Tight Regulation of Unstructured Proteins: From Transcript Synthesis to Protein Degradation
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Altered abundance of several intrinsically unstructured proteins (IUPs) has been associated with perturbed cellular signaling that may lead to pathological conditions such as cancer. Therefore, it is important to understand how cells precisely regulate the availability of IUPs. We observed that regulation of transcript clearance, proteolytic degradation, and translational rate contribute to controlling the abundance of IUPs, some of which are present in low amounts and for short periods of time. Abundant phosphorylation and low stochasticity in transcription and translation indicate that the availability of IUPs can be finely tuned. Fidelity in signaling may require that most IUPs be available in appropriate amounts and not present longer than needed.
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Intrinsically disordered proteins are on average twice as likely to be kinase substrates.
“Intrinsically disordered proteins are on average twice more likely to be substrates of kinases, highlighting the importance of post-translational modifications in fine-tuning function.254”
From Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell (2016) · cites this paper as [254]
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Flagged first, then by citations
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- Authors
- Gsponer, J., Futschik, M. E., Teichmann, S. A., & Babu, M. M.
- Affiliations
- Medical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Babu, M. Madan
- Venue
- Science
- Published
- 2008-11-28
- Volume
- 322
- Issue
- 5906
- Pages
- 1365-1368
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC2803065
- OpenAlex
- W2154335467
- Cited by
- 466
- References
- 107
- Citations by year
- 2026: 5 · 2025: 13 · 2024: 14 · 2023: 14 · 2022: 22 · 2021: 30 · 2020: 27 · 2019: 32 · 2018: 30 · 2017: 16 · 2016: 25 · 2015: 19 · 2014: 38 · 2013: 39 · 2012: 45
- FWCI
- 13.29
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, cc-by)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- intrinsically disordered proteins, protein abundance regulation, proteolysis, protein phosphorylation, transcriptional noise, cancer
- MeSH terms
- Amino Acid Sequence, Cell Cycle, Genes, Fungal, Humans, Phosphorylation, Protein Conformation, Protein Kinases, RNA, Fungal, RNA, Messenger, Saccharomyces cerevisiae, Transcription, Genetic, Protein Biosynthesis, Signal Transduction, Computational Biology, Proteome, Saccharomyces cerevisiae Proteins, Schizosaccharomyces pombe Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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