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Papers In Press, published online ahead of print March 4, 2005
Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0651
Corresponding Author: mfarquhar{at}ucsd.edu
In this report we characterize GIV (G
J. Biol. Chem, 10.1074/jbc.M501833200
Submitted on February 17, 2005
Revised on March 4, 2005
Accepted on March 4, 2005
Identification and characterization of GIV, a nove G
i/s interacting protein found on COPI, ER-Golgi transport vesicles
____ Interacting Vesicle associated protein), a novel protein that binds members of the Gi and Gs subfamilies of heterotrimeric G proteins. The G interaction site was mapped to an 83 aa 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, 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 Gi3-YFP expressed in Cos7 cells. By immunoelectron microscopy, GIV colocalizes with -COP and Gi3 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 (Gi1-3, Gs) 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 between the ER and the Golgi.
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