OPEN ACCESS ARTICLE

This Article Free via Open Access: OA OA Full Text Full Text (PDF) Supplemental Data OA All Versions of this Article: 18/11/3182    most recent tpc.105.036400v1 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 (15) Citing Articles via Google Scholar Google Scholar Articles by Saint-Jore-Dupas, C. Articles by Gomord, V. Search for Related Content PubMed PubMed Citation Articles by Saint-Jore-Dupas, C. Articles by Gomord, V. Agricola Articles by Saint-Jore-Dupas, C. Articles by Gomord, V.

Plant N-Glycan Processing Enzymes Employ Different Targeting Mechanisms for Their Spatial Arrangement along the Secretory Pathway^[W],[OA]

^a Centre National de la Recherche Scientifique, Unité Mixte de Recherche 6037, IFRMP 23, GDR 2590, UFR des Sciences, Université de Rouen, 76821 Mont-Saint-Aignan Cedex, France
^b Department of Biochemistry, Cellular, and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996-0840
^c School of Biological and Molecular Sciences, Oxford Brookes University, Oxford OX3 0BP, United Kingdom

¹ To whom correspondence should be addressed. E-mail vgomord{at}crihan.fr; fax 33-2-35-14-67-87.

The processing of N-linked oligosaccharides in the secretory pathway requires the sequential action of a number of glycosidases and glycosyltransferases. We studied the spatial distribution of several type II membrane-bound enzymes from Glycine max, Arabidopsis thaliana, and Nicotiana tabacum. Glucosidase I (GCSI) localized to the endoplasmic reticulum (ER), -1,2 mannosidase I (ManI) and N-acetylglucosaminyltransferase I (GNTI) both targeted to the ER and Golgi, and ß-1,2 xylosyltransferase localized exclusively to Golgi stacks, corresponding to the order of expected function. ManI deletion constructs revealed that the ManI transmembrane domain (TMD) contains all necessary targeting information. Likewise, GNTI truncations showed that this could apply to other type II enzymes. A green fluorescent protein chimera with ManI TMD, lengthened by duplicating its last seven amino acids, localized exclusively to the Golgi and colocalized with a trans-Golgi marker (ST52-mRFP), suggesting roles for protein–lipid interactions in ManI targeting. However, the TMD lengths of other plant glycosylation enzymes indicate that this mechanism cannot apply to all enzymes in the pathway. In fact, removal of the first 11 amino acids of the GCSI cytoplasmic tail resulted in relocalization from the ER to the Golgi, suggesting a targeting mechanism relying on protein–protein interactions. We conclude that the localization of N-glycan processing enzymes corresponds to an assembly line in the early secretory pathway and depends on both TMD length and signals in the cytoplasmic tail.

This article has been cited by other articles:

				H. Kajiura, H. Koiwa, Y. Nakazawa, A. Okazawa, A. Kobayashi, T. Seki, and K. Fujiyama Two Arabidopsis thaliana Golgi {alpha}-mannosidase I enzymes are responsible for plant N-glycan maturation Glycobiology, February 1, 2010; 20(2): 235 - 247. [Abstract] [Full Text] [PDF]

				E. Liebminger, S. Huttner, U. Vavra, R. Fischl, J. Schoberer, J. Grass, C. Blaukopf, G. J. Seifert, F. Altmann, L. Mach, et al. Class I {alpha}-Mannosidases Are Required for N-Glycan Processing and Root Development in Arabidopsis thaliana PLANT CELL, December 1, 2009; 21(12): 3850 - 3867. [Abstract] [Full Text] [PDF]

				C. Faso, Y.-N. Chen, K. Tamura, M. Held, S. Zemelis, L. Marti, R. Saravanan, E. Hummel, L. Kung, E. Miller, et al. A Missense Mutation in the Arabidopsis COPII Coat Protein Sec24A Induces the Formation of Clusters of the Endoplasmic Reticulum and Golgi Apparatus PLANT CELL, November 1, 2009; 21(11): 3655 - 3671. [Abstract] [Full Text] [PDF]

