Plant Cell Advance Online Publication
Published on November 4, 2008; 10.1105/tpc.107.057711
OPEN ACCESS ARTICLE
Received December 20, 2007
Returned for revision September 23, 2008
Accepted October 24, 2008
A SNARE Complex Unique to Seed Plants Is Required for Protein Storage Vacuole Biogenesis and Seed Development of Arabidopsis thaliana
Kazuo Ebine 1, Yusuke Okatani 1, Tomohiro Uemura 1, Tatsuaki Goh 1, Keiko Shoda 2, Mitsuru Niihama 3, Miyo Terao Morita 3, Christoph Spitzer 4, Marisa S. Otegui 4, Akihiko Nakano 5, and Takashi Ueda 1*
1 Department of Biological Sciences, Graduate School of Science, University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan
2 Molecular Membrane Biology Laboratory, RIKEN Discovery Research Institute, Wako, Saitama 351-0198, Japan
3 Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0101, Japan
4 Department of Botany, University of Wisconsin, Madison, Wisconsin 53706
5 Department of Biological Sciences, Graduate School of Science, University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan; Molecular Membrane Biology Laboratory, RIKEN Discovery Research Institute, Wako, Saitama 351-0198, Japan
* To whom correspondence should be addressed. E-mail: tueda{at}biol.s.u-tokyo.ac.jp.
The SNARE complex is a key regulator of vesicular traffic, executing membrane fusion between transport vesicles or organelles and target membranes. A functional SNARE complex consists of four coiled-coil helical bundles, three of which are supplied by Q-SNAREs and another from an R-SNARE. Arabidopsis thaliana VAMP727 is an R-SNARE, with homologs only in seed plants. We have found that VAMP727 colocalizes with SYP22/ VAM3, a Q-SNARE, on a subpopulation of prevacuolar compartments/endosomes closely associated with the vacuolar membrane. Genetic and biochemical analyses, including examination of a synergistic interaction of vamp727 and syp22 mutations, histological examination of protein localization, and coimmunoprecipitation from Arabidopsis lysates indicate that VAMP727 forms a complex with SYP22, VTI11, and SYP51 and that this complex plays a crucial role in vacuolar transport, seed maturation, and vacuole biogenesis. We suggest that the VAMP727 complex mediates the membrane fusion between the prevacuolar compartment and the vacuole and that this process has evolved as an essential step for seed development.
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