ArticleThe EMBO journal1998
Modulation of the intracellular stability and toxicity of diphtheria toxin through degradation by the N-end rule pathway.
Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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Who cites it
13 citing papers in PubMed, 36 citations in OpenAlex.
- Cellular recovery from exposure to sub-optimal concentrations of AB toxins that inhibit protein synthesis.Scientific reports · 2018Article
- Article
- A d-Amino Acid at the N-Terminus of a Protein Abrogates Its Degradation by the N-End Rule Pathway.ACS central science · 2015Article
- Review
- Article
- The N-end rule pathway and regulation by proteolysis.Protein science : a publication of the Protein Society · 2011Review
- Toxin-based therapeutic approaches.Toxins · 2010Review
- Sensitivity of cancer cells to truncated diphtheria toxin.PloS one · 2010Article
- Processing of Pseudomonas aeruginosa exotoxin A is dispensable for cell intoxication.Infection and immunity · 2009Article
- Article
- Designing immunotoxins for cancer therapy.Immunologic research · 2002Review
- Diphtheria toxin fused to human interleukin-3 is toxic to blasts from patients with myeloid leukemias.Leukemia · 2000Article
- Toxins that are activated by HIV type-1 protease through removal of a signal for degradation by the N-end-rule pathway.The Biochemical journal · 1999Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The enzymatically active A-fragment of diphtheria toxin enters the cytosol of sensitive cells where it inhibits protein synthesis by inactivating elongation factor 2 (EF-2). We have constructed a number of diphtheria toxin mutants that are degraded by the N-end rule pathway in Vero cells, and that display a wide range of intracellular stabilities. The degradation could be inhibited by the proteasome inhibitor lactacystin, indicating that the proteasome is responsible for N-end rule-mediated degradation in mammalian cells. Previously, the N-end rule has been investigated by studying the co-translational degradation of intracellularly expressed beta-galactosidase. Our work shows that a mature protein entering the cytosol from the exterior can also be degraded by the N-end rule pathway with a similar, but not identical specificity to that previously found. We found a correlation between the intracellular stability of the mutants and their toxic effect on cells, thus demonstrating a novel manner of modulating the toxicity of a protein toxin. The data also indicate that the inactivation of EF-2 is the rate-limiting step in the intoxication process.
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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.