Unraveling the function of Arabidopsis thaliana OS9 in the endoplasmic reticulum-associated degradation of glycoproteins
| Autor: | Jennifer Schoberer, Josephine Grass, Richard Strasser, Christiane Veit, Silvia Hüttner |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
0106 biological sciences
Mutant Arabidopsis Plant Science Protein aggregation Sodium Chloride Endoplasmic Reticulum 01 natural sciences Unfolded protein response Protein glycosylation chemistry.chemical_classification 0303 health sciences Membrane Glycoproteins Life Sciences General Medicine Endoplasmic Reticulum-Associated Degradation Cell biology Phenotype Biochemistry ER stress Protein Binding Recombinant Fusion Proteins Green Fluorescent Proteins Molecular Sequence Data macromolecular substances Saccharomyces cerevisiae Endoplasmic-reticulum-associated protein degradation Biology Article 03 medical and health sciences Polysaccharides Stress Physiological Genetics ERAD pathway Amino Acid Sequence 030304 developmental biology Glycoproteins Arabidopsis Proteins Endoplasmic reticulum fungi Plant Sciences ERAD Plant Pathology biology.organism_classification Protein quality control Protein Structure Tertiary Biochemistry general chemistry Mutation Posttranslational modification Glycoprotein Agronomy and Crop Science 010606 plant biology & botany |
| Zdroj: | Plant Molecular Biology |
| ISSN: | 1573-5028 0167-4412 |
| Popis: | 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. Electronic supplementary material The online version of this article (doi:10.1007/s11103-012-9891-4) contains supplementary material, which is available to authorized users. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink