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Vol. 12, Issue 11, 3573-3588, November 2001
University of Cambridge, Department of Clinical Biochemistry,
Wellcome Trust Centre for the Study of Molecular Mechanisms in Disease,
Cambridge CB2 2XY, United Kingdom
We have previously identified a novel family of proteins called the
GGAs (Golgi-localized, 
-ear-containing, ADP-ribosylation factor-binding proteins). These proteins consist of an
NH2-terminal VHS domain, followed by a GAT domain, a
variable domain, and a -adaptin ear homology domain. Studies from
our own laboratory and others, making use of both yeast and mammals
cells, indicate that the GGAs facilitate trafficking from the
trans-Golgi network to endosomes. Here we have further investigated the
function of the GGAs. We find that GGA-deficient yeast are not only
defective in vacuolar protein sorting but they are also impaired in
their ability to process 
-factor. Using deletion mutants and
chimeras, we show that the VHS domain is required for GGA function and
that the VHS domain from Vps27p will not substitute for the GGA VHS domain. In contrast, the -adaptin ear homology domain contributes to
GGA function but is not absolutely required, and full function can be
restored by replacing the GGA ear domain with the -adaptin ear
domain. Deleting the -adaptin gene together with the two GGA genes exacerbates the phenotype in yeast, suggesting
that they function on parallel pathways. In mammalian cells, the
association of GGAs with the membrane is extremely unstable, which may
account for their absence from purified clathrin-coated vesicles.
Double- and triple-labeling immunofluorescence experiments indicate
that the GGAs and AP-1 are associated with distinct populations of clathrin-coated vesicles budding from the trans-Golgi network. Together
with results from other studies, our findings suggest that the GGAs act
as monomeric adaptors, with the four domains involved in cargo
selection, membrane localization, clathrin binding, and accessory
protein recruitment.
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