OPEN ACCESS ARTICLE

This Article Free via Open Access: OA OA Full Text Full Text (PDF) Supplemental Data OA All Versions of this Article: 18/12/3535    most recent tpc.106.046151v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Web of Science (6) Citing Articles via Google Scholar Google Scholar Articles by Li, L. Articles by Hara-Nishimura, I. Search for Related Content PubMed PubMed Citation Articles by Li, L. Articles by Hara-Nishimura, I. Agricola Articles by Li, L. Articles by Hara-Nishimura, I.

MAIGO2 Is Involved in Exit of Seed Storage Proteins from the Endoplasmic Reticulum in Arabidopsis thaliana^[W],[OA]

^a Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
^b Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma 630-0101, Japan
^c Department of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan

¹ To whom correspondence should be addressed. E-mail ihnishi{at}gr.bot.kyoto-u.ac.jp; fax 81-75-753-4142.

Seed storage proteins are synthesized on the endoplasmic reticulum (ER) as precursors and then transported to protein storage vacuoles, where they are processed into mature forms. Here, we isolated an Arabidopsis thaliana mutant, maigo2 (mag2), that accumulated the precursors of two major storage proteins, 2S albumin and 12S globulin, in dry seeds. mag2 seed cells contained many novel structures, with an electron-dense core that was composed of the precursor forms of 2S albumin. 12S globulins were segregated from 2S albumin and were localized in the matrix region of the structures together with the ER chaperones lumenal binding protein and protein disulfide isomerase, which were more abundant in mag2 seeds. The MAG2 gene was identified as At3g47700, and the MAG2 protein had a RINT-1/TIP20 domain in the C-terminal region. We found that some MAG2 molecules were peripherally associated with the ER membrane. MAG2 had an ability to bind to two ER-localized t-SNAREs (for target-soluble NSF [N-ethylmaleimide–sensitive fusion protein] attachment protein receptor; At Sec20 and At Ufe1). Our findings suggest that MAG2 functions in the transport of storage protein precursors between the ER and Golgi complex in plants.

This article has been cited by other articles:

				R. T. Nakano, R. Matsushima, H. Ueda, K. Tamura, T. Shimada, L. Li, Y. Hayashi, M. Kondo, M. Nishimura, and I. Hara-Nishimura GNOM-LIKE1/ERMO1 and SEC24a/ERMO2 Are Required for Maintenance of Endoplasmic Reticulum Morphology in Arabidopsis thaliana PLANT CELL, November 1, 2009; 21(11): 3672 - 3685. [Abstract] [Full Text] [PDF]

				R. J. Perry, F. D. Mast, and R. A. Rachubinski Endoplasmic Reticulum-Associated Secretory Proteins Sec20p, Sec39p, and Dsl1p Are Involved in Peroxisome Biogenesis Eukaryot. Cell, June 1, 2009; 8(6): 830 - 843. [Abstract] [Full Text] [PDF]

				K. Ebine, Y. Okatani, T. Uemura, T. Goh, K. Shoda, M. Niihama, M. T. Morita, C. Spitzer, M. S. Otegui, A. Nakano, et al. A SNARE Complex Unique to Seed Plants Is Required for Protein Storage Vacuole Biogenesis and Seed Development of Arabidopsis thaliana PLANT CELL, November 1, 2008; 20(11): 3006 - 3021. [Abstract] [Full Text] [PDF]

				C. Andeme Ondzighi, D. A. Christopher, E. J. Cho, S.-C. Chang, and L. A. Staehelin Arabidopsis Protein Disulfide Isomerase-5 Inhibits Cysteine Proteases during Trafficking to Vacuoles before Programmed Cell Death of the Endothelium in Developing Seeds PLANT CELL, August 1, 2008; 20(8): 2205 - 2220. [Abstract] [Full Text] [PDF]

				E. Rojo and J. Denecke What Is Moving in the Secretory Pathway of Plants? Plant Physiology, August 1, 2008; 147(4): 1493 - 1503. [Full Text] [PDF]

				M. Yamazaki, T. Shimada, H. Takahashi, K. Tamura, M. Kondo, M. Nishimura, and I. Hara-Nishimura Arabidopsis VPS35, a Retromer Component, is Required for Vacuolar Protein Sorting and Involved in Plant Growth and Leaf Senescence Plant Cell Physiol., February 1, 2008; 49(2): 142 - 156. [Abstract] [Full Text] [PDF]

				P. R. Hunter, C. P. Craddock, S. Di Benedetto, L. M. Roberts, and L. Frigerio Fluorescent Reporter Proteins for the Tonoplast and the Vacuolar Lumen Identify a Single Vacuolar Compartment in Arabidopsis Cells Plant Physiology, December 1, 2007; 145(4): 1371 - 1382. [Abstract] [Full Text] [PDF]

				E. J. Sohn, M. Rojas-Pierce, S. Pan, C. Carter, A. Serrano-Mislata, F. Madueno, E. Rojo, M. Surpin, and N. V. Raikhel The shoot meristem identity gene TFL1 is involved in flower development and trafficking to the protein storage vacuole PNAS, November 20, 2007; 104(47): 18801 - 18806. [Abstract] [Full Text] [PDF]

				K. Fuji, T. Shimada, H. Takahashi, K. Tamura, Y. Koumoto, S. Utsumi, K. Nishizawa, N. Maruyama, and I. Hara-Nishimura Arabidopsis Vacuolar Sorting Mutants (green fluorescent seed) Can Be Identified Efficiently by Secretion of Vacuole-Targeted Green Fluorescent Protein in Their Seeds PLANT CELL, February 1, 2007; 19(2): 597 - 609. [Abstract] [Full Text] [PDF]