Myosin II-independent contraction of actin filaments in membrane nanotubes.

Authors

Md Arsalan Ashraf, Tapas Singha, Susav Pradhan, Serene Rose David, Pierre Sens, Pramod Pullarkat

Published in

Proceedings of the National Academy of Sciences of the United States of America. Volume 123. Issue 37. Pages e2521821123. Sep 15, 2026. Epub Sep 08, 2026.

Abstract

The ability to generate active stresses within filamentous actin matrices is a fundamental and evolutionarily conserved process driving locomotion and morphogenetic changes in cells. The generation of pushing forces by actin polymerization is reasonably well understood, and is known to drive lamellipodia based motility and filopodial extension. Actin filaments decorated with myosin motors can also generate contractile stresses as in the cell cortex or in cytokinetic rings. In this article we use membrane nanotubes pulled out of axonal shaft to investigate actin dynamics and force generation. We report cyclic growth and retraction dynamics of actin within the tube and correlated contraction events giving rise to sustained load and fail cycles. The contraction mechanism operates independent of myosin II motor proteins. Furthermore, we analyzed the dynamics of actin within the tube, including under various biochemical or genetic perturbations. By combining these results with physical modeling, we argue that stresses generated in the actin filaments by the binding of actin depolymerizing factor (ADF/cofilin) proteins can explain the cyclic load-fail behavior.

PMID:
42709792
Bibliographic data and abstract were imported from PubMed on 09 Sep 2026.

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