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

  • Zhu G
  • Zhai P
  • Wakeham N
 et al. 
  • 3

    Readers

    Mendeley users who have this article in their library.
  • 2

    Citations

    Citations of this article.

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.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

  • Guangyu Zhu

  • Peng Zhai

  • Nancy Wakeham

  • Xiangyuan He

  • Xuejun C. Zhang

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free