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Volume 272, Number 31, Issue of August 1, 1997 pp. 19099-19102
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
A Novel Interaction between Adrenergic Receptors and the alpha -Subunit of Eukaryotic Initiation Factor 2B

(Received for publication, March 25, 1997, and in revised form, May 2, 1997)

Uwe Klein Dagger § , M. Teresa Ramirez Dagger § , Brian K. Kobilka Dagger Dagger Dagger and Mark von Zastrow §

From the § Nina Ireland Laboratory, Departments of Psychiatry and Cellular and Molecular Pharmacology, University of California, San Francisco, California 94143-0984 and the Dagger Dagger  Howard Hughes Medical Institute and Dagger  Division of Cardiovascular Medicine, Stanford University Medical School, Stanford, California 94305

The alpha -subunit of eukaryotic initiation factor 2B (eIF-2B), a guanine nucleotide exchange protein that functions in regulation of translation, was observed to associate with the carboxyl-terminal cytoplasmic domains of the alpha 2A- and alpha 2B-adrenergic receptors in a yeast two-hybrid screen of a cDNA library prepared from 293 cells. This protein association was confirmed in vitro by affinity chromatography and was shown to be specific for a subset of G protein-coupled receptors, including the alpha 2A-, alpha 2B-, alpha 2C-, and beta 2-adrenergic receptors, but not the vasopressin (V2) receptor. Association of these proteins in vivo was confirmed by specific co-immunoprecipitation of eIF-2Balpha with full-length beta 2-adrenergic receptors expressed in transfected 293 cells and by fluorescence microscopy showing co-localization of these proteins in intact cells. Remarkably, eIF-2Balpha co-localized with receptors exclusively in regions of the plasma membrane that are in contact with the extracellular medium, but failed to associate with membranes making cell-cell contacts. Overexpression of eIF-2Balpha in 293 cells caused a small (~15%) but significant enhancement of beta 2-adrenergic receptor-mediated activation of adenylyl cyclase, without affecting forskolin or V2 receptor-mediated activation. These observations suggest a new role for a previously identified guanine nucleotide exchange protein in membrane biology and cell signaling.


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