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Volume 272, Number 15, Issue of April 11, 1997 pp. 9601-9604
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
beta -Adrenergic Receptor Kinase (GRK2) Colocalizes with beta -Adrenergic Receptors during Agonist-induced Receptor Internalization

(Received for publication, January 13, 1997, and in revised form, February 10, 1997)

Ana Ruiz-Gómez and Federico Mayor Jr.

From the Departamento de Biología Molecular and Centro de Biología Molecular "Severo Ochoa" (Consejo Superior de Investigaciones Científicas-Universidad Autónoma) Universidad Autónoma de Madrid, 28049 Madrid, Spain

Rapid regulation of G protein-coupled receptors appears to involve agonist-promoted receptor phosphorylation by G protein-coupled receptor kinases (GRKs). This is followed by binding of uncoupling proteins termed arrestins and transient receptor internalization. In this report we show that the beta -adrenergic receptor kinase (beta ARK-1 or GRK2) follows a similar pattern of internalization upon agonist activation of beta 2-adrenergic receptors (beta 2AR) and that beta ARK expression levels modulate receptor sequestration. Stable cotransfected cells expressing an epitope-tagged beta 2AR and beta ARK-1 show an increased rate and extent of beta 2AR internalization compared with cells expressing receptor alone. Moreover, subcellular gradient fractionation studies suggest that beta ARK colocalizes with the internalized receptors. In fact, double immunofluorescence analysis using confocal microscopy shows extensive colocalization of beta 2AR and beta ARK in intracellular vesicles upon receptor stimulation. Our results confirm a functional relationship between receptor phosphorylation and sequestration and indicate that beta ARK does not only translocates from the cytoplasm to the plasma membrane in response to receptor occupancy, but shares endocytic mechanisms with the beta 2AR. These data suggest a direct role for beta ARK in the sequestration process and/or the involvement of receptor internalization in the intracellular trafficking of the kinase.


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