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A more recent version of this article appeared on October 13, 2000
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M002780200v1
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Papers In Press, published online ahead of print August 3, 2000
J. Biol. Chem, 10.1074/jbc.M002780200
Submitted on April 3, 2000
Revised on July 5, 2000
Accepted on August 3, 2000

Binding of calmodulin to the D2-dopamine receptor reduces receptor signaling by arresting the G protein activation switch

Elisa Bofill-Cardona, Oliver Kudlacek, Qiong Yang, Horst Ahorn, Michael Freissmuth, and Christian Nanoff

Institute of Pharmacology, University of Vienna, Vienna, Austria A-1090

Corresponding Author: christian.nanoff{at}univie.ac.at

Signaling by D2-dopamine receptors in neurons likely proceeds in the presence of Ca2+ oscillations. We here describe the biochemical basis for a cross-talk between intracellular Ca2+ and the D2-receptor. By activation of calmodulin (CaM)1, Ca2+ directly inhibits the D2-receptor; this conclusion is based on the following observations: (i) The receptor contains a CaM-binding motif in the N-terminal end of the 3rd loop, a domain involved in activating Gi/o. A peptide fragment encompassing this domain (D2N) bound dansylated CaM in a Ca2+-dependent manner (KD ~0.1 µM). (ii) Activation of purified Galpha i-1 by D2N, and D2-receptor-promoted GTPgamma S-binding in membranes was suppressed by Ca2+/CaM (IC50 ~ 0.1µM). (iii) If Ca2+-influx was elicited in D2-receptor expressing HEK293 cells, agonist-dependent inhibition of cAMP formation decreased. This effect was not seen with other Gi-coupled receptors (A1-adenosine and Mel1A-melatonin receptor). (iv) The D2-receptor was retained by immobilized CaM and radiolabeled CaM was co-immunoprecipitated with the receptor. Specifically, inhibition by CaM does not result from uncoupling the D2-receptor from its cognate G protein(s); rather, CaM directly targets the D2-receptor to block the receptor-operated G protein activation-switch.


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