GGAs are a family of adaptor proteins involved in vesicular transport. As an effector of the small GTPase Arf, GGA interacts using its GAT domain with the GTP-bound form of Arf. The GAT domain is also found to interact with ubiquitin and rabaptin-5. Rabaptin-5 is, in turn, an effector of another small GTPase, Rab5, which regulates early endosome fusion. The interaction between GGAs and rabaptin-5 is likely to take place in a pathway between the trans-Golgi network and early endosomes. This chapter describes in vitro biochemical characterization of the interaction between the GGA1 GAT domain and rabaptin-5. Combining with the complex crystal structure, we reveal that the binding mode is helix bundle-to-helix bundle in nature. Copyright 2005, Elsevier Inc. All rights reserved.
Zhu, G., Zhai, P., Wakeham, N., He, X., & Zhang, X. C. (2005). Analysis of the interaction between GGA1 GAT domain and rabaptin-5. Methods in Enzymology, 403, 583–592. https://doi.org/10.1016/S0076-6879(05)03050-8