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

Institutions

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

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Magnesium Cations Modulate Actin Bundles Formed by α ‐Actinin

Hyeran Kang, Jung Han Kim, Jinho Park, Eunyoung Moon et al.
Cytoskeleton
Cellular Mechanics and Interactions
article

Magnesium Cations Modulate Actin Bundles Formed by α ‐Actinin

Hyeran Kang, Jung Han Kim, Jinho Park, Eunyoung Moon, Ramsha Hashmi
article en

Abstract

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.

Cytoskeleton
University of Central Florida (US), Korea Basic Science Institute (KR), Dong-A University (KR)
National Science Foundation, Korea Basic Science Institute, National Science and Technology Council
Openalex Percentile: Top 14%
Cellular Mechanics and Interactions
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.

Magnesium Cations Modulate Actin Bundles Formed by α ‐Actinin — Hyeran Kang, Jung Han Kim, et al. · Cytoskeleton (2026) | TGRS Research Map | TGRS