ArticleJournal of the American Chemical Society2024
Surface Charge Can Modulate Phase Separation of Multidomain Proteins.
Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Holographic Fingerprinting Reveals Oligomer-Driven Phase Separation in Bovine Serum Albumin.Chemical & biomedical imaging · 2026Article
- Marine-Derived Proteins: Individual Variability in Health Effects Across Protein Structure, Host Genetics, and Gut Microbiota.Comprehensive reviews in food science and food safety · 2026Review
- Counteraction of HMGB1 at ss-dsDNA junctions maintains liquidity of protamine-DNA co-condensates.Nature communications · 2026Article
- Electrostatic bimodality of human cytosolic DNA sensor cGAS-dsDNA condensates revealed by millisecond flashing electrophoretic separation.Nature communications · 2026Article
- Counteraction of HMGB1 at ss-dsDNA junctions maintains liquidity of protamine-DNA co-condensates.bioRxiv : the preprint server for biology · 2026Article
- Mass spectrometry integrates protein design into structural biology method development.QRB discovery · 2026Review
- Fluorescent protein and peptide tags alter condensate formation and dynamics in vivo and in vitro.EMBO reports · 2026Article
- The regulatory principles, physiological functions, and phase transition of biomolecular condensates.Frontiers in cell and developmental biology · 2026Review
- Phase separation and biomolecular condensate formation drive plant endomembrane and autophagy crosstalk.Journal of experimental botany · 2025Review
- How the Extent of Protein Folding and Oligomerization Modulate Condensate Formation and Properties.The journal of physical chemistry letters · 2025Article
- Fast calculation of small-angle scattering profiles of dense protein solutions modeled at the all-atom level.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Correlated Segments of Intrinsically Disordered Proteins as Drivers of Homotypic Phase Separation.JACS Au · 2025Article
- A Charge-Driven Strategy for Covalent Modification and Modulation of Biomolecular Condensates.Journal of the American Chemical Society · 2025Article
- Reconciling competing models on the roles of condensates and soluble complexes in transcription factor function.Molecular cell · 2025Article
- Article
- Regulatory links between the circadian clock and stress-induced biomolecular condensates.Npj biological timing and sleep · 2025Review
- Anisotropic DLVO-like interaction for charge patchiness in colloids and proteins.Nature communications · 2025Article
- Electric charge and salting in/out effects on glucagon's dipole moments and polarizabilities using the GruPol database.Acta crystallographica Section B, Structural science, crystal engineering and materials · 2025Article
- Patchy Charge Distribution Affects the pH in Protein Solutions during Dialysis.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Structured protein domains enter the spotlight: modulators of biomolecular condensate form and function.Trends in biochemical sciences · 2025Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Phase separation has emerged as an important mechanism explaining the formation of certain biomolecular condensates. Biological phase separation is often driven by the multivalent interactions of modular protein domains. Beyond valency, the physical features of folded domains that promote phase separation are poorly understood. We used a model system─the small ubiquitin modifier (SUMO) and its peptide ligand, the SUMO interaction motif (SIM)─to examine how domain surface charge influences multivalency-driven phase separation. Phase separation of polySUMO and polySIM was altered by pH via a change in the protonation state of SUMO surface histidines. These effects were recapitulated by histidine mutations, which modulated SUMO solubility and polySUMO-polySIM phase separation in parallel and were quantitatively explained by atomistic modeling of weak interactions among proteins in the system. Thus, surface charge can tune the phase separation of multivalent proteins, suggesting a means of controlling phase separation biologically, evolutionarily, and therapeutically.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.