Analysis of the interaction between GGA1 GAT domain and Rabaptin-5.
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.
Guangyu
G
Zhu
Peng
P
Zhai
Nancy
N
Wakeham
Xiangyuan
X
He
Xuejun C
XC
Zhang
D020727:ADP-Ribosylation Factors / Q000378:metabolism*; D033942:Adaptor Proteins, Vesicular Transport / Q000378:metabolism*; D002460:Cell Line; D018076:DNA, Complementary; D006801:Humans; D011485:Protein Binding; D033921:Vesicular Transport Proteins / Q000378:metabolism*
D033942:Adaptor Proteins, Vesicular Transport; D018076:DNA, Complementary; C407306:GGA adaptor proteins; C097227:RABEP1 protein, human; D033921:Vesicular Transport Proteins; D020727:ADP-Ribosylation Factors