Self-organizing actin patterns shape membrane architecture but not cell mechanics
Name
Self-organizing actin.pