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First published online July 18, 2002; 10.1104/pp.003624

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Plant Physiol, August 2002, Vol. 129, pp. 1507-1520

ADP-Ribosylation Factor 1 of Arabidopsis Plays a Critical Role in Intracellular Trafficking and Maintenance of Endoplasmic Reticulum Morphology in Arabidopsis1

Mi Hee Lee,2 Myung Ki Min,2 Yong Jik Lee, Jing Bo Jin, Dong Han Shin, Dae Heon Kim, Kwang-Hee Lee, and Inhwan Hwang*

Center for Plant Intracellular Trafficking (M.H.L., Y.J.L., J.B.J., D.H.K., K.-H.L., I.H.) and Division of Molecular and Life Sciences (M.K.M., D.H.S., I.H.), Pohang University of Science and Technology, Pohang, 790-784, Korea

ADP-ribosylation factors (Arf), a family of small GTP-binding proteins, play important roles in intracellular trafficking in animal and yeast cells. Here, we investigated the roles of two Arf homologs, Arf1 and Arf3 of Arabidopsis, in intracellular trafficking in plant cells. We generated dominant negative mutant forms of Arf 1 and Arf3 and examined their effect on trafficking of reporter proteins in protoplasts. Arf1[T31N] inhibited trafficking of H+-ATPase:green fluorescent protein (GFP) and sialyltransferase (ST):GFP to the plasma membrane and the Golgi apparatus. In addition, Arf1[T31N] caused relocalization of the Golgi reporter protein ST:GFP to the endoplasmic reticulum (ER). In protoplasts expressing Arf1[T31N], ST:red fluorescent protein remained in the ER, whereas H+-ATPase:GFP was mistargeted to another organelle. Also, expression of Arf1[T31N] in protoplasts resulted in profound changes in the morphology of the ER. The treatment of protoplasts with brefeldin A had exactly the same effect as Arf1[T31N] on various intracellular trafficking pathways. In contrast, Arf3[T31N] did not affect trafficking of any of these reporter proteins. Inhibition experiments using mutants with various domains swapped between Arf1 and Arf3 revealed that the N-terminal domain is interchangeable for trafficking inhibition. However, in addition to the T31N mutation, motifs in domains II, III, and IV of Arf1 were necessary for inhibition of trafficking of H+-ATPase:GFP. Together, these results strongly suggest that Arf1 plays a role in the intracellular trafficking of cargo proteins in Arabidopsis, and that Arf1 functions through a brefeldin A-sensitive factor.

1 This work was supported by a grant from National Creative Research Initiatives from the Ministry of Science and Technology.

2 These authors contributed equally to the paper.

* Corresponding author; e-mail ihhwang{at}postech.ac.kr; fax 82-54-279-8159.

© 2002 American Society of Plant Physiologists


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