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Persistent and recyclable myosin II minifilaments drive cortical contractility in the early C. elegans embryo
bioRxiv · · Preprint · Open access
Chauca Espinoza, Suman + 6 more
Abstract ↗AI summary
The abstract is read at the publisher; the summary is JClub's.
In the early Caenorhabditis elegans embryo, myosin II minifilaments persist as intact units after cortical unbinding and can be recycled over long distances.
- Why it matters: Cortical contractility depends on how myosin minifilaments organize and exchange between cortex and cytoplasm, but their in vivo dynamics and functional implications remain unclear.
- What they did: The study used SIM-TIRF and single-molecule TIRF to track minifilament structure and behaviors, including partition-like events, proto-stress fiber alignment, and sequential unbinding/rebinding, plus photoconversion and numerical simulations.
- The result: Minifilaments are predominantly stationary when bound to actin, and simulations indicate this static behavior is essential for sustaining cortical stress within a continuously remodeling actin network.
The findingWhy it mattersWhat they didThe result
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