ArticleTraffic (Copenhagen, Denmark)2012
N-glycosylation does not affect the catalytic activity of ricin a chain but stimulates cytotoxicity by promoting its transport out of the endoplasmic reticulum.
Article in Traffic (Copenhagen, Denmark), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 26 citations in OpenAlex.
- Biophysical and Biochemical Assays for Screening Small Molecule Inhibitors Targeting Toxin-Ribosome Interactions.Toxins · 2026Review
- Development of an InnovativeToxins · 2026Article
- Ricin as a Biothreat Agent: From Molecular Mechanisms to Clinical Toxicology, Forensic Aspects, and Risk Mitigation.BioMed research international · 2026Review
- Article
- Article
- Ribosome depurination by ricin leads to inhibition of endoplasmic reticulum stress-inducedThe Journal of biological chemistry · 2019Article
- Review
- Toxins Utilize the Endoplasmic Reticulum-Associated Protein Degradation Pathway in Their Intoxication Process.International journal of molecular sciences · 2019Review
- Functional Assays for Measuring the Catalytic Activity of Ribosome Inactivating Proteins.Toxins · 2018Review
- Conserved Arginines at the P-Protein Stalk Binding Site and the Active Site Are Critical for Ribosome Interactions of Shiga Toxins but Do Not Contribute to Differences in the Affinity of the A1 Subunits for the Ribosome.Infection and immunity · 2016Article
- Article
- Ricin trafficking in cells.Toxins · 2015Review
- Enhanced expression of heterologous proteins in yeast cells via the modification of N-glycosylation sites.Bioengineered · 2015Article
- Functional divergence between the two P1-P2 stalk dimers on the ribosome in their interaction with ricin A chain.The Biochemical journal · 2014Article
- Article
- Article
- Toxin instability and its role in toxin translocation from the endoplasmic reticulum to the cytosol.Biomolecules · 2013Article
- Arginine residues on the opposite side of the active site stimulate the catalysis of ribosome depurination by ricin A chain by interacting with the P-protein stalk.The Journal of biological chemistry · 2013Article
- Targeting ricin to the ribosome.Toxicon : official journal of the International Society on Toxinology · 2013Review
- A relatively low level of ribosome depurination by mutant forms of ricin toxin A chain can trigger protein synthesis inhibition, cell signaling and apoptosis in mammalian cells.The international journal of biochemistry & cell biology · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Ricin A chain (RTA) depurinates the α-sarcin/ricin loop after it undergoes retrograde trafficking to the cytosol. The structural features of RTA involved in intracellular transport are not known. To explore this, we fused enhanced green fluorescent protein (EGFP) to precursor (preRTA-EGFP), containing a 35-residue leader, and mature RTA (matRTA-EGFP). Both were enzymatically active and toxic in Saccharomyces cerevisiae. PreRTA-EGFP was localized in the endoplasmic reticulum (ER) initially and was subsequently transported to the vacuole, whereas matRTA-EGFP remained in the cytosol, indicating that ER localization is a prerequisite for vacuole transport. When the two glycosylation sites in RTA were mutated, the mature form was fully active and toxic, suggesting that the mutations do not affect catalytic activity. However, nonglycosylated preRTA-EGFP had reduced toxicity, depurination and delayed vacuole transport, indicating that N-glycosylation affects transport of RTA out of the ER. Point mutations in the C-terminal hydrophobic region restricted RTA to the ER and eliminated toxicity and depurination, indicating that this sequence is critical for ER exit. These results demonstrate that N-glycosylation and the C-terminal hydrophobic region stimulate the toxicity of RTA by promoting ER export. The timing of depurination coincided with the timing of vacuole transport, suggesting that RTA may enter the cytosol during vacuole transport.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.