Key result
Anillin, a diffusible non-motor actin crosslinker, can propel the constriction of actin rings in vitro by generating forces that maximize overlap lengths between filaments.
Why the study?
In multiple organisms, cytokinetic actin ring constriction is myosin independent, but how actin rings constrict without motor activity remained unclear.
Anillin, a non-motor actin crosslinker, can propel the constriction of actin rings independently of myosin motors.
Suggests myosin-independent actin contractility; leaves open relevance to cardiomyocyte division or remodeling in vivo.
Constriction of the actin cytokinetic ring is an essential step of cell division. In a generally accepted view, the constriction is driven by relative sliding of actin filaments propelled by myosin motors. However, in multiple organisms, the ring constriction is myosin independent. How actin rings constrict in the absence of motor activity remains unclear. Here, we demonstrate that actin contractility can be propelled by anillin, a diffusible non-motor actin crosslinker, localising to the cytokinetic ring. We in vitro observed the formation and constriction of rings comprising multiple actin filaments bundled by anillin. Rings constricted due to anillin-generated forces maximising the overlap lengths between the filaments. Actin disassembly promoted constriction. We propose that actin crosslinkers, generating forces complementary to molecular motors, contribute to the contractility of diverse actin structures, including the cytokinetic ring.
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Kučera et al. (2020) studied Cell division / Cytokinesis. Anillin was evaluated on Actin ring constriction. Anillin, a diffusible non-motor actin crosslinker, can propel the constriction of actin rings in vitro by generating forces that maximize overlap lengths between filaments.
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