ArticlePlant molecular biology2012
Unraveling the function of Arabidopsis thaliana OS9 in the endoplasmic reticulum-associated degradation of glycoproteins.
Article in Plant molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 88 citations in OpenAlex.
- The Hrd1-Mediated ERAD Pathway in Plants: Conserved Principles and Plant-Specific Innovations.International journal of molecular sciences · 2026Review
- The endoplasmic reticulum-associated degradation machinery selectively degrades stress-induced TIN1 during stress recovery.Plant physiology · 2025Article
- Elucidation of the late steps in the glycan-dependent ERAD of soluble misfolded glycoproteins.The Plant journal : for cell and molecular biology · 2025Article
- Heterologous expression of influenza haemagglutinin leads to early and transient activation of the unfolded protein response in Nicotiana benthamiana.Plant biotechnology journal · 2024Article
- Article
- Analysis of Protein Glycosylation in the ER.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Mechanisms of Endoplasmic Reticulum Protein Homeostasis in Plants.International journal of molecular sciences · 2023Review
- Genetic dissection of maize (Zea maysL.) trace element traits using genome-wide association studies.BMC plant biology · 2023Article
- Parallel evolution of two AIM24 protein subfamilies and their conserved functions in ER stress tolerance in land plants.Plant communications · 2023Article
- MeJA-mediated enhancement of salt-tolerance of Populus wutunensis by 5-aminolevulinic acid.BMC plant biology · 2023Article
- Molecular Mechanisms of Plant Responses to Salt Stress.Frontiers in plant science · 2022Review
- A Non-redundant Function of MNS5: A Class I α-1, 2 Mannosidase, in the Regulation of Endoplasmic Reticulum-Associated Degradation of Misfolded Glycoproteins.Frontiers in plant science · 2022Article
- Prolyl Hydroxylase Paralogs inFrontiers in plant science · 2021Article
- The Endoplasmic Reticulum Role in the Plant Response to Abiotic Stress.Frontiers in plant science · 2021Review
- Cracking the "Sugar Code": A Snapshot ofFrontiers in plant science · 2021Review
- Quantitative Proteomic Analysis of ER Stress Response Reveals both Common and Specific Features in Two Contrasting Ecotypes ofInternational journal of molecular sciences · 2020Article
- The Crucial Role of Demannosylating Asparagine-Linked Glycans in ERADicating Misfolded Glycoproteins in the Endoplasmic Reticulum.Frontiers in plant science · 2020Review
- Salt stress induces endoplasmic reticulum stress-responsive genes in a grapevine rootstock.PloS one · 2020Article
- Important roles of C-terminal residues in degradation of capsid protein of classical swine fever virus.Virology journal · 2019Article
- PAWH1 and PAWH2 are plant-specific components of an Arabidopsis endoplasmic reticulum-associated degradation complex.Nature communications · 2019Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
In the endoplasmic reticulum, immature polypeptides coincide with terminally misfolded proteins. Consequently, cells need a well-balanced quality control system, which decides about the fate of individual proteins and maintains protein homeostasis. Misfolded and unassembled proteins are sent for destruction via the endoplasmic reticulum-associated degradation (ERAD) machinery to prevent the accumulation of potentially toxic protein aggregates. Here, we report the identification of Arabidopsis thaliana OS9 as a component of the plant ERAD pathway. OS9 is an ER-resident glycoprotein containing a mannose-6-phosphate receptor homology domain, which is also found in yeast and mammalian lectins involved in ERAD. OS9 fused to the C-terminal domain of YOS9 can complement the ERAD defect of the corresponding yeast Δyos9 mutant. An A. thaliana OS9 loss-of-function line suppresses the severe growth phenotype of the bri1-5 and bri1-9 mutant plants, which harbour mutated forms of the brassinosteroid receptor BRI1. Co-immunoprecipitation studies demonstrated that OS9 associates with Arabidopsis SEL1L/HRD3, which is part of the plant ERAD complex and with the ERAD substrates BRI1-5 and BRI1-9, but only the binding to BRI1-5 occurs in a glycan-dependent way. OS9-deficiency results in activation of the unfolded protein response and reduces salt tolerance, highlighting the role of OS9 during ER stress. We propose that OS9 is a component of the plant ERAD machinery and may act specifically in the glycoprotein degradation pathway.
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