ArticleNature communications2025
Molecular simulations of enzymatic phosphorylation of disordered proteins and their condensates.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Active Field Theory Approach to Explain Size Control of Transcriptional Condensates.Macromolecular bioscience · 2026Article
- Therapeutic targeting of the conserved region within the low-complexity domain of TDP-43 is neuroprotective and extends survival in amyotrophic lateral sclerosis mice.Nature aging · 2026Article
- Characterizing the Effects of Protein Glycosylation Perturbation on Phosphorylation Signaling.Analytical chemistry · 2026Article
- Molecular Modeling of the Pathogenetic Mechanisms of Neuropsychiatric Disorders.International journal of molecular sciences · 2026Review
- Molecular Modulation of the Crosstalk Between TDP-43 and SOD1.International journal of molecular sciences · 2026Article
- Prioritizing missense mutations via a deep learning phosphorylation prediction model.Human genomics · 2025Article
- Characterizing the Effects of Protein Glycosylation Perturbation on Phosphorylation Signaling.bioRxiv : the preprint server for biology · 2025Article
- Transcriptional condensates encode a "golden mean" to optimize enhancer-promoter communication across genomic distances.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Repulsive vs Attractive Crowding Distinctly Regulate TDP-43 Condensates through Region-specific Structural Dynamics.JACS Au · 2025Article
- Molecular simulations of enzymatic phosphorylation of disordered proteins and their condensates.Nature communications · 2025Article
- Modeling biomolecular condensates across scales: Atomistic, coarse-grained, and data-driven approaches.Advances in physics: X · 2025Article
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4 authors.
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Abstract
Condensation and aggregation of disordered proteins in cellular non-equilibrium environments are shaped decisively by enzymes. Enzymes called kinases phosphorylate proteins, consuming the chemical fuel ATP. Protein phosphorylation by kinases such as Casein kinase 1 delta (CK1δ) determines the interactions of neurodegeneration-linked proteins such as TDP-43. Hyperphosphorylation of TDP-43 by CK1δ may be a cytoprotective mechanism for neurons, but how CK1δ interacts with protein condensates is not known. Molecular dynamics simulations hold the promise to resolve how kinases interact with disordered proteins and their condensates, and how this shapes the phosphorylation dynamics. In practice, it is difficult to verify whether implementations of chemical-fuel driven coarse-grained simulations are thermodynamically consistent, which we address by a generally applicable and automatic Markov state modeling approach. In this work, we thus elucidate with coarse-grained simulations, drivers of how TDP-43 is phosphorylated by CK1δ and how this leads to the dissolution of TDP-43 condensates upon hyperphosphorylation.
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