Cross-linker binding strength influences actin assembly microstructure and myosin II driven remodeling
- 1Clemson University
Abstract
The actin cytoskeleton is a self-assembled material that acts as the mechanical scaffold of the cell. Within the cell, protein cross-linkers organize actin filaments into assemblies with various microstructures that support distinct physiological functions. These protein cross-linkers differ in structural features. To decouple the role of individual cross-linker properties in actin assembly microstructure and mechanics, we synthesize programmable cross-linkers using a DNA linker coupled to binding domains. We find that high affinity cross-linkers induce actin bundling, while low affinity cross-linkers form actin networks. Myosin II motors remodel and contract all cross-linked networks tested in distinct ways from uncross-linked networks. We find that networks with high affinity cross-linkers have different myosin induced dynamics than networks with low affinity cross-linkers. This research expands our understanding of how cells regulate their mechanics and microstructures, while also providing insight towards the structure-property relationship in complex soft materials.
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BibTeX
@misc{feigeles2026crosslinker,
title = {{Cross-linker binding strength influences actin assembly microstructure and myosin II driven remodeling}},
author = {C. A. Feigeles and M. Janquart and V. Armstrong and K. L. Weirich},
howpublished = {bioRxiv},
year = {2026},
month = oct,
doi = {10.64898/2026.10.02.756345},
url = {https://www.biorxiv.org/content/10.64898/2026.10.02.756345v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - Cross-linker binding strength influences actin assembly microstructure and myosin II driven remodeling
AU - C. A. Feigeles
AU - M. Janquart
AU - V. Armstrong
AU - K. L. Weirich
PY - 2026
DA - 2026/10/02
PB - bioRxiv
DO - 10.64898/2026.10.02.756345
UR - https://www.biorxiv.org/content/10.64898/2026.10.02.756345v1
AB - The actin cytoskeleton is a self-assembled material that acts as the mechanical scaffold of the cell. Within the cell, protein cross-linkers organize actin filaments into assemblies with various microstructures that support distinct physiological functions. These protein cross-linkers differ in structural features. To decouple the role of individual cross-linker properties in actin assembly microstructure and mechanics, we synthesize programmable cross-linkers using a DNA linker coupled to binding domains. We find that high affinity cross-linkers induce actin bundling, while low affinity cross-linkers form actin networks. Myosin II motors remodel and contract all cross-linked networks tested in distinct ways from uncross-linked networks. We find that networks with high affinity cross-linkers have different myosin induced dynamics than networks with low affinity cross-linkers. This research expands our understanding of how cells regulate their mechanics and microstructures, while also providing insight towards the structure-property relationship in complex soft materials.
ER -