Analysis of the interaction between GGA1 GAT domain and rabaptin-5

2Citations
Citations of this article
4Readers
Mendeley users who have this article in their library.
Get full text

Abstract

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.

Cite

CITATION STYLE

APA

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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free