TY - JOUR
T1 - Cations Modulate Actin Bundle Mechanics, Assembly Dynamics, and Structure
AU - Castaneda, Nicholas
AU - Zheng, Tianyu
AU - Rivera-Jacquez, Hector J.
AU - Lee, Hyun Ju
AU - Hyun, Jaekyung
AU - Balaeff, Alexander
AU - Huo, Qun
AU - Kang, Hyeran
N1 - Publisher Copyright:
© 2018 American Chemical Society.
PY - 2018/4/12
Y1 - 2018/4/12
N2 - Actin bundles are key factors in the mechanical support and dynamic reorganization of the cytoskeleton. High concentrations of multivalent counterions promote bundle formation through electrostatic attraction between actin filaments that are negatively charged polyelectrolytes. In this study, we evaluate how physiologically relevant divalent cations affect the mechanical, dynamic, and structural properties of actin bundles. Using a combination of total internal reflection fluorescence microscopy, transmission electron microscopy, and dynamic light scattering, we demonstrate that divalent cations modulate bundle stiffness, length distribution, and lateral growth. Molecular dynamics simulations of an all-atom model of the actin bundle reveal specific actin residues coordinate cation-binding sites that promote the bundle formation. Our work suggests that specific cation interactions may play a fundamental role in the assembly, structure, and mechanical properties of actin bundles.
AB - Actin bundles are key factors in the mechanical support and dynamic reorganization of the cytoskeleton. High concentrations of multivalent counterions promote bundle formation through electrostatic attraction between actin filaments that are negatively charged polyelectrolytes. In this study, we evaluate how physiologically relevant divalent cations affect the mechanical, dynamic, and structural properties of actin bundles. Using a combination of total internal reflection fluorescence microscopy, transmission electron microscopy, and dynamic light scattering, we demonstrate that divalent cations modulate bundle stiffness, length distribution, and lateral growth. Molecular dynamics simulations of an all-atom model of the actin bundle reveal specific actin residues coordinate cation-binding sites that promote the bundle formation. Our work suggests that specific cation interactions may play a fundamental role in the assembly, structure, and mechanical properties of actin bundles.
UR - https://www.scopus.com/pages/publications/85045473791
U2 - 10.1021/acs.jpcb.8b00663
DO - 10.1021/acs.jpcb.8b00663
M3 - Article
C2 - 29608304
AN - SCOPUS:85045473791
SN - 1520-6106
VL - 122
SP - 3826
EP - 3835
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
IS - 14
ER -