				S. Cotton, R. Grangeon, K. Thivierge, I. Mathieu, C. Ide, T. Wei, A. Wang, and J.-F. Laliberte Turnip Mosaic Virus RNA Replication Complex Vesicles Are Mobile, Align with Microfilaments, and Are Each Derived from a Single Viral Genome J. Virol., October 15, 2009; 83(20): 10460 - 10471. [Abstract] [Full Text] [PDF]

				Y. Kong, G. Zhou, U. Avci, X. Gu, C. Jones, Y. Yin, Y. Xu, and M. G. Hahn Two Poplar Glycosyltransferase Genes, PdGATL1.1 and PdGATL1.2, Are Functional Orthologs to PARVUS/AtGATL1 in Arabidopsis Mol Plant, September 1, 2009; 2(5): 1040 - 1050. [Abstract] [Full Text] [PDF]

				L. Chatre, V. Wattelet-Boyer, S. Melser, L. Maneta-Peyret, F. Brandizzi, and P. Moreau A novel di-acidic motif facilitates ER export of the syntaxin SYP31 J. Exp. Bot., July 1, 2009; 60(11): 3157 - 3165. [Abstract] [Full Text] [PDF]

				D. Avisar, M. Abu-Abied, E. Belausov, E. Sadot, C. Hawes, and I. A. Sparkes A Comparative Study of the Involvement of 17 Arabidopsis Myosin Family Members on the Motility of Golgi and Other Organelles Plant Physiology, June 1, 2009; 150(2): 700 - 709. [Abstract] [Full Text] [PDF]

				A. D. J. van Dijk, D. Bosch, C. J. F. ter Braak, A. R. van der Krol, and R. C. H. J. van Ham Predicting sub-Golgi localization of type II membrane proteins Bioinformatics, August 15, 2008; 24(16): 1779 - 1786. [Abstract] [Full Text] [PDF]

				L. A. Staehelin and B.-H. Kang Nanoscale Architecture of Endoplasmic Reticulum Export Sites and of Golgi Membranes as Determined by Electron Tomography Plant Physiology, August 1, 2008; 147(4): 1454 - 1468. [Full Text] [PDF]

				M. A. Held, A. Boulaflous, and F. Brandizzi Advances in Fluorescent Protein-Based Imaging for the Analysis of Plant Endomembranes Plant Physiology, August 1, 2008; 147(4): 1469 - 1481. [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]

				C. L. Alvim Kamei, J. Boruc, K. Vandepoele, H. Van den Daele, S. Maes, E. Russinova, D. Inze, and L. De Veylder The PRA1 Gene Family in Arabidopsis Plant Physiology, August 1, 2008; 147(4): 1735 - 1749. [Abstract] [Full Text] [PDF]

				P. Abbal, M. Pradal, L. Muniz, F.-X. Sauvage, P. Chatelet, T. Ueda, and C. Tesniere Molecular characterization and expression analysis of the Rab GTPase family in Vitis vinifera reveal the specific expression of a VvRabA protein J. Exp. Bot., June 1, 2008; 59(9): 2403 - 2416. [Abstract] [Full Text] [PDF]

				A. Marmagne, M. Vinauger-Douard, D. Monachello, A. F. de Longevialle, C. Charon, M. Allot, F. Rappaport, F.-A. Wollman, H. Barbier-Brygoo, and G. Ephritikhine Two members of the Arabidopsis CLC (chloride channel) family, AtCLCe and AtCLCf, are associated with thylakoid and Golgi membranes, respectively J. Exp. Bot., September 14, 2007; (2007) erm187v1. [Abstract] [Full Text] [PDF]

				R. Strasser, J. S. Bondili, U. Vavra, J. Schoberer, B. Svoboda, J. Glossl, R. Leonard, J. Stadlmann, F. Altmann, H. Steinkellner, et al. A Unique {beta}1,3-Galactosyltransferase Is Indispensable for the Biosynthesis of N-Glycans Containing Lewis a Structures in Arabidopsis thaliana PLANT CELL, July 1, 2007; 19(7): 2278 - 2292. [Abstract] [Full Text] [PDF]