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The Plant Cell, Vol. 13, 1511-1526, July 2001, Copyright © 2001,
American Society of Plant Biologists

A New Dynamin-Like Protein, ADL6, Is Involved in Trafficking from the trans-Golgi Network to the Central Vacuole in Arabidopsis

Jing Bo Jina, Young A Kimb, Soo Jin Kimb, Sung Hoon Leeb, Dae Heon Kimb, Gang-Won Cheongc and Inhwan Hwangb,1

a Department of Molecular Biology, Gyeongsang National University, Chinju 660-701, Korea
b Center for Plant Intracellular Trafficking and Division of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Korea
c Department of Biochemistry, Gyeongsang National University, Chinju 660-701, Korea

1 To whom correspondence should be addressed. E-mail ihhwang{at}postech.ac.kr; fax 82-54-279-8159

Dynamin, a high-molecular-weight GTPase, plays a critical role in vesicle formation at the plasma membrane during endocytosis in animal cells. Here we report the identification of a new dynamin homolog in Arabidopsis named Arabidopsis dynamin-like 6 (ADL6). ADL6 is quite similar to dynamin I in its structural organization: a conserved GTPase domain at the N terminus, a pleckstrin homology domain at the center, and a Pro-rich motif at the C terminus. In the cell, a majority of ADL6 is associated with membranes. Immunohistochemistry and in vivo targeting experiments revealed that ADL6 is localized to the Golgi apparatus. Expression of the dominant negative mutant ADL6[K51E] in Arabidopsis protoplasts inhibited trafficking of cargo proteins destined for the lytic vacuole and caused them to accumulate at the trans-Golgi network. In contrast, expression of ADL6[K51E] did not affect trafficking of a cargo protein, H+-ATPase:green fluorescent protein, destined for the plasma membrane. These results suggest that ADL6 is involved in vesicle formation for vacuolar trafficking at the trans-Golgi network but not for trafficking to the plasma membrane in plant cells.




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