{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,28]],"date-time":"2025-11-28T17:09:30Z","timestamp":1764349770124},"reference-count":61,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2003,12,23]],"date-time":"2003-12-23T00:00:00Z","timestamp":1072137600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Traffic"],"published-print":{"date-parts":[[2004,2]]},"abstract":"<jats:p> <jats:bold>GGAs comprise a family of Arf\u2010dependent coat proteins or adaptors that regulate vesicle traffic from the <jats:italic>trans<\/jats:italic>\u2010Golgi network (TGN). GGAs bind activated Arf, cargo, and additional components necessary for vesicle budding through interactions with their four functional domains: VHS, GAT, hinge, and GAE. We identified three sites of phosphorylation in GGA1 by tandem mass spectrometry: S268 and T270 in the GAT domain and S480 in the hinge. Expression of HA\u2010GGA1 in mammalian cells and comparison to endogenous GGA1 confirmed their localization to late Golgi compartments. In contrast, mutations that mimic the phosphoprotein (HA\u2010GGA1[S268D] or HA\u2010GGA1[T270D]) at either of the sites in the GAT domain caused a decrease in the colocalization with markers of the Golgi and TGN and an increase in puncta in cytoplasm. Quantitative comparisons of the extent of colocalization of GGA1 proteins with the known components of GGA1 vesicles revealed that the composition of those markers tested in HA\u2010GGA1[S268D] and HA\u2010GGA1[T270D] vesicles were indistinguishable from those of HA\u2010GGA1 vesicles. 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