Functional role of the third cytoplasmic loop in muscarinic receptor dimerization.

The Journal of Biological Chemistry
Roberto MaggioGiovanni U Corsini

Abstract

By means of the expression of two chimeric receptors, alpha2/m3 and m3/alpha2, in which the carboxyl-terminal receptor portions, containing transmembrane (TM) domains VI and VII, were exchanged between the alpha2C adrenergic and the m3 muscarinic receptor, Maggio et al. (Maggio, R., Vogel, Z., and Wess, J. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 3103-31073) demonstrated that G protein-linked receptors are able to interact functionally with each other at the molecular level to form (hetero)dimers. In the present study we tested the hypothesis that interaction between receptors might depend on the presence of a long third intracellular (i3) loop and that shortening this loop could impair the capability of receptors to form dimers. To address this question, we initially created short chimeric alpha2 adrenergic/m3 muscarinic receptors in which 196 amino acids were deleted from the i3 loop (alpha2/m3-short and m3/alpha2-short). Although co-transfection of alpha2/m3 and m3/alpha2 resulted in the appearance of specific binding, the co-expression of the two short constructs (alpha2/m3-short and m3/alpha2-short), either together or in combination, respectively, with m3/alpha2 and alpha2/m3 did not result in any detectable binding act...Continue Reading

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