ArticleNature communications2020
Behavior control of membrane-less protein liquid condensates with metal ion-induced phase separation.
Article in Nature communications, 2020. 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.
- Symmetry-Guided Optical Control of Dynamic 1D Protein Self-Assembly and Precise In Vitro Initiation of Biomolecular Condensation.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Advances in engineering and applications of synthetic phase-separated membraneless organelles in biotechnology.Synthetic and systems biotechnology · 2026Review
- Peptide-Metal Cation Coacervate Microdroplets as Membrane-free Protocells with Enhanced Light-Induced Catalysis.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- The Effect of Protein Tagging on Aggregation and Phase Separation.Journal of cellular biochemistry · 2026Review
- Metal-dependent and metal-free mechanisms of peptide condensate catalysts.Nature communications · 2026Article
- Photothermal-Responsive Phase Transition of Proteoliposomes for Heat Shock Protein Sequestering against Cancer Thermoresistance.Research (Washington, D.C.) · 2026Article
- Topography-driven movement of biomolecular condensates.PloS one · 2026Article
- BR-bodies facilitate adaptive responses and survival during copper stress in Caulobacter crescentus.The Journal of biological chemistry · 2025Article
- Purification tags markedly affect self-aggregation of CPEB3.FEBS letters · 2025Article
- Programming biological communication between distinct membraneless compartments.Nature chemical biology · 2025Article
- Investigating the Nature of PRM:SH3 Interactions Using Artificial Intelligence and Molecular Dynamics.Journal of chemical information and modeling · 2025Article
- Rational design of chemical- and light-inducible cGAS activation based on mechanistic insights.Communications biology · 2025Article
- BR-Bodies Facilitate Adaptive Responses and Survival During Copper Stress inbioRxiv : the preprint server for biology · 2025Article
- Structured protein domains enter the spotlight: modulators of biomolecular condensate form and function.Trends in biochemical sciences · 2025Review
- catGRANULE 2.0: accurate predictions of liquid-liquid phase separating proteins at single amino acid resolution.Genome biology · 2025Article
- Size-controlled assembly of phase separated protein condensates with interfacial protein cages.Nature communications · 2025Article
- Trifluoroacetic Acid as a Molecular Probe for the Dense Phase in Liquid-Liquid Phase-Separating Peptide Systems.Analytical chemistry · 2025Article
- How bacteria actively use passive physics to make biofilms.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Biomolecular Condensates Decipher Molecular Codes of Cell Fate: From Biophysical Fundamentals to Therapeutic Practices.International journal of molecular sciences · 2024Review
- A platform to induce and mature biomolecular condensates using chemicals and light.Nature chemical biology · 2024Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phase separation of specific biomolecules into liquid droplet-like condensates is a key mechanism to form membrane-less organelles, which spatio-temporally organize diverse biochemical processes in cells. To investigate the working principles of these biomolecular condensates as dynamic reaction centers, precise control of diverse condensate properties is essential. Here, we design a strategy for metal ion-induced clustering of minimal protein modules to produce liquid protein condensates, the properties of which can be widely varied by simple manipulation of the protein clustering systems. The droplet forming-minimal module contains only a single receptor protein and a binding ligand peptide with a hexahistidine tag for divalent metal ion-mediated clustering. A wide range of protein condensate properties such as droplet forming tendency, droplet morphology, inside protein diffusivity, protein recruitment, and droplet density can be varied by adjusting the nature of receptor/ligand pairs or used metal ions, metal/protein ratios, incubation time, binding motif variation on recruited proteins, and even spacing between receptor/ligand pairs and the hexahistidine tag. We also demonstrate metal-ion-induced protein phase separation in cells. The present phase separation strategy provides highly versatile protein condensates, which will greatly facilitate investigation of molecular and structural codes of droplet-forming proteins and the monitoring of biomolecular behaviors inside diverse protein condensates.
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