Actin Dynamics in Cellular Systems
Summary
Actin constitutes a fundamental component of the eukaryotic cytoskeleton, cycling between monomeric globular (G-actin) and filamentous (F-actin) forms to underpin cell shape, motility, division and intracellular transport. Polymerisation is initiated by nucleation factors and sustained by elongation at filament barbed ends, while depolymerisation at pointed ends enables a treadmilling behaviour that drives protrusive forces in lamellipodia and filopodia. A diverse array of actin-binding proteins (ABPs), including formins, the Arp2/3 complex and severing factors such as cofilin, finely tune filament architecture, branching and turnover. This dynamic network transduces mechanical signals, integrates biochemical pathways and orchestrates events from tissue morphogenesis to immune cell function. Aberrant actin regulation underlies pathologies ranging from metastatic invasion to cardiomyopathy, emphasising the global significance of mechanochemical control within living systems.
Research from Nature Portfolio
Recent studies have introduced engineered protein switches that permit precise, stimulus-responsive recruitment of ABP modules to F-actin in living cells. These controllable actin-binding switches operate orthogonally and can be multiplexed to sculpt cytoskeletal arrangements and modulate cell and tissue geometry on demand. Complementary work has characterised small-molecule stabilisers of actin, revealing that closely related compounds may differ in their competition with cofilin and gelsolin, thereby selectively influencing filament nucleation, stabilisation and downstream transcriptional programmes. In parallel, novel Affimer reagents have been developed as genetically encoded F-actin affinity probes for live and fixed cells, with distinct binding kinetics and minimal perturbation of native dynamics, offering versatile alternatives to traditional toxins or peptides for imaging and mechanobiology.
Actin Dynamics in Cellular Systems publication trend
The graph below shows the total number of articles in actin dynamics in cellular systems across all publications each year (not limited to Nature Index journals).
Technical terms
G-actin: Monomeric globular form of actin that polymerises into filaments.
F-actin: Filamentous polymer of actin subunits forming microfilaments.
Nucleation: The initial assembly of a small actin oligomer that seeds filament growth.
Treadmilling: Simultaneous addition of actin monomers at the barbed end and loss at the pointed end of a filament.
Arp2/3 complex: A seven-subunit protein assembly that nucleates branched actin networks.
Cryo-EM: Electron cryomicroscopy technique for determining high-resolution structures of macromolecular complexes.
DARPins: Designed ankyrin repeat proteins used as customisable affinity reagents.
Affimers: Synthetic non-antibody binding proteins selected for specific targets such as F-actin.
References
- Turn-on protein switches for controlling actin binding in cells. Nature Communications (2024).
- Designed Ankyrin Repeat Proteins as Actin Labels of Distinct Cytoskeletal Structures in Living Cells. ACS Nano (2024).
- Structure of the F-tractin–F-actin complex. Journal of Cell Biology (2025).
- Actin stabilizing compounds show specific biological effects due to their binding mode. Scientific Reports (2019).
- Affimer proteins for F-actin: novel affinity reagents that label F-actin in live and fixed cells. Scientific Reports (2018).
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