Electrostatics of salt-dependent reentrant phase behaviors highlights diverse roles of ATP in biomolecular condensates

Liquid-liquid phase separation (LLPS) involving intrinsically disordered protein regions (IDRs) is a major physical mechanism for biological membraneless compartmentalization. The multifaceted electrostatic effects in these biomolecular condensates are exemplified here by experimental and theoretica...

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Main Authors: Yi-Hsuan Lin, Tae Hun Kim, Suman Das, Tanmoy Pal, Jonas Wessén, Atul Kaushik Rangadurai, Lewis E Kay, Julie D Forman-Kay, Hue Sun Chan
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2025-03-01
Series:eLife
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Online Access:https://elifesciences.org/articles/100284
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author Yi-Hsuan Lin
Tae Hun Kim
Suman Das
Tanmoy Pal
Jonas Wessén
Atul Kaushik Rangadurai
Lewis E Kay
Julie D Forman-Kay
Hue Sun Chan
author_facet Yi-Hsuan Lin
Tae Hun Kim
Suman Das
Tanmoy Pal
Jonas Wessén
Atul Kaushik Rangadurai
Lewis E Kay
Julie D Forman-Kay
Hue Sun Chan
author_sort Yi-Hsuan Lin
collection DOAJ
description Liquid-liquid phase separation (LLPS) involving intrinsically disordered protein regions (IDRs) is a major physical mechanism for biological membraneless compartmentalization. The multifaceted electrostatic effects in these biomolecular condensates are exemplified here by experimental and theoretical investigations of the different salt- and ATP-dependent LLPSs of an IDR of messenger RNA-regulating protein Caprin1 and its phosphorylated variant pY-Caprin1, exhibiting, for example, reentrant behaviors in some instances but not others. Experimental data are rationalized by physical modeling using analytical theory, molecular dynamics, and polymer field-theoretic simulations, indicating that interchain ion bridges enhance LLPS of polyelectrolytes such as Caprin1 and the high valency of ATP-magnesium is a significant factor for its colocalization with the condensed phases, as similar trends are observed for other IDRs. The electrostatic nature of these features complements ATP’s involvement in π-related interactions and as an amphiphilic hydrotrope, underscoring a general role of biomolecular condensates in modulating ion concentrations and its functional ramifications.
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spelling doaj-art-4a6c258cd3384322b50954bcfb19ea5b2025-08-20T02:00:51ZengeLife Sciences Publications LtdeLife2050-084X2025-03-011310.7554/eLife.100284Electrostatics of salt-dependent reentrant phase behaviors highlights diverse roles of ATP in biomolecular condensatesYi-Hsuan Lin0Tae Hun Kim1Suman Das2Tanmoy Pal3Jonas Wessén4https://orcid.org/0000-0002-5904-8442Atul Kaushik Rangadurai5Lewis E Kay6https://orcid.org/0000-0002-4054-4083Julie D Forman-Kay7https://orcid.org/0000-0001-8265-972XHue Sun Chan8https://orcid.org/0000-0002-1381-923XDepartment of Biochemistry, University of Toronto, Toronto, Canada; Molecular Medicine, Hospital for Sick Children, Toronto, CanadaDepartment of Biochemistry, University of Toronto, Toronto, Canada; Molecular Medicine, Hospital for Sick Children, Toronto, Canada; Department of Molecular Genetics, University of Toronto, Toronto, Canada; Department of Chemistry, University of Toronto, Toronto, CanadaDepartment of Biochemistry, University of Toronto, Toronto, Canada; Department of Chemistry, Gandhi Institute of Technology and Management, Visakhapatnam, IndiaDepartment of Biochemistry, University of Toronto, Toronto, CanadaDepartment of Biochemistry, University of Toronto, Toronto, CanadaDepartment of Biochemistry, University of Toronto, Toronto, Canada; Molecular Medicine, Hospital for Sick Children, Toronto, Canada; Department of Molecular Genetics, University of Toronto, Toronto, Canada; Department of Chemistry, University of Toronto, Toronto, CanadaDepartment of Biochemistry, University of Toronto, Toronto, Canada; Molecular Medicine, Hospital for Sick Children, Toronto, Canada; Department of Molecular Genetics, University of Toronto, Toronto, Canada; Department of Chemistry, University of Toronto, Toronto, CanadaDepartment of Biochemistry, University of Toronto, Toronto, Canada; Molecular Medicine, Hospital for Sick Children, Toronto, CanadaDepartment of Biochemistry, University of Toronto, Toronto, CanadaLiquid-liquid phase separation (LLPS) involving intrinsically disordered protein regions (IDRs) is a major physical mechanism for biological membraneless compartmentalization. The multifaceted electrostatic effects in these biomolecular condensates are exemplified here by experimental and theoretical investigations of the different salt- and ATP-dependent LLPSs of an IDR of messenger RNA-regulating protein Caprin1 and its phosphorylated variant pY-Caprin1, exhibiting, for example, reentrant behaviors in some instances but not others. Experimental data are rationalized by physical modeling using analytical theory, molecular dynamics, and polymer field-theoretic simulations, indicating that interchain ion bridges enhance LLPS of polyelectrolytes such as Caprin1 and the high valency of ATP-magnesium is a significant factor for its colocalization with the condensed phases, as similar trends are observed for other IDRs. The electrostatic nature of these features complements ATP’s involvement in π-related interactions and as an amphiphilic hydrotrope, underscoring a general role of biomolecular condensates in modulating ion concentrations and its functional ramifications.https://elifesciences.org/articles/100284liquid-liquid phase separationphosphorylationintrinsically disordered proteinsrandom phase approximationfield-theoretic simulationmolecular dynamics
spellingShingle Yi-Hsuan Lin
Tae Hun Kim
Suman Das
Tanmoy Pal
Jonas Wessén
Atul Kaushik Rangadurai
Lewis E Kay
Julie D Forman-Kay
Hue Sun Chan
Electrostatics of salt-dependent reentrant phase behaviors highlights diverse roles of ATP in biomolecular condensates
eLife
liquid-liquid phase separation
phosphorylation
intrinsically disordered proteins
random phase approximation
field-theoretic simulation
molecular dynamics
title Electrostatics of salt-dependent reentrant phase behaviors highlights diverse roles of ATP in biomolecular condensates
title_full Electrostatics of salt-dependent reentrant phase behaviors highlights diverse roles of ATP in biomolecular condensates
title_fullStr Electrostatics of salt-dependent reentrant phase behaviors highlights diverse roles of ATP in biomolecular condensates
title_full_unstemmed Electrostatics of salt-dependent reentrant phase behaviors highlights diverse roles of ATP in biomolecular condensates
title_short Electrostatics of salt-dependent reentrant phase behaviors highlights diverse roles of ATP in biomolecular condensates
title_sort electrostatics of salt dependent reentrant phase behaviors highlights diverse roles of atp in biomolecular condensates
topic liquid-liquid phase separation
phosphorylation
intrinsically disordered proteins
random phase approximation
field-theoretic simulation
molecular dynamics
url https://elifesciences.org/articles/100284
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