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Volumn 109, Issue 1, 2012, Pages 285-290

Depolarization induces a conformational change in the binding site region of the M 2 muscarinic receptor

Author keywords

Acetylcholine; Electrochromic; Fluorescence quenching; Gating

Indexed keywords

ACETYLCHOLINE; FLUORESCENT DYE; G PROTEIN COUPLED RECEPTOR; MUSCARINIC M2 RECEPTOR;

EID: 84856011296     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1119424109     Document Type: Article
Times cited : (32)

References (25)
  • 1
    • 79953156424 scopus 로고    scopus 로고
    • Conformational changes in the M2 muscarinic receptor induced by membrane voltage and agonist binding
    • Navarro-Polanco RA, et al. (2011) Conformational changes in the M2 muscarinic receptor induced by membrane voltage and agonist binding. J Physiol 589:1741-1753.
    • (2011) J Physiol , vol.589 , pp. 1741-1753
    • Navarro-Polanco, R.A.1
  • 2
    • 33750580538 scopus 로고    scopus 로고
    • Movement of 'gating charge' is coupled to ligand binding in a G-protein-coupled receptor
    • DOI 10.1038/nature05259, PII NATURE05259
    • Ben-Chaim Y, et al. (2006) Movement of 'gating charge' is coupled to ligand binding in a G-protein-coupled receptor. Nature 444:106-109. (Pubitemid 44684765)
    • (2006) Nature , vol.444 , Issue.7115 , pp. 106-109
    • Ben-Chaim, Y.1    Chanda, B.2    Dascal, N.3    Bezanilla, F.4    Parnas, I.5    Parnas, H.6
  • 3
    • 0038605062 scopus 로고    scopus 로고
    • The M2 muscarinic G-protein-coupled receptor is voltage-sensitive
    • Ben-Chaim Y, Tour O, Dascal N, Parnas I, Parnas H (2003) The M2 muscarinic G-protein-coupled receptor is voltage-sensitive. J Biol Chem 278:22482-22491.
    • (2003) J Biol Chem , vol.278 , pp. 22482-22491
    • Ben-Chaim, Y.1    Tour, O.2    Dascal, N.3    Parnas, I.4    Parnas, H.5
  • 4
    • 33747682900 scopus 로고    scopus 로고
    • The metabotropic glutamate G-protein-coupled receptors mGluR3 and mGluR1a are voltage-sensitive
    • DOI 10.1074/jbc.M513447200
    • Ohana L, Barchad O, Parnas I, Parnas H (2006) The metabotropic glutamate G-protein-coupled receptors mGluR3 and mGluR1a are voltage-sensitive. J Biol Chem 281: 24204-24215. (Pubitemid 44274194)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.34 , pp. 24204-24215
    • Ohana, L.1    Barchad, O.2    Parnas, I.3    Parnas, H.4
  • 10
    • 0032832975 scopus 로고    scopus 로고
    • Depolarization affects the binding properties of muscarinic acetylcholine receptors and their interaction with proteins of the exocytic apparatus
    • Ilouz N, Branski L, Parnis J, Parnas H, Linial M (1999) Depolarization affects the binding properties of muscarinic acetylcholine receptors and their interaction with proteins of the exocytic apparatus. J Biol Chem 274:29519-29528.
    • (1999) J Biol Chem , vol.274 , pp. 29519-29528
    • Ilouz, N.1    Branski, L.2    Parnis, J.3    Parnas, H.4    Linial, M.5
  • 11
    • 0025871087 scopus 로고
    • Depolarization-induced changes in the muscarinic receptor in rat brain and heart are mediated by Pertussis-toxin-sensitive G-proteins
    • Cohen-Armon M, Sokolovsky M (1991) Depolarization-induced changes in the muscarinic receptor in rat brain and heart are mediated by pertussis-toxin- sensitive G-proteins. J Biol Chem 266:2595-2605. (Pubitemid 21909105)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.4 , pp. 2595-2605
    • Cohen-Armon, M.1    Sokolovsky, M.2
  • 12
    • 0015868742 scopus 로고
    • Currents related to movement of the gating particles of the sodium channels
    • Armstrong CM, Bezanilla F (1973) Currents related to movement of the gating particles of the sodium channels. Nature 242:459-461.
    • (1973) Nature , vol.242 , pp. 459-461
    • Armstrong, C.M.1    Bezanilla, F.2
  • 13
    • 0031697562 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1085/jgp.112.4.391
    • Cha A, Bezanilla F (1998) Structural implications of fluorescence quenching in the Shaker K+ channel. J Gen Physiol 112:391-408. (Pubitemid 28467597)
    • (1998) Journal of General Physiology , vol.112 , Issue.4 , pp. 391-408
    • Cha, A.1    Bezanilla, F.2
  • 14
    • 0036490942 scopus 로고    scopus 로고
    • Allosteric binding sites on cell-surface receptors: Novel targets for drug discovery
    • Christopoulos A (2002) Allosteric binding sites on cell-surface receptors: Novel targets for drug discovery. Nat Rev Drug Discov 1:198-210.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 198-210
    • Christopoulos, A.1
  • 15
