ArticleScientific reports2014
A design principle underlying the paradoxical roles of E3 ubiquitin ligases.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 10 citations in OpenAlex.
- Investigating the underlying mechanism of Saccharomyces cerevisiae in response to ethanol stress employing RNA-seq analysis.World journal of microbiology & biotechnology · 2017Article
- Identification of Unintuitive Features of Sumoylation through Mathematical Modeling.The Journal of biological chemistry · 2016Article
- Cullin-RING ubiquitin ligases in salicylic acid-mediated plant immune signaling.Frontiers in plant science · 2015Review
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
E3 ubiquitin ligases are important cellular components that determine the specificity of proteolysis in the ubiquitin-proteasome system. However, an increasing number of studies have indicated that E3 ubiquitin ligases also participate in transcription. Intrigued by the apparently paradoxical functions of E3 ubiquitin ligases in both proteolysis and transcriptional activation, we investigated the underlying design principles using mathematical modeling. We found that the antagonistic functions integrated in E3 ubiquitin ligases can prevent any undesirable sustained activation of downstream genes when E3 ubiquitin ligases are destabilized by unexpected perturbations. Interestingly, this design principle of the system is similar to the operational principle of a safety interlock device in engineering systems, which prevents a system from abnormal operation unless stability is guaranteed.
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