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J. Biol. Chem., Vol. 267, Issue 4, 2222-2227, 02, 1992
K Haga and T Haga
We have partially purified a protein kinase that phosphorylates muscarinic
receptors (mAChR) in the presence of agonists and have shown that the
phosphorylation is stimulated by the beta gamma subunits of the GTP binding
protein Go (Haga, K., and Haga, T. (1990) FEBS Lett. 268, 43-47). We report
here that rhodopsin is also phosphorylated in a light-dependent manner by
the same kinase preparation and that beta gamma subunits derived from Gs,
Gi, and Go stimulate the phosphorylation of both rhodopsin and mAChRs. The
rhodopsin- and mAChR- phosphorylating activities were eluted in the same
fractions using a purification procedure that is essentially the same as
that used for the purification of beta-adrenergic receptor kinase (Benovic,
J.L., Strasser, R.H., Caron, M.G., and Lefkowitz, R.J. (1986) Proc. Natl.
Acad. Sci. U. S. A. 83, 2797-2801) and were inhibited by low concentrations
of heparin, an inhibitor of beta-adrenergic receptor kinase, (IC50 = 15
nM), suggesting that both mAChR and rhodopsin are phosphorylated by the
same or very similar kinase(s) belonging to the beta-adrenergic receptor
kinase family. G protein beta gamma subunits increased the Vmax of the
phosphorylation of rhodopsin 12-fold. Kinetic data were consistent with the
assumptions that the protein kinase (mAChR kinase) binds rhodopsin and beta
gamma subunits in a random order and that the reaction rate is proportional
to concentration of the ternary complex. By contrast, the light-dependent
phosphorylation of rhodopsin by the rhodopsin kinase was not stimulated by
the beta gamma subunits. These results indicate that beta gamma subunits
may interact with and activate the mAChR kinase but not rhodopsin kinase
and suggest that the beta gamma subunit of G proteins may take part in the
desensitization of G protein-linked receptors.
Activation by G protein beta gamma subunits of agonist- or light- dependent phosphorylation of muscarinic acetylcholine receptors and rhodopsin
Department of Biochemistry, Faculty of Medicine, University of Tokyo, Japan.
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