Abstract
GGAs (Golgi-localizing, γ-adaptin ear homology domain, ARF-binding proteins) are a family of monomeric clathrin adaptor proteins that are conserved from yeasts to humans. The GGA molecule is composed of four functional regions : a VHS domain that interacts with TGN sorting receptors, such as mannose 6-phosphate receptors (MPR) ; a GAT domain that binds to the GTP-bound form of ARF; a hinge region that interacts with clathrin; a GAE domain interacts with accessory proteins. We have determined the crystal structures of VHS, GAT and AP-1 γ-ear domain that is the homolog of GAE domain. And we have also revealed the crystal structure of glucuronyltransferase, GlcAT-P which is critical enzyme in the biosynthesis of the carbohydrate epitope HNK-1.
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