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J. Biol. Chem., Vol. 280, Issue 23, 22012-22020, June 10, 2005

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Identification and Characterization of GIV, a Novel G_i/s -interacting Protein Found on COPI, Endoplasmic Reticulum-Golgi Transport Vesicles^*

Helen Le-Niculescu, Ingrid Niesman, Thierry Fischer, Luc DeVries, and Marilyn G. Farquhar¶

From the Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, California 92093 and the Departement de Biologie Cellulaire et Moleculaire, Institut de Recherche Pierre Fabre CRPF, Castres Cedex, France 81106

In this report, we characterize GIV (G-interacting vesicle-associated protein), a novel protein that binds members of the G_i and G subfamilies of heterotrimeric G proteins. The G_s interaction site was mapped to an 83-amino acid region of GIV that is enriched in highly charged amino acids. BLAST searches revealed two additional mammalian family members, Daple and an uncharacterized protein, FLJ00354 These family members share the highest homology at the G binding domain, are homologous at the N terminus and central coiled coil domain but diverge at the C terminus. Using affinity-purified IgG made against two different regions of the protein, we localized GIV to COPI, endoplasmic reticulum (ER)-Golgi transport vesicles concentrated in the Golgi region in GH3 pituitary cells and COS7 cells. Identification as COPI vesicles was based on colocalization with -COP, a marker for these vesicles. GIV also codistributes in the Golgi region with endogenous calnuc and the KDEL receptor, which are cis Golgi markers and with G_i3-yellow fluorescent protein expressed in COS7 cells. By immunoelectron microscopy, GIV colocalizes with -COP and G_i3 on vesicles found in close proximity to ER exit sites and to cis Golgi cisternae. In cell fractions prepared from rat liver, GIV is concentrated in a carrier vesicle fraction (CV2) enriched in ER-Golgi transport vesicles. -COP and several G subunits (G_i1–3, G_s) are also most enriched in CV2. Our results demonstrate the existence of a novel G-interacting protein associated with COPI transport vesicles that may play a role in G-mediated effects on vesicle trafficking within the Golgi and/or between the ER and the Golgi.

Received for publication, February 17, 2005

^* This work was supported by National Institutes of Health Grants DK17780 and CA100768 (to M. G. F.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed: Dept. of Cellular and Molecular Medicine, University of California San Diego, 9500 Gilman Dr., George Palade Laboratories of Cellular and Molecular Medicine, La Jolla, CA 92093-0651. Tel.: 858-534-7711; Fax: 858-534-8549; E-mail: mfarquhar{at}ucsd.edu.

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