptor pore-lining M2 segment. Nat. Neurosci. 4:2001;477-485
    • (2001) Nat. Neurosci. , vol.4 , pp. 477-485
    • Horenstein, J.1    Wagner, D.A.2    Czajkowski, C.3    Akabas, M.H.4
  • 29
    • 0001736094 scopus 로고
    • Perfection of a synaptic receptor: Kinetics and energetics of the acetylcholine receptor
    • Jackson M.B. Perfection of a synaptic receptor. kinetics and energetics of the acetylcholine receptor Proc. Natl. Acad. Sci. USA. 86:1989;2199-2203
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2199-2203
    • Jackson, M.B.1
  • 30
    • 0029593370 scopus 로고
    • Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins
    • Karlin A., Akabas M.H. Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins. Neuron. 15:1995;1231-1244
    • (1995) Neuron , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, M.H.2
  • 31
    • 0028219505 scopus 로고
    • Mutations in the M4 domain of Torpedo californica acetylcholine receptor dramatically alter ion channel function
    • Lee Y.H., Li L., Lasalde J., Rojas L., McNamee M., Ortiz-Miranda S.I., Pappone P. Mutations in the M4 domain of Torpedo californica acetylcholine receptor dramatically alter ion channel function. Biophys. J. 66:1994;646-653
    • (1994) Biophys. J. , vol.66 , pp. 646-653
    • Lee, Y.H.1    Li, L.2    Lasalde, J.3    Rojas, L.4    McNamee, M.5    Ortiz-Miranda, S.I.6    Pappone, P.7
  • 33
    • 0026704565 scopus 로고
    • Site-specific mutations of nicotinic acetylcholine receptor at the lipid-protein interface dramatically alter ion channel gating
    • Li L., Lee Y.H., Pappone P., Palma A., McNamee M.G. Site-specific mutations of nicotinic acetylcholine receptor at the lipid-protein interface dramatically alter ion channel gating. Biophys. J. 62:1992;61-63
    • (1992) Biophys. J. , vol.62 , pp. 61-63
    • Li, L.1    Lee, Y.H.2    Pappone, P.3    Palma, A.4    McNamee, M.G.5
  • 34
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa A., Fujiyoshi Y., Unwin N. Structure and gating mechanism of the acetylcholine receptor pore. Nature. 423:2003;949-955
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 35
    • 0030873046 scopus 로고    scopus 로고
    • Mutations in the M4 domain of the Torpedo californica nicotinic acetylcholine receptor alter channel opening and closing
    • Ortiz-Miranda S.I., Lasalde J.A., Pappone P.A., McNamee M.G. Mutations in the M4 domain of the Torpedo californica nicotinic acetylcholine receptor alter channel opening and closing. J. Membr. Biol. 158:1997;17-30
    • (1997) J. Membr. Biol. , vol.158 , pp. 17-30
    • Ortiz-Miranda, S.I.1    Lasalde, J.A.2    Pappone, P.A.3    McNamee, M.G.4
  • 36
    • 1542285356 scopus 로고    scopus 로고
    • Restoration of single-channel currents using the segmental k-means method based on hidden Markov modeling
    • Qin F. Restoration of single-channel currents using the segmental k-means method based on hidden Markov modeling. Biophys. J. 86:2004;1488-1501
    • (2004) Biophys. J. , vol.86 , pp. 1488-1501
    • Qin, F.1
  • 37
    • 0030956174 scopus 로고    scopus 로고
    • Maximum likelihood estimation of aggregated Markov processes
    • Qin F., Auerbach A., Sachs F. Maximum likelihood estimation of aggregated Markov processes. Proc. R. Soc. Lond. B. Biol. Sci. 264:1997;375-383
    • (1997) Proc. R. Soc. Lond. B. Biol. Sci. , vol.264 , pp. 375-383
    • Qin, F.1    Auerbach, A.2    Sachs, F.3
  • 38
    • 0033808511 scopus 로고    scopus 로고
    • A direct optimization approach to hidden Markov modeling for single channel kinetics
    • Qin F., Auerbach A., Sachs F. A direct optimization approach to hidden Markov modeling for single channel kinetics. Biophys. J. 79:2000;1915-1927
    • (2000) Biophys. J. , vol.79 , pp. 1915-1927
    • Qin, F.1    Auerbach, A.2    Sachs, F.3
  • 39
    • 0033561222 scopus 로고    scopus 로고
    • A re-examination of adult mouse nicotinic acetylcholine receptor channel activation kinetics
    • Salamone F.N., Zhou M., Auerbach A. A re-examination of adult mouse nicotinic acetylcholine receptor channel activation kinetics. J. Physiol. 516:1999;315-330
    • (1999) J. Physiol. , vol.516 , pp. 315-330
    • Salamone, F.N.1    Zhou, M.2    Auerbach, A.3
  • 40
    • 0036891560 scopus 로고    scopus 로고
    • The nicotinic receptor ligand binding domain
    • Sine S.M. The nicotinic receptor ligand binding domain. J. Neurobiol. 53:2002;431-446
    • (2002) J. Neurobiol. , vol.53 , pp. 431-446
    • Sine, S.M.1
  • 41
    • 0026045588 scopus 로고
    • Gamma- and delta-subunits regulate the affinity and the cooperativity of ligand binding to the acetylcholine receptor
    • Sine S.M., Claudio T. Gamma- and delta-subunits regulate the affinity and the cooperativity of ligand binding to the acetylcholine receptor. J. Biol. Chem. 266:1991;19369-19377
    • (1991) J. Biol. Chem. , vol.266 , pp. 19369-19377
    • Sine, S.M.1    Claudio, T.2
  • 42
    • 0032772075 scopus 로고    scopus 로고
    • Alteration in ion channel function of mouse nicotinic acetylcholine receptor by mutations in the M4 transmembrane domain
    • Tamamizu S., Lee Y., Hung B., McNamee M.G., Lasalde-Dominicci J.A. Alteration in ion channel function of mouse nicotinic acetylcholine receptor by mutations in the M4 transmembrane domain. J. Membr. Biol. 170:1999;157-164
    • (1999) J. Membr. Biol. , vol.170 , pp. 157-164
    • Tamamizu, S.1    Lee, Y.2    Hung, B.3    McNamee, M.G.4    Lasalde-Dominicci, J.A.5
  • 43
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 a resolution
    • Unwin N. Nicotinic acetylcholine receptor at 9 A resolution. J. Mol. Biol. 229:1993;1101-1124
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 44
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin N. Acetylcholine receptor channel imaged in the open state. Nature. 373:1995;37-43
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 45
    • 0034731271 scopus 로고    scopus 로고
    • The Croonian Lecture 2000. Nicotinic acetylcholine receptor and the structural basis of fast synaptic transmission
    • Unwin N. The Croonian Lecture 2000. Nicotinic acetylcholine receptor and the structural basis of fast synaptic transmission. Philos. Trans. R. Soc. Lond. B Biol. Sci. 355:2000;1813-1829
    • (2000) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.355 , pp. 1813-1829
    • Unwin, N.1
  • 46
    • 0037015161 scopus 로고    scopus 로고
    • Lipids in the structure, folding, and function of the KcsA K+ channel
    • Valiyaveetil F.I., Zhou Y., MacKinnon R. Lipids in the structure, folding, and function of the KcsA K+ channel. Biochemistry. 41:2002;10771-10777
    • (2002) Biochemistry , vol.41 , pp. 10771-10777
    • Valiyaveetil, F.I.1    Zhou, Y.2    MacKinnon, R.3
  • 47
    • 0033621177 scopus 로고    scopus 로고
    • Serum choline activates mutant acetylcholine receptors that cause slow channel congenital myasthenic syndromes
    • Zhou M., Engel A.G., Auerbach A. Serum choline activates mutant acetylcholine receptors that cause slow channel congenital myasthenic syndromes. Proc. Natl. Acad. Sci. USA. 96:1999;10466-10471
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10466-10471
    • Zhou, M.1    Engel, A.G.2    Auerbach, A.3


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