Actomyosin Dynamics in Cellular Systems

The orchestrated interplay between filamentous actin (F-actin) and myosin motor proteins underpins a wealth of cellular processes ranging from shape modulation and migration to division and mechanosensation. Actomyosin networks assemble at diverse cellular compartments, where actin polymerisation, crosslinking by specialised proteins and motor-driven contractility produce dynamic tension and structural organisation. Biochemical signalling pathways and membrane interfaces regulate filament nucleation, turnover and myosin recruitment, while mechanical feedback from the environment and boundary conditions fine-tune network connectivity and force transmission. Experimental reconstitutions in cell-sized vesicles and planar lipid bilayers, combined with active matter theories and high-resolution imaging, have elucidated how spatial confinement, filament architecture and motor activity together govern emergent behaviours in both disordered and ordered actomyosin arrays. These insights not only clarify the physical basis of processes such as cortical flow, contractile ring formation and stress fibre alignment but also inform the design of synthetic cytoskeletal systems for bottom-up cell engineering.

Research from Nature Portfolio

Recent studies have harnessed modular assemblies of peptide–DNA crosslinkers to engineer synthetic cytoskeletal scaffolds within cell-sized droplets, enabling tunable localisation of filament bundles and reversible recruitment of molecular payloads. By varying crosslinker geometry and DNA hybridisation, researchers achieved precise control over network mechanics and triggered shape deformations via heat-induced reconfiguration, charting a path towards programmable synthetic cells. In parallel, minimal model cortices reconstituted inside liposomes have dissected the passive role of membrane tension in driving F-actin rearrangement and the active role of myosin in pore opening dynamics, revealing how boundary-induced stresses direct cortical organisation in the absence of complex regulation. Furthermore, encapsulation of bundled actin and myosin in giant unilamellar vesicles has yielded contractile rings whose formation critically depends on membrane association; ATP-driven myosin motors then constrict these rings to induce furrow-like deformations, mirroring the mechanics of cytokinesis.

Actomyosin Dynamics in Cellular Systems publication trend

The graph below shows the total number of articles in actomyosin dynamics in cellular systems across all publications each year (not limited to Nature Index journals).

Technical terms

F-actin: Polymerised filamentous form of actin that constitutes the structural scaffold of the cytoskeleton.

Myosin II: Motor protein that hydrolyses ATP to generate contractile forces on F-actin filaments.

Active gel: Continuum model treating the cytoskeleton as a polymer network with embedded force-generating motors and internal energy conversion.

Giant unilamellar vesicle (GUV): Synthetic single-membrane compartment used to reconstitute cytoskeletal assemblies in a cell-like geometry.

Supported lipid bilayer: Planar membrane system on a solid substrate that mimics the cell surface for controlled studies of membrane–cytoskeleton interactions.

Crosslinker: Molecule or protein that binds multiple actin filaments, stabilising network structures and mediating mechanical coupling.

References

1. Designer peptide–DNA cytoskeletons regulate the function of synthetic cells. Nature Chemistry (2024).
2. Membrane tension induces F-actin reorganization and flow in a biomimetic model cortex. Communications Biology (2023).
3. Reconstitution of contractile actomyosin rings in vesicles. Nature Communications (2021).
4. Bioinspired Membrane Interfaces: Controlling Actomyosin Architecture and Contractility. ACS Applied Materials & Interfaces (2023).
5. MEDYAN: Mechanochemical Simulations of Contraction and Polarity Alignment in Actomyosin Networks. PLOS Computational Biology (2016).