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Plant Cell Advance Online Publication
Published on November 30, 2006; 10.1105/tpc.105.036400

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Received July 21, 2005
Returned for revision August 31, 2006
Accepted November 2, 2006

Plant N-Glycan Processing Enzymes Employ Different Targeting Mechanisms for Their Spatial Arrangement along the Secretory Pathway

Claude Saint-Jore-Dupas 1, Andreas Nebenführ 2, Aurélia Boulaflous 1, Marie-Laure Follet-Gueye 1, Carole Plasson 1, Chris Hawes 3, Azeddine Driouich 1, Loïc Faye 1, and Véronique Gomord 1*

1 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
2 Department of Biochemistry, Cellular, and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996-0840
3 School of Biological and Molecular Sciences, Oxford Brookes University, Oxford OX3 0BP, United Kingdom

* To whom correspondence should be addressed. E-mail: vgomord{at}crihan.fr.

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), {alpha}-1,2 mannosidase I (ManI) and N-acetylglucosaminyltransferase I (GNTI) both targeted to the ER and Golgi, and {beta}-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.






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