ArticlePlant physiology2005
Endoplasmic reticulum-associated degradation of ricin A chain has unique and plant-specific features.
Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 51 citations in OpenAlex.
- The Hrd1-Mediated ERAD Pathway in Plants: Conserved Principles and Plant-Specific Innovations.International journal of molecular sciences · 2026Review
- Elucidation of the late steps in the glycan-dependent ERAD of soluble misfolded glycoproteins.The Plant journal : for cell and molecular biology · 2025Article
- The Crucial Role of Demannosylating Asparagine-Linked Glycans in ERADicating Misfolded Glycoproteins in the Endoplasmic Reticulum.Frontiers in plant science · 2020Review
- Review
- Plant Serine Protease Inhibitors: Biotechnology Application in Agriculture and Molecular Farming.International journal of molecular sciences · 2019Review
- Toxins Utilize the Endoplasmic Reticulum-Associated Protein Degradation Pathway in Their Intoxication Process.International journal of molecular sciences · 2019Review
- A context-independent N-glycan signal targets the misfolded extracellular domain of Arabidopsis STRUBBELIG to endoplasmic-reticulum-associated degradation.The Biochemical journal · 2014Article
- Endoplasmic reticulum-mediated protein quality control in Arabidopsis.Frontiers in plant science · 2014Review
- Toxin instability and its role in toxin translocation from the endoplasmic reticulum to the cytosol.Biomolecules · 2013Article
- Endoplasmic reticulum (ER) stress response and its physiological roles in plants.International journal of molecular sciences · 2013Review
- Secretory pathway research: the more experimental systems the better.The Plant cell · 2012Review
- The secreted plant N-glycoproteome and associated secretory pathways.Frontiers in plant science · 2012Article
- Endoplasmic reticulum-associated degradation of glycoproteins in plants.Frontiers in plant science · 2012Article
- Antibody degradation in tobacco plants: a predominantly apoplastic process.BMC biotechnology · 2011Article
- Ricin trafficking in plant and mammalian cells.Toxins · 2011Review
- Dislocation of ricin toxin A chains in human cells utilizes selective cellular factors.The Journal of biological chemistry · 2011Article
- Endoplasmic reticulum protein quality control and its relationship to environmental stress responses in plants.The Plant cell · 2010Review
- Folding-competent and folding-defective forms of ricin A chain have different fates after retrotranslocation from the endoplasmic reticulum.Molecular biology of the cell · 2010Article
- Induction of protein body formation in plant leaves by elastin-like polypeptide fusions.BMC biology · 2009Article
- A pollen protein, NaPCCP, that binds pistil arabinogalactan proteins also binds phosphatidylinositol 3-phosphate and associates with the pollen tube endomembrane system.Plant physiology · 2009Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins that fail to fold in the endoplasmic reticulum (ER) or cannot find a pattern for assembly are often disposed of by a process named ER-associated degradation (ERAD), which involves transport of the substrate protein across the ER membrane (dislocation) followed by rapid proteasome-mediated proteolysis. Different ERAD substrates have been shown to be ubiquitinated during or soon after dislocation, and an active ubiquitination machinery has been found to be required for the dislocation of certain defective proteins. We have previously shown that, when expressed in tobacco (Nicotiana tabacum) protoplasts, the A chain of the heterodimeric toxin ricin is degraded by a pathway that closely resembles ERAD but is characterized by an unusual uncoupling between the dislocation and the degradation steps. Since lysine (Lys) residues are a major target for ubiquitination, we have investigated the effects of changing the Lys content on the retrotranslocation and degradation of ricin A chain in tobacco protoplasts. Here we show that modulating the number of Lys residues does not affect recognition events within the ER lumen nor the transport of the protein from this compartment to the cytosol. Rather, the introduced modifications have a clear impact on the degradation of the dislocated protein. While the substitution of the two Lys residues present in ricin A chain with arginine slowed down degradation, the introduction of four extra lysyl residues had an opposite effect and converted the ricin A chain to a standard ERAD substrate that is disposed via a process in which dislocation and degradation steps are tightly coupled.
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