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Published on February 16, 2007; 10.1104/pp.106.095091

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Received December 20, 2006
Accepted February 6, 2007

Overexpression of Arabidopsis AGD7 Causes Relocation of Golgi-localized Proteins to the ER and Inhibits Protein Trafficking in Plant Cells

Myung Ki Min , Soo Jin Kim , Yangsong Miao , Juyeon Shin , Liwen Jiang , and Inhwan Hwang *

Center for Plant Intracellular Trafficking and Division of Molecular and Life Sciences; Pohang University of Science and Technology, Pohang, 790-784, Korea and Department of Biology and Molecular Biotechnology Program; The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China

* Corresponding author; email: ihhwang{at}postech.ac.kr.

ADP ribosylation factor (Arf) GTPase activating proteins (GAPs) promote the hydrolysis of GTP bound to Arfs to GDP, which plays a pivotal role in regulating Arfs by converting the active GTP-bound forms of these proteins into their inactive GDP-bound forms. Here, we investigated the biological role of AGD7, an Arf GAP homolog, in Arabidopsis. We show that AGD7 bears a highly-conserved N-terminal region and a unique C-terminal region, interacts with Arf1 both in vitro and in vivo, and stimulates Arf1 GTPase activity in a phosphatidic acid-dependent manner in vitro. In plant cells, AGD7 localized to the Golgi complex, where its overexpression was found to inhibit the Golgi-localization of {gamma}-COP and promote the relocation of Golgi proteins into the ER in both protoplasts and transgenic plants. Furthermore, overexpression of AGD7 inhibited anterograde trafficking of proteins from the ER. We propose that AGD7 functions as a GAP for Arf1 in the Golgi complex and plays a critical role in protein trafficking by controlling Arf1 activity.




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