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Plant Cell, Vol. 12, 739-756, May 2000, Copyright © 2000, American Society of Plant Physiologists

Protein Recycling from the Golgi Apparatus to the Endoplasmic Reticulum in Plants and Its Minor Contribution to Calreticulin Retention

Sophie Pagnya, Marion Cabanes-Macheteaua, Jeffrey W. Gillikinb, Nathalie Leborgne-Castela, Patrice Lerougea, Rebecca S. Bostonb, Loïc Fayea, and Véronique Gomorda
a Laboratoire des Transports Intracellulaires, CNRS-ESA 6037, IFRMP23, Université de Rouen, 76821 Mont St. Aignan Cedex, France
b Department of Botany, North Carolina State University, Raleigh, North Carolina 27695-7612

Correspondence to: Véronique Gomord, vgomord{at}crihan.fr (E-mail), 33-02-35-146787 (fax)

Using pulse–chase experiments combined with immunoprecipitation and N-glycan structural analysis, we showed that the retrieval mechanism of proteins from post–endoplasmic reticulum (post-ER) compartments is active in plant cells at levels similar to those described previously for animal cells. For instance, recycling from the Golgi apparatus back to the ER is sufficient to block the secretion of as much as 90% of an extracellular protein such as the cell wall invertase fused with an HDEL C-terminal tetrapeptide. Likewise, recycling can sustain fast retrograde transport of Golgi enzymes into the ER in the presence of brefeldin A. However, on the basis of our data, we propose that this retrieval mechanism in plants has little impact on the ER retention of a soluble ER protein such as calreticulin. Indeed, the latter is retained in the ER without any N-glycan–related evidence for a recycling through the Golgi apparatus. Taken together, these results indicate that calreticulin and perhaps other plant reticuloplasmins are possibly largely excluded from vesicles exported from the ER. Instead, they are probably retained in the ER by mechanisms that rely primarily on signals other than H/KDEL motifs.




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