# Mechanochemical feedback between confinement and actin crosslinking drives the shape dynamics of liquid-like droplets

**Authors:** Daniel Mansour, Dominique Jordan, Caleb Walker, Aravind Chandrasekaran, Christopher T. Lee, Kristin Graham, Jeanne C. Stachowiak, Padmini Rangamani

PMC · DOI: 10.1038/s41467-026-69803-4 · Nature Communications · 2026-02-23

## TL;DR

This paper shows how droplet mechanics and actin crosslinkers work together to shape liquid-like droplets and organize actin networks.

## Contribution

The study reveals a mechanochemical feedback mechanism linking droplet confinement and actin crosslinking to shape dynamics.

## Key findings

- Droplet deformation leads to tightly-bundled actin rings and weakly-bundled discs.
- Crosslinked bundle thickness and droplet diameter follow a power law.
- Droplet deformation dynamics depend on surface tension and crosslinker binding kinetics.

## Abstract

Several actin-binding proteins form phase-separated condensates that promote actin filament assembly and bundling. However, the mechanism by which crosslinker multivalency, actin growth, and condensate mechanics regulate actin organization and droplet shape is not well understood. Here, using a combination of agent-based simulations and experiments, we show that a dynamically deformable droplet interface enables the emergence of tightly-bundled actin rings and weakly-bundled actin discs. We find that crosslinked bundle thickness and droplet diameter follow a power law, consistent with measurements in condensates formed by vasodilator-stimulated phosphoprotein. In addition, the dynamics of droplet deformation exhibit a dynamic snapping behavior that depends on droplet surface tension and crosslinker binding kinetics. We assess the generalizability of these predictions in condensates formed by lamellipodin and RGG. Together, these results indicate that mechanochemical feedback between droplet interfacial mechanics and crosslinker multivalency tunes actin organization and controls the dynamics of droplet deformation driven by actin networks.

Actin-binding proteins form condensates that dynamically organize actin filaments. Here, the authors show that mechanochemical feedback between droplet mechanics and crosslinker multivalency tunes actin network structure and drives droplet deformation.

## Linked entities

- **Proteins:** rgg (quorum-sensing system transcriptional regulator Rgg)

## Full-text entities

- **Genes:** VASP (vasodilator stimulated phosphoprotein) [NCBI Gene 7408], RAPH1 (Ras association (RalGDS/AF-6) and pleckstrin homology domains 1) [NCBI Gene 65059] {aka ALS2CR18, ALS2CR9, LPD, PREL-2, PREL2, RMO1}

## Full text

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## Figures

8 figures with captions in the complete paper: https://tomesphere.com/paper/PMC13039813/full.md

## References

7 references — full list in the complete paper: https://tomesphere.com/paper/PMC13039813/full.md

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Source: https://tomesphere.com/paper/PMC13039813