A residue in the middle of the M2‐M3 loop of the β4 subunit specifically affects gating of neuronal nicotinic receptors

FEBS Letters

Rovira, José Carlos¹  Vicente-Agulló, Francisco²  Criado, Manuel²  Sala, Francisco²  Campos-Caro, Antonio²  Ballesta, Juan José¹  Sala, Salvador³ 

[1] Departamento de Farmacologı́a, Instituto de Neurociencias, Universidad Miguel Hernández, Campus de San Juan, Aptdo. Correos 18, 03550 San Juan, Alicante, Spain;Departamento de Neuroquı́mica, Instituto de Neurociencias, Universidad Miguel Hernández, Campus de San Juan, Aptdo. Correos 18, 03550 San Juan, Alicante, Spain;Departamento de Fisiologı́a, Instituto de Neurociencias, Universidad Miguel Hernández, Campus de San Juan, Aptdo. Correos 18, 03550 San Juan, Alicante, Spain

关键词: Neuronal nicotinic receptor;    α3β4 Receptor;    Binding and gating coupling;    Single-channel conductance;   

DOI  :  10.1016/S0014-5793(98)00889-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

An aspartate residue in the M2-M3 loop of neuronal nicotinic receptor α₇ subunits is a major determinant of the channel functional response. This residue is conserved in most β₄ subunits, e.g. human and rat, but not in others, e.g. bovine. We have used these differences to examine the mechanism by which this residue alters the functional properties of α₃β₄ receptors. Having ruled out an effect on the macroscopic binding ability of the agonist, the level of receptor expression, or the single channel conductance, the results suggest that receptors lacking that residue have a deficient coupling between binding and gating.

【 授权许可】

Unknown