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Vol. 14, Issue 6, 2385-2398, June 2003

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Binding Partners for the COOH-Terminal Appendage Domains of the GGAs and -Adaptin

Winnie W.Y. Lui ^*, Brett M. Collins ^* , Jennifer Hirst ^* , Alison Motley ^*, Caroline Millar ^*, Peter Schu , David J. Owen ^*, and Margaret S. Robinson ^* 

^* Department of Clinical Biochemistry, Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 2XY, United Kingdom; Department of Biochemie II, Zentrum für Biochemie und Molekulare Zellbiologie, Universität Göttingen, D-37073 Göttingen, Germany

Submitted November 15, 2002; Revised January 28, 2003; Accepted February 5, 2003
Monitoring Editor: Suzanne R. Pfeffer

The adaptor appendage domains are believed to act as binding platforms for coated vesicle accessory proteins. Using glutathione S-transferase pulldowns from pig brain cytosol, we find three proteins that can bind to the appendage domains of both the AP-1 subunit and the GGAs: -synergin and two novel proteins, p56 and p200. p56 elicited better antibodies than p200 and was generally more tractable. Although p56 and -synergin bind to both GGA and appendages in vitro, immunofluorescence labeling of nocodazole-treated cells shows that p56 colocalizes with GGAs on TGN46-positive membranes, whereas -synergin colocalizes with AP-1 primarily on a different membrane compartment. Furthermore, in AP-1–deficient cells, p56 remains membrane-associated whereas -synergin becomes cytosolic. Thus, p56 and -synergin show very strong preferences for GGAs and AP-1, respectively, in vivo. However, the GGA and appendages share the same fold as determined by x-ray crystallography, and mutagenesis reveals that the same amino acids contribute to their binding sites. By overexpressing wild-type GGA and appendage domains in cells, we can drive p56 and -synergin, respectively, into the cytosol, suggesting a possible mechanism for selectively disrupting the two pathways.

Corresponding author. E-mail address: msr12{at}mole.bio.cam.ac.uk.

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