ArticleGenome biology2009
Insights into the regulation of intrinsically disordered proteins in the human proteome by analyzing sequence and gene expression data.
Article in Genome biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 74 citations in OpenAlex.
- <i>Drosophila</i> insulator proteins exhibit in vivo liquid-liquid phase separation properties.Life science alliance · 2022Article
- Intrinsically Disordered Proteins: Critical Components of the Wetware.Chemical reviews · 2022Review
- Intrinsically disordered proteins: Ensembles at the limits of Anfinsen's dogma.Biophysics reviews · 2022Review
- Intrinsically disordered regions in the rodent hepevirus proteome.Bioinformation · 2022Article
- Protein conformational dynamics and phenotypic switching.Biophysical reviews · 2021Review
- Role of "dual-personality" fragments in HEV adaptation-analysis of Y-domain region.Journal, genetic engineering & biotechnology · 2021Article
- Article
- Exploring Potential Signals of Selection for Disordered Residues in Prokaryotic and Eukaryotic Proteins.Genomics, proteomics & bioinformatics · 2020Article
- Presence and structure-activity relationship of intrinsically disordered regions across mucins.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Modulation of Disordered Proteins with a Focus on Neurodegenerative Diseases and Other Pathologies.International journal of molecular sciences · 2019Review
- Molecular model of human tropoelastin and implications of associated mutations.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Intrinsic protein disorder reduces small-scale gene duplicability.DNA research : an international journal for rapid publication of reports on genes and genomes · 2017Article
- Functional constraints on adaptive evolution of protein ubiquitination sites.Scientific reports · 2017Article
- Neurodegeneration and Cancer: Where the Disorder Prevails.Scientific reports · 2015Article
- Content of intrinsic disorder influences the outcome of cell-free protein synthesis.Scientific reports · 2015Article
- Identifying Similar Patterns of Structural Flexibility in Proteins by Disorder Prediction and Dynamic Programming.International journal of molecular sciences · 2015Article
- Classification of intrinsically disordered regions and proteins.Chemical reviews · 2014Review
- Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs).Chemical reviews · 2014Review
- Advantages of proteins being disordered.Protein science : a publication of the Protein Society · 2014Review
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
backgroundDisordered proteins need to be expressed to carry out specified functions; however, their accumulation in the cell can potentially cause major problems through protein misfolding and aggregation. Gene expression levels, mRNA decay rates, microRNA (miRNA) targeting and ubiquitination have critical roles in the degradation and disposal of human proteins and transcripts. Here, we describe a study examining these features to gain insights into the regulation of disordered proteins.
resultsIn comparison with ordered proteins, disordered proteins have a greater proportion of predicted ubiquitination sites. The transcripts encoding disordered proteins also have higher proportions of predicted miRNA target sites and higher mRNA decay rates, both of which are indicative of the observed lower gene expression levels. The results suggest that the disordered proteins and their transcripts are present in the cell at low levels and/or for a short time before being targeted for disposal. Surprisingly, we find that for a significant proportion of highly disordered proteins, all four of these trends are reversed. Predicted estimates for miRNA targets, ubiquitination and mRNA decay rate are low in the highly disordered proteins that are constitutively and/or highly expressed.
conclusionsMechanisms are in place to protect the cell from these potentially dangerous proteins. The evidence suggests that the enrichment of signals for miRNA targeting and ubiquitination may help prevent the accumulation of disordered proteins in the cell. Our data also provide evidence for a mechanism by which a significant proportion of highly disordered proteins (with high expression levels) can escape rapid degradation to allow them to successfully carry out their function.
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