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First published online October 21, 2005; 10.1104/pp.105.067447 Plant Physiology 139:1244-1254 (2005) © 2005 American Society of Plant Biologists Sec22 and Memb11 Are v-SNAREs of the Anterograde Endoplasmic Reticulum-Golgi Pathway in Tobacco Leaf Epidermal Cells1Laboratoire de Biogenèse Membranaire, Unité Mixte de Recherche 5200, Centre National de la Recherche Scientifique-Université Bordeaux 2, 33076 Bordeaux, France (L.C., A.H., P.M.); Department of Biology, University of Saskatchewan, Saskatoon, SK S7N 5E2, Canada (F.B.); Ecole Supèrieure de Technologie des Biomolécules de Bordeaux, Université Bordeaux 2, 33076 Bordeaux, France (A.H.); and Research School of Biological and Molecular Sciences, Oxford Brookes University, Oxford OX3 0BP, United Kingdom (C.H.)
Distinct sets of soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptors (SNAREs) are distributed to specific intracellular compartments and catalyze membrane fusion events. Although the central role of these proteins in membrane fusion is established in nonplant systems, little is known about their role in the early secretory pathway of plant cells. Analysis of the Arabidopsis (Arabidopsis thaliana) genome reveals 54 genes encoding SNARE proteins, some of which are expected to be key regulators of membrane trafficking between the endoplasmic reticulum (ER) and the Golgi. To gain insights on the role of SNAREs of the early secretory pathway in plant cells, we have cloned the Arabidopsis v-SNAREs Sec22, Memb11, Bet11, and the t-SNARE Sed5, and analyzed their distribution in plant cells in vivo. By means of live cell imaging, we have determined that these SNAREs localize at the Golgi apparatus. In addition, Sec22 was also distributed at the ER. We have then focused on understanding the function of Sec22 and Memb11 in comparison to the other SNAREs. Overexpression of the v-SNAREs Sec22 and Memb11 but not of the other SNAREs induced collapse of Golgi membrane proteins into the ER, and the secretion of a soluble secretory marker was abrogated by all SNAREs. Our studies suggest that Sec22 and Memb11 are involved in anterograde protein trafficking at the ER-Golgi interface.
1 This work was supported by the Centre National de la Recherche Scientifique and the University Victor Segalen Bordeaux 2. P.M. and C.H. were the recipients of a Franco-British Research Partnership Program Alliance (Egide/British Council). The authors responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) are: Patrick Moreau (pmoreau{at}biomemb.u-bordeaux2.fr) and Chris Hawes (chawes{at}brookes.ac.uk). Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.105.067447. * Corresponding author; e-mail pmoreau{at}biomemb.u-bordeaux2.fr; fax 33556518361. Received June 19, 2005; returned for revision September 21, 2005; accepted September 21, 2005. This article has been cited by other articles:
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