Magnesium Cations Modulate Actin Bundles Formed by α ‐Actinin
ABSTRACT α ‐Actinin is an actin‐crosslinking protein that influences cytoskeletal organization by forming actin bundles or networks. Divalent cations, such as magnesium cations (Mg 2+ ), promote bundling through counterion condensation. While α ‐actinin and Mg 2+ individually promote actin bundle assembly, their combined effects on actin bundling remain unclear. Here, we determine how Mg 2+ affects α ‐actinin's binding to filaments and its subsequent bundling activities through biophysical analysis. We show that increasing Mg 2+ concentrations enhance the binding of α ‐actinin to actin filaments, producing more compact bundles instead of loose networks. Molecular dynamics simulation indicates that Mg 2+ modulates the interaction between filaments and the calponin homology 1 domain of α ‐actinin. We propose a mechanism by which divalent cations and α ‐actinin crosslinking act simultaneously to drive actin bundle formation.
Authors
- Hyeran Kang (ORCID: https://orcid.org/0000-0003-2785-3479)
- Jung Han Kim (ORCID: https://orcid.org/0000-0002-6678-2282)
- Jinho Park (ORCID: https://orcid.org/0000-0002-3664-2238)
- Eunyoung Moon (ORCID: https://orcid.org/0000-0002-6632-8071)
- Ramsha Hashmi (ORCID: https://orcid.org/0000-0002-5880-6934)
Institutions
- University of Central Florida (US)
- Korea Basic Science Institute (KR)
- Dong-A University (KR)
Publication Details
- Journal
- Cytoskeleton
- Published
- 2026-08-24
- DOI
- https://doi.org/10.1002/cm.70188
- Primary Topic
- Cellular Mechanics and Interactions
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Science Foundation
- Korea Basic Science Institute
- National Science and Technology Council