ArticleBiophysical journal2017
Phosphorylation-Induced Mechanical Regulation of Intrinsically Disordered Neurofilament Proteins.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Neurofilament Light Disordered Tail Mutations Reshape Its Self-Assembled Network Structure.Journal of the American Chemical Society · 2026Article
- Phosphorylation of disordered proteins tunes local and global intramolecular interactions.Biophysical journal · 2024Article
- Dissecting neurofilament tail sequence-phosphorylation-structure relationships with multicomponent reconstituted protein brushes.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Phosphorylation of disordered proteins tunes local and global intramolecular interactions.bioRxiv : the preprint server for biology · 2024Article
- Neurofilament Biophysics: From Structure to Biomechanics.Molecular biology of the cell · 2024Review
- From isolated polyelectrolytes to star-like assemblies: the role of sequence heterogeneity on the statistical structure of the intrinsically disordered neurofilament-low tail domain.The European physical journal. E, Soft matter · 2024Article
- Identifying the Phenotypes of Diffuse Axonal Injury Following Traumatic Brain Injury.Brain sciences · 2023Review
- Intramolecular structural heterogeneity altered by long-range contacts in an intrinsically disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Neurofilament accumulations in amyotrophic lateral sclerosis patients' motor neurons impair axonal initial segment integrity.Cellular and molecular life sciences : CMLS · 2023Article
- The role of neurofilament transport in the radial growth of myelinated axons.Molecular biology of the cell · 2023Article
- Self-Assembly of Tunable Intrinsically Disordered Peptide Amphiphiles.Biomacromolecules · 2023Article
- Electron cryo-tomography reveals the subcellular architecture of growing axons in human brain organoids.eLife · 2021Article
- Order from Disorder with Intrinsically Disordered Peptide Amphiphiles.Journal of the American Chemical Society · 2021Article
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- Influence of a GSK3β phosphorylation site within the proximal C-terminus of Neurofilament-H on neurofilament dynamics.Biology open · 2017Article
- Paradoxes and wonders of intrinsic disorder: Stability of instability.Intrinsically disordered proteins · 2017Article
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Authors and funding
8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The biological function of protein assemblies has been conventionally equated with a unique three-dimensional protein structure and protein-specific interactions. However, in the past 20 years it has been found that some assemblies contain long flexible regions that adopt multiple structural conformations. These include neurofilament proteins that constitute the stress-responsive supportive network of neurons. Herein, we show that the macroscopic properties of neurofilament networks are tuned by enzymatic regulation of the charge found on the flexible protein regions. The results reveal an enzymatic (phosphorylation) regulation of macroscopic properties such as orientation, stress response, and expansion in flexible protein assemblies. Using a model that explains the attractive electrostatic interactions induced by enzymatically added charges, we demonstrate that phosphorylation regulation is far richer and versatile than previously considered.
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