Profilin Dynamics in Actin Cytoskeleton Regulation

The actin cytoskeleton underpins a vast array of cellular processes, from migration and division to morphogenesis and intracellular transport. Central to its dynamic remodelling is profilin, a small (12–15 kDa) actin-binding protein that catalyses ADP–ATP exchange on actin monomers (G-actin) and channels them to filament ends (F-actin). By engaging with formins and Ena/VASP proteins, profilin directs rapid filament elongation, while its interactions with phosphoinositides and proline-rich ligands integrate membrane signalling with cytoskeletal assembly. This dual capacity to catalyse monomer recycling and to sense lipid-derived cues enables cells to adapt protrusive forces and contractile tension in response to external stimuli. Aberrant profilin expression or activity perturbs actomyosin contractility, disturbs microtubule–actin crosstalk and contributes to pathologies ranging from vascular inflammation and neurodegeneration to tumour cell invasion. Recent advances in live-cell microscopy and biophysical assays have begun to unravel how swift profilin-actin cycling at leading edges sustains motile behaviour, whilst its transient sequestration modulates network plasticity, highlighting new avenues for therapeutic targeting.

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Profilin Dynamics in Actin Cytoskeleton Regulation publication trend

The graph below shows the total number of articles in profilin dynamics in actin cytoskeleton regulation across all publications each year (not limited to Nature Index journals).

Technical terms

Profilin: A small actin-binding protein that catalyses nucleotide exchange on actin monomers and delivers them to growing filaments, thereby regulating actin polymerisation.
G-actin: Globular monomeric form of actin that serves as the building block for filamentous actin.
F-actin: Filamentous polymer of actin monomers that forms the structural framework of the cytoskeleton.
Phosphoinositide: Membrane phospholipids, notably PI(4,5)P₂ and PI(3,4,5)P₃, that act as signalling cofactors and modulate actin-binding protein localisation and activity.

References

1. Prolonged depletion of profilin 1 or F-actin causes an adaptive response in microtubules. Journal of Cell Biology (2024).
2. Vascular endothelial cell-specific disruption of the profilin1 gene leads to severe multiorgan pathology and inflammation causing mortality. PNAS Nexus (2023).
3. Actin-binding protein profilin1 is an important determinant of cellular phosphoinositide control. Journal of Biological Chemistry (2023).