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Vol. 11, Issue 4, 1241-1255, April 2000
Department of Biochemistry, Emory University School of Medicine,
Atlanta, Georgia 30322-3050
A family of three structurally related proteins were cloned
from human cDNA libraries by their ability to interact preferentially with the activated form of human ADP-ribosylation factor 3 (ARF3) in
two-hybrid assays. The specific and GTP-dependent binding was later
confirmed through direct protein binding of recombinant proteins. The
three proteins share large (
300 residues) domains at their N termini
that are 60-70% identical to each other and a shorter (73 residues)
domain at their C termini with 70% homology to the C-terminal
"ear" domain of 
-adaptin. Although GGA1 is found predominantly
as a soluble protein by cell fractionation, all three proteins were
found to localize to the trans-Golgi network (TGN) by
indirect immunofluorescence. The binding of GGAs to TGN was sensitive
to brefeldin A, consistent with this being an ARF-dependent event.
Thus, these proteins have been named Golgi-localizing, -adaptin ear
homology domain, ARF-binding proteins, or GGAs. The finding that
overexpression of GGAs was sufficient to alter the distribution of
markers of the TGN (TGN38 and mannose 6-phosphate receptors) led us to
propose that GGAs are effectors for ARFs that function in the
regulation of membrane traffic through the TGN.
Corresponding author. E-mail address:
rkahn{at}bimcore.emory.edu.
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