Key roles of hydrophobic rings of TM2 in gating of the α9α10 nicotinic cholinergic receptor
We have performed a systematic mutagenesis of three hydrophobic rings (17′, 13′ and 9′) within transmembrane region (TM) 2 of the α9α10 nicotinic cholinergic receptor (nAChR) to a hydrophilic (threonine) residue and compared the properties of mutant receptors reconstituted in Xenopus laevis oocytes....
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2005
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 13349caa a22013817a 4500 | ||
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| 001 | PAPER-4019 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203331.0 | ||
| 008 | 190411s2005 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-23744483520 | |
| 024 | 7 | |2 cas |a tropisetron, 89565-68-4; Acetylcholine, 51-84-3; Calcium, 7440-70-2; Cholinergic Agents; Chrna9 protein, rat; Protein Subunits; Receptors, Nicotinic; Recombinant Proteins; alpha10 acetylcholine receptor, rat | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a BJPCB | ||
| 100 | 1 | |a Plazas, P.V. | |
| 245 | 1 | 0 | |a Key roles of hydrophobic rings of TM2 in gating of the α9α10 nicotinic cholinergic receptor |
| 260 | |c 2005 | ||
| 270 | 1 | 0 | |m Elgoyhen, A.B.; Institute de Investigaciones en Ingenieria Genetica y Biologia Molecular (INGEBI), CONICET-UBA, Vuelta de Obligado 2490, Buenos Aires 1428, Argentina; email: elgoyhen@dna.uba.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 504 | |a Weisstaub, N., Vetter, D., Elgoyhen, A., Katz, E., The alpha9/alpha10 nicotinic acetylcholine receptor is permeable to and is modulated by divalent cations (2002) Hearing Res., 167, pp. 122-135 | ||
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| 520 | 3 | |a We have performed a systematic mutagenesis of three hydrophobic rings (17′, 13′ and 9′) within transmembrane region (TM) 2 of the α9α10 nicotinic cholinergic receptor (nAChR) to a hydrophilic (threonine) residue and compared the properties of mutant receptors reconstituted in Xenopus laevis oocytes. Phenotypic changes in α9α10 mutant receptors were evidenced by a decrease in the desensitization rate, an increase in both the EC 50 for ACh as well as the efficacy of partial agonists and the reduction of the allosteric modulation by extracellular Ca 2+. Mutated receptors exhibited spontaneous openings and, at the single-channel level, an increased apparent mean open time with no major changes in channel conductance, thus suggesting an increase in gating of the channel as the underlying mechanism. Overall, the degrees of the phenotypes of mutant receptors were more overt in the case of the centrally located V13′T mutant. Based on the atomic model of the pore of the electric organ of the Torpedo ray, we can propose that the interactions of side chains at positions 13′ and 9′ are key ones in creating an energetic barrier to ion permeation. In spite of the fact that the roles of the TM2 residues are mostly conserved in the distant α9α10 member of the nAChR family, their mechanistic contributions to channel gating show significant differences when compared to other nAChRs. These differences might be originated from slight differential intramolecular rearrangements during gating for the different receptors and might lead each nAChR to be in tune with their physiological roles. © 2005 Nature Publishing Group All rights reserved. |l eng | |
| 593 | |a Institute de Investigaciones en Ingenieria Genetica y Biologia Molecular (INGEBI), CONICET-UBA, Vuelta de Obligado 2490, Buenos Aires 1428, Argentina | ||
| 593 | |a Instituto de Investigaciones Bioquímicas de Bahía Blanca, UNS-CONICET, Bahía Blanca F-8000FWB, Argentina | ||
| 593 | |a Departamento de Fisiología, Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires 1428, Argentina | ||
| 593 | |a Columbia Genome Center, Columbia University, 1150 St Nicholas Ave., New York, NY 10032, United States | ||
| 593 | |a Columbia University, 1051 Riverside Drive, New York, NY 10032, United States | ||
| 690 | 1 | 0 | |a ACETYLCHOLINE |
| 690 | 1 | 0 | |a CHANNEL GATING |
| 690 | 1 | 0 | |a CYS-LOOP RECEPTORS |
| 690 | 1 | 0 | |a IONOTROPIC RECEPTORS |
| 690 | 1 | 0 | |a NICOTINIC RECEPTORS |
| 690 | 1 | 0 | |a NICOTINIC RECEPTOR |
| 690 | 1 | 0 | |a PARTIAL AGONIST |
| 690 | 1 | 0 | |a TROPISETRON |
| 690 | 1 | 0 | |a ANIMAL CELL |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CHANNEL GATING |
| 690 | 1 | 0 | |a CONTROLLED STUDY |
| 690 | 1 | 0 | |a ELECTRIC ORGAN |
| 690 | 1 | 0 | |a EXTRACELLULAR CALCIUM |
| 690 | 1 | 0 | |a HYDROPHILICITY |
| 690 | 1 | 0 | |a HYDROPHOBICITY |
| 690 | 1 | 0 | |a ION TRANSPORT |
| 690 | 1 | 0 | |a MEMBRANE POTENTIAL |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PHENOTYPE |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a RING OPENING |
| 690 | 1 | 0 | |a XENOPUS LAEVIS |
| 690 | 1 | 0 | |a ACETYLCHOLINE |
| 690 | 1 | 0 | |a ALLOSTERIC REGULATION |
| 690 | 1 | 0 | |a AMINO ACID SEQUENCE |
| 690 | 1 | 0 | |a ANIMALS |
| 690 | 1 | 0 | |a CALCIUM |
| 690 | 1 | 0 | |a CHOLINERGIC AGENTS |
| 690 | 1 | 0 | |a DOSE-RESPONSE RELATIONSHIP, DRUG |
| 690 | 1 | 0 | |a ION CHANNEL GATING |
| 690 | 1 | 0 | |a MEMBRANE POTENTIALS |
| 690 | 1 | 0 | |a MOLECULAR SEQUENCE DATA |
| 690 | 1 | 0 | |a MUTAGENESIS, SITE-DIRECTED |
| 690 | 1 | 0 | |a OOCYTES |
| 690 | 1 | 0 | |a PATCH-CLAMP TECHNIQUES |
| 690 | 1 | 0 | |a PHENOTYPE |
| 690 | 1 | 0 | |a PROTEIN SUBUNITS |
| 690 | 1 | 0 | |a RECEPTORS, NICOTINIC |
| 690 | 1 | 0 | |a RECOMBINANT PROTEINS |
| 690 | 1 | 0 | |a SEQUENCE ALIGNMENT |
| 690 | 1 | 0 | |a TRANSFECTION |
| 690 | 1 | 0 | |a XENOPUS LAEVIS |
| 700 | 1 | |a De Rosa, M.J. | |
| 700 | 1 | |a Gomez-Casati, M.E. | |
| 700 | 1 | |a Verbitsky, M. | |
| 700 | 1 | |a Weisstaub, N. | |
| 700 | 1 | |a Katz, E. | |
| 700 | 1 | |a Bouzat, C. | |
| 700 | 1 | |a Elgoyhen, A.B. | |
| 773 | 0 | |d 2005 |g v. 145 |h pp. 963-974 |k n. 7 |p Br. J. Pharmacol. |x 00071188 |w (AR-BaUEN)CENRE-9552 |t British Journal of Pharmacology | |
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