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© The Rockefeller University Press, 0021-9525/2000//81 $5.00
The Journal of Cell Biology, Volume 149, Number 1, , 2000 81-94

Ggas

Esteban C. Dell'Angelica^a, Rosa Puertollano^a, Chris Mullins^a, Rubén C. Aguilar^a, José D. Vargas^a, Lisa M. Hartnell^a, and Juan S. Bonifacino^a

^a Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Building 18T, Room 101, National Institutes of Health, Bethesda, MD 20892.(301) 402-0078(301) 496-6368

juan{at}helix.nih.gov

Formation of intracellular transport intermediates and selection of cargo molecules are mediated by protein coats associated with the cytosolic face of membranes. Here, we describe a novel family of ubiquitous coat proteins termed GGAs, which includes three members in humans and two in yeast. GGAs have a modular structure consisting of a VHS domain, a region of homology termed GAT, a linker segment, and a region with homology to the ear domain of -adaptins. Immunofluorescence microscopy showed colocalization of GGAs with Golgi markers, whereas immunoelectron microscopy of GGA3 revealed its presence on coated vesicles and buds in the area of the TGN. Treatment with brefeldin A or overexpression of dominant-negative ADP ribosylation factor 1 (ARF1) caused dissociation of GGAs from membranes. The GAT region of GGA3 was found to: target a reporter protein to the Golgi complex; induce dissociation from membranes of ARF-regulated coats such as AP-1, AP-3, AP-4, and COPI upon overexpression; and interact with activated ARF1. Disruption of both GGA genes in yeast resulted in impaired trafficking of carboxypeptidase Y to the vacuole. These observations suggest that GGAs are components of ARF-regulated coats that mediate protein trafficking at the TGN.

Key Words: trans-Golgi network • ADP ribosylation factor • coats • adaptins • VHS

© 2000 The Rockefeller University Press

Abbreviations used in this paper: 3AT, 3-amino-1,2,4-triazole; AP, adaptor protein; ARF, ADP-ribosylation factor; BFA, brefeldin A; CPY, carboxypeptidase Y; GAE, -adaptin ear; GAL4ad, GAL4 transcription activation domain; GAL4bd, GAL4 binding domain; GAT, GGA and TOM1; GFP, green fluorescent protein; GST, glutathione-S-transferase; GTPS, guanosine 5'-O-(3-thiotriphosphate); ORF, open reading frame; TOM1, target of myb1.

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• Sweeney, D. A., Siddhanta, A., Shields, D. (2002). Fragmentation and Re-assembly of the Golgi Apparatus in Vitro. A REQUIREMENT FOR PHOSPHATIDIC ACID AND PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE SYNTHESIS. J. Biol. Chem. 277: 3030-3039 [Abstract] [Full Text]  
• Santy, L. C., Casanova, J. E. (2001). Activation of ARF6 by ARNO stimulates epithelial cell migration through downstream activation of both Rac1 and phospholipase D. JCB 154: 599-610 [Abstract] [Full Text]  
• Poon, P. P., Nothwehr, S. F., Singer, R. A., Johnston, G. C. (2001). The Gcs1 and Age2 ArfGAP proteins provide overlapping essential function for transport from the yeast trans-Golgi network. JCB 155: 1239-1250 [Abstract] [Full Text]  

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