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Members of the G Protein-Coupled Receptor Kinase Family That Phosphorylate the β2-Adrenergic Receptor Facilitate Sequestration

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Howard Hughes Medical Institute Laboratories and Departments of Cell Biology, Medicine, and Biochemistry, Duke University Medical Center, Durham, North Carolina 27710
Cite this: Biochemistry 1996, 35, 13, 4155–4160
Publication Date (Web):April 2, 1996
https://doi.org/10.1021/bi952961+
Copyright © 1996 American Chemical Society

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    Abstract

    We recently reported that a β2-adrenergic receptor (β2AR) mutant, Y326A, defective in its ability to sequester in response to agonist stimulation was a poor substrate for G protein-coupled receptor kinase (GRK)-mediated phosphorylation; however, its ability to be phosphorylated and sequestered could be restored by overexpressing GRK2 [Ferguson etal. (1995) J.Biol.Chem.270, 24782]. In the present report, we tested the ability of each of the known GRKs (GRK1−6) to phosphorylate and rescue the sequestration of the Y326A mutant in HEK-293 cells. We demonstrate that in addition to GRK2, GRK3−6 can phosphorylate the Y326A mutant and rescue its sequestration; however, GRK1 was totally ineffective in rescuing either the phosphorylation or the sequestration of the mutant receptor. We found that the agonist-dependent rescue of Y326A mutant phosphorylation by GRK2, -3, and -5 was associated with the agonist-dependent rescue of sequestration. In contrast, overexpression of GRK4 and -6 led mainly to agonist-independent phosphorylation of the Y326A mutant accompanied by increased basal receptor sequestration. Our results demonstrate that phosphorylation perse, but not the interaction with a specific GRK, is required to facilitate β2AR sequestration.

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     This work was supported by NIH Grant NS 19576 and by a Bristol Myers Squibb Unrestricted Grant Award to M.G.C. S.S.G.F. is the recipient of a fellowship from The Medical Research Council of Canada. L.S.B. is the recipient of a fellowship from the Howard Hughes Medical Institute.

     Department of Cell Biology, Duke University Medical Center.

    §

     These authors contributed equally to this work.

     Howard Hughes Medical Institute Laboratories.

     Department of Biochemistry, Duke University Medical Center.

    *

     To whom correspondence should be addressed at the Duke University Medical Center, Box 3287, Durham, NC 27710. Telephone:  (919) 684-5433. Fax:  (919) 681-8641.

     Abstract published in Advance ACS Abstracts, March 15, 1996.

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