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J Biol Chem, Vol. 273, Issue 25, 15317-15320, June 19, 1998
3 into a Functional Nicotinic Receptor
§,, and
From the We have investigated whether the neuronal
nicotinic subunit Department of Pharmacology, University
College London, Gower St., London WC1E 6BT, United Kingdom and the
§ Department of Experimental Molecular Biology, Janssen
Research Foundation, Turnhoutseweg 30, B-2340 Beerse, Belgium
3 can participate in the assembly of functional
recombinant receptors. Although 3 is expressed in several areas of
the central nervous system, it does not form functional receptors when
expressed heterologously together with an 
or another nicotinic
subunit. We inserted into the human 3 subunit a reporter mutation
(V273T), which, if incorporated into a functional receptor, would be
expected to increase its agonist sensitivity and maximum response to
partial agonists. Expressing the mutant 3V273T in
Xenopus oocytes together with both the 3 and the 4
subunits resulted in the predicted changes in the properties of the
resulting nicotinic receptor when compared with those of 34
receptors. This indicated that some of the receptors incorporated the
mutant 3 subunit, as part of a "triplet" 34 3 receptor.
The proportion of triplet receptors was dependent on the ratios of the
3:4:3 cRNA injected. We conclude that, like the related 5
subunit, the 3 subunit can form functional receptors only if
expressed together with both and subunits.
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