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J. Biol. Chem., Vol. 269, Issue 1, 37-40, Jan, 1994
I Boekhoff, J Inglese, S Schleicher, WJ Koch, RJ Lefkowitz and H Breer
Olfaction is mediated by G protein-coupled receptors. In isolated rat
olfactory cilia, odorants such as citralva stimulate a burst of cAMP, which
peaks in 50 ms and returns almost to base-line level within 150 ms in the
continuing presence of odorant. This desensitization is mediated by the
cAMP dependent protein kinase and a specialized G protein-coupled receptor
kinase originally termed beta ARK2 (GRK3). In vitro experiments suggest
that the prenylated beta gamma-subunits of heterotrimeric G proteins target
the cytosolic beta ARK1 (GRK2) enzyme to its membrane bound receptor
substrate by binding to sites in its carboxyl terminus. Here we demonstrate
that odorants stimulate translocation of GRK3 from cytosol to membranes in
isolated rat olfactory cilia. We introduced a glutathione
S-transferase-GRK3ct fusion protein, containing the carboxyl-terminal 222
amino acid residues of GRK3, which includes the beta gamma binding site, or
a 28- amino acid peptide derived therefrom, into permeabilized cilia
preparations. These reagents block odorant-mediated enzyme translocation
and desensitization while markedly attenuating odorant- stimulated
phosphorylation of olfactory proteins. These findings suggest that beta
gamma-subunits may physiologically regulate a G protein-coupled receptor
kinase and that enzyme translocation may be a general and required feature
of the activity of some members of this enzyme family.
Olfactory desensitization requires membrane targeting of receptor kinase mediated by beta gamma-subunits of heterotrimeric G proteins
Department of Zoophysiology, Universitat Hohenheim, Stuttgart, Germany.
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