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GGA proteins: new players in the sorting game

Annette L. Boman

Department of Biochemistry and Molecular Biology, University of Minnesota, School of Medicine Duluth, 10 University Drive, Duluth, MN 55812, USA



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Fig. 1. Domain organization of GGA proteins. The amino acids comprising each domain are shown, using the numbering of human GGA1. The domains are described in detail in the text.

 


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Fig. 2. Pathways in yeast tested for GGA involvement. Each of the molecules shown was tested for trafficking defects in strains lacking both GGA genes. Proteins with defective sorting and/or transport are highlighted in blue. Proteins with altered processing but normal transport are shown in green. Transport pathways unaffected by loss of GGA proteins are in black. The early and late endosomes are shown together as the prevacuolar compartment (PVC). Abbreviations: TGN, trans-Golgi network; ALP, alkaline phosphatase; CPS, carboxypeptidase S; CPY, carboxypeptidase Y.

 


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Fig. 3. Model of GGA interactions with other proteins. Each domain of GGA proteins has been shown to interact with one or more proteins. These interactions are depicted to occur at the TGN membrane, facilitating cargo sorting and vesicle formation in response to GTP exchange on ARF.

 





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