A plant receptor domain with functional analogies to animal malectin disables ER stress responses upon infection

Malectins from the oligosaccharyltransferase (OST) complex in the endoplasmic reticulum (ER) of animal cells are involved in ER quality control and contribute to the Unfolded Protein Response (UPR). Malectins are not found in plant cells, but malectin-like domains (MLDs) are constituents of many mem...

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Published iniScience Vol. 25; no. 3; p. 103877
Main Authors Giordano, Laïla, Allasia, Valérie, Cremades, Alexandra, Hok, Sophie, Panabières, Franck, Bailly-Maître, Béatrice, Keller, Harald
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 18.03.2022
Elsevier
Subjects
Environmental Sciences
Molecular biology
Plant biology
Plant pathology
Plant biology
Molecular biology
Plant pathology
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Summary:Malectins from the oligosaccharyltransferase (OST) complex in the endoplasmic reticulum (ER) of animal cells are involved in ER quality control and contribute to the Unfolded Protein Response (UPR). Malectins are not found in plant cells, but malectin-like domains (MLDs) are constituents of many membrane-bound receptors. In Arabidopsis thaliana, the MLD-containing receptor IOS1 promotes successful infection by filamentous plant pathogens. We show that the MLD of its exodomain retains IOS1 in the ER of plant cells and attenuates the infection-induced UPR. Expression of the MLD in the ios1-1 knockout background is sufficient to complement infection-related phenotypes of the mutant, such as increased UPR and reduced disease susceptibility. IOS1 interacts with the ER membrane-associated ribophorin HAP6 from the OST complex, and hap6 mutants show decreased pathogen-responsive UPR and increased disease susceptibility. Altogether, this study revealed a previously uncharacterized role of a plant receptor domain in the regulation of ER stress during infection. [Display omitted] •The Unfolded Protein Response (UPR) in plants impairs downy mildew infection•The pathogen exploits a molecular mechanism of the host cell to promote disease•The extracellular domain of the receptor IOS1 attenuates the pathogen-induced UPR•IOS1 interacts with the ribophorin HAP6 in the ER to fine-tune the UPR Molecular biology; Plant biology; Plant pathology
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ISSN:2589-0042
2589-0042
DOI:10.1016/j.isci.2022.103877