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Plant and Cell Physiology Advance Access originally published online on August 22, 2006
Plant and Cell Physiology 2006 47(9):1187-1194; doi:10.1093/pcp/pcj103
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© The Author 2006. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Rapid Paper

AtVPS29, a Putative Component of a Retromer Complex, is Required for the Efficient Sorting of Seed Storage Proteins

Tomoo Shimada1, Yasuko Koumoto1, Lixin Li1, Misako Yamazaki1, Maki Kondo2, Mikio Nishimura2 and Ikuko Hara-Nishimura1,*

1 Graduate School of Science, Kyoto University, Kyoto, 606-8502 Japan
2 Department of Cell Biology, National Institute for Basic Biology, Okazaki, 444-8585 Japan

* Corresponding author: E-mail, ihnishi{at}gr.bot.kyoto-u.ac.jp; Fax, +81-75-753-4142.

Seed storage proteins are synthesized on rough endoplasmic reticulum (ER) as larger precursors and are sorted to protein storage vacuoles, where they are converted into the mature forms. We report here an Arabidopsis mutant, maigo 1 (mag1), which abnormally accumulates the precursors of two major storage proteins, 12S globulin and 2S albumin, in dry seeds. Electron microscopy revealed that mag1 seeds mis-sort storage proteins by secreting them from cells. mag1 seeds have smaller protein storage vacuoles in the seeds than do wild-type seeds. The MAG1 gene encodes a homolog of the yeast (Saccharomyces cerevisiae) protein VPS29. VPS29 is a component of a retromer complex for recycling a vacuolar sorting receptor VPS10 from the pre-vacuolar compartment to the Golgi complex. Our findings suggest that MAG1/AtVPS29 protein is involved in recycling a plant receptor for the efficient sorting of seed storage proteins. The mag1 mutant exhibits a dwarf phenotype. A plant retromer complex plays a significant role in plant growth and development.

(Received July 23, 2006; Accepted August 10, 2006)
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