Journal Article

Fusion with HDEL Protects Cell Wall Invertase from Early Degradation when <i>N</i>-glycosylation is Inhibited

Sophie Pagny, Lise-Anne Denmat-Ouisse, Véronique Gomord and Loïc Faye

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 44, issue 2, pages 173-182
Published in print February 2003 | ISSN: 0032-0781
Published online February 2003 | e-ISSN: 1471-9053 | DOI:
Fusion with HDEL Protects Cell Wall Invertase from Early Degradation when N-glycosylation is Inhibited

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  • Biochemistry
  • Molecular and Cell Biology
  • Plant Sciences and Forestry


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Previous data obtained in different suspension-cultured plant cells have clearly illustrated that N-glycans are absolutely required for transport of glycoproteins to the extracellular compartment, regardless of their oligosaccharide structure [see Lerouge et al. (1998) Plant Mol. Biol. 38: 31 for review]. In the present study the role of N-glycosylation in the transport of glycoproteins to the cell surface was studied in BY2 tobacco cells using both endogenous and recombinant cell wall invertases as markers. When synthesized without their N-glycans, both invertases were very rapidly degraded. This degradation did not occur in an acidic compartment and was brefeldin A-insensitive. Therefore, it most probably represents a pre-Golgi event. However, the low efficiency of specific inhibitors did not favor a strong contribution of proteasomes in this proteolysis. In contrast, addition of a C-terminal His-Asp-Glu-Leu (HDEL) extension prevented arrival of these non-glycosylated glycoproteins in the compartment where they are degraded. These results argue for the presence of an endoplasmic reticulum (ER) domain specialized in protein degradation. Consistent with our results and the well-known stabilization of recombinant proteins retained in the ER, the addition of an ER retention signal to a protein would prevent its targeting to an ER domain devoted to degradation.

Keywords: Keywords: BY2 tobacco cells — N-glycosylation — Protein degradation — Protein transport — Secretory pathway.; Abbreviations: CBZ, carboxybenzyl Leu Leu leucinal; BFA, brefeldin A; BY2, bright yellow 2; ER, endoplasmic reticulum; LLnL, acetyl Leu Leu norleucinal; PHA, phytohemagglutinin.

Journal Article.  8508 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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