    • 0037426919 scopus 로고    scopus 로고
    • A fluorometric approach to local electric field measurements in a voltage-gated ion channel
    • DOI 10.1016/S0896-6273(02)01126-1
    • Asamoah OK, Wuskell JP, Loew LM, Bezanilla F (2003) A fluorometric approach to local electric field measurements in a voltage-gated ion channel. Neuron 37:85-97. (Pubitemid 36106436)
    • (2003) Neuron , vol.37 , Issue.1 , pp. 85-97
    • Asamoah, O.K.1    Wuskell, J.P.2    Loew, L.M.3    Bezanilla, F.4
  • 16
    • 77749317396 scopus 로고    scopus 로고
    • New mechanism for voltage induced charge movement revealed in GPCRs-Theory and experiments
    • Zohar A, Dekel N, Rubinsky B, Parnas H (2010) New mechanism for voltage induced charge movement revealed in GPCRs-Theory and experiments. PLoS ONE 5:e8752.
    • (2010) PLoS ONE , vol.5
    • Zohar, A.1    Dekel, N.2    Rubinsky, B.3    Parnas, H.4
  • 17
    • 78651335929 scopus 로고    scopus 로고
    • A novel fast mechanism for GPCR-mediated signal transduction-Control of neurotransmitter release
    • Kupchik YM, et al. (2011) A novel fast mechanism for GPCR-mediated signal transduction-Control of neurotransmitter release. J Cell Biol 192:137-151.
    • (2011) J Cell Biol , vol.192 , pp. 137-151
    • Kupchik, Y.M.1
  • 18
    • 33750530193 scopus 로고    scopus 로고
    • Detection of the opening of the bundle crossing in KcsA with fluorescence lifetime spectroscopy reveals the existence of two gates for ion conduction
    • DOI 10.1085/jgp.200609638
    • Blunck R, Cordero-Morales JF, Cuello LG, Perozo E, Bezanilla F (2006) Detection of the opening of the bundle crossing in KcsA with fluorescence lifetime spectroscopy reveals the existence of two gates for ion conduction. J Gen Physiol 128:569-581. (Pubitemid 44664634)
    • (2006) Journal of General Physiology , vol.128 , Issue.5 , pp. 569-581
    • Blunck, R.1    Cordero-Morales, J.F.2    Cuello, L.G.3    Perozo, E.4    Bezanilla, F.5
  • 19
    • 77951223981 scopus 로고    scopus 로고
    • Identification of orthosteric and allosteric site mutations in M2 muscarinic acetylcholine receptors that contribute to ligand-selective signaling bias
    • Gregory KJ, Hall NE, Tobin AB, Sexton PM, Christopoulos A (2010) Identification of orthosteric and allosteric site mutations in M2 muscarinic acetylcholine receptors that contribute to ligand-selective signaling bias. J Biol Chem 285:7459-7474.
    • (2010) J Biol Chem , vol.285 , pp. 7459-7474
    • Gregory, K.J.1    Hall, N.E.2    Tobin, A.B.3    Sexton, P.M.4    Christopoulos, A.5
  • 21
    • 79954987479 scopus 로고    scopus 로고
    • The role of transmembrane domain 3 in the actions of orthosteric, allosteric, and atypical agonists of the M4 muscarinic acetylcholine receptor
    • Leach K, Davey AE, Felder CC, Sexton PM, Christopoulos A (2011) The role of transmembrane domain 3 in the actions of orthosteric, allosteric, and atypical agonists of the M4 muscarinic acetylcholine receptor. Mol Pharmacol 79:855-865.
    • (2011) Mol Pharmacol , vol.79 , pp. 855-865
    • Leach, K.1    Davey, A.E.2    Felder, C.C.3    Sexton, P.M.4    Christopoulos, A.5
  • 22
    • 33745282128 scopus 로고    scopus 로고
    • Allosteric interactions with muscarinic acetylcholine receptors: Complex role of the conserved tryptophan M2422Trp in a critical cluster of amino acids for baseline affinity, subtype selectivity, and cooperativity
    • Prilla S, Schrobang J, Ellis J, Höltje HD, Mohr K (2006) Allosteric interactions with muscarinic acetylcholine receptors: Complex role of the conserved tryptophan M2422Trp in a critical cluster of amino acids for baseline affinity, subtype selectivity, and cooperativity. Mol Pharmacol 70:181-193.
    • (2006) Mol Pharmacol , vol.70 , pp. 181-193
    • Prilla, S.1    Schrobang, J.2    Ellis, J.3    Höltje, H.D.4    Mohr, K.5
  • 23
    • 0032321375 scopus 로고    scopus 로고
    • Cut-open oocyte voltage-clamp technique
    • Stefani E, Bezanilla F (1998) Cut-open oocyte voltage-clamp technique. Methods Enzymol 293:300-318.
    • (1998) Methods Enzymol , vol.293 , pp. 300-318
    • Stefani, E.1    Bezanilla, F.2
  • 25
    • 0017697163 scopus 로고
    • Inactivation of the sodium channel. I. Sodium current experiments
    • Bezanilla F, Armstrong CM (1977) Inactivation of the sodium channel. I. Sodium current experiments. J Gen Physiol 70:549-566. (Pubitemid 8239321)
    • (1977) Journal of General Physiology , vol.70 , Issue.5 , pp. 549-566
    • Bezanilla, F.1    Armstrong, C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.