NDLI: Stoichiometry of human recombinant neuronal nicotinic receptors containing the β3 subunit expressed in Xenopus oocytes

Content Provider	PubMed Central
Author	Boorman, James P. B. Grootkormelink, Paul J. Sivilotti, Lucia G.
Copyright Year	2000
Abstract	The neuronal nicotinic subunit β3 forms functional receptors when co-expressed with both an α and a β subunit, such as α3 and β4. We examined the subunit stoichiometry of these ‘triplet’α3β4β3 receptors by expression in Xenopus oocytes of the α3, β4 and β3 subunits, either in wild-type form or after insertion of a reporter mutation. The mutation chosen was the substitution of a conserved hydrophobic residue in the second transmembrane domain of the subunits (leucine or valine 9′) with a hydrophilic threonine. In other ion channels within the nicotinic superfamily, this mutation type consistently increases the potency of agonists. In muscle-type nicotinic receptors, the magnitude of this effect is approximately constant for each mutant subunit incorporated. In α3β4β3 receptors, the ACh EC50 was decreased by approximately 17-fold when this mutation was in α3 alone and only by fourfold when β3 alone was mutated. Mutating β4 was equivalent to mutating α3, suggesting that the ‘triplet’ receptor contains one copy of β3 and two copies each of α3 and β4. Mutating β3 and α3 or β3 and β4 reduced the ACh EC50 further, to values two- to threefold lower than those seen when only α3 or β4 carried the mutation. In ‘pair’α3β4 receptors (known to contain two α and three β subunits), mutating β4 had a greater effect on the ACh EC50 than mutating α3, in agreement with an α:β ratio of 2:3 and a constant and independent effect of each copy of the mutation. Our results suggest that α3β4β3 neuronal nicotinic receptors contain one copy of β3 and two copies each of α3 and β4 and confirm that in pair α3β4 receptors the α/β subunits are present in a 2:3 ratio.
Related Links	http://dx.doi.org/10.1111/j.1469-7793.2000.00565.x
Starting Page	565
File Format	PDF
ISSN	14697793
e-ISSN	14697793
Journal	The Journal of Physiology
Issue Number	Pt 3
Volume Number	529
Language	English
Publisher	Blackwell Science Inc
Publisher Date	2000-12-15
Access Restriction	Open
Rights Holder	Blackwell Science Inc
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Physiology Sports Science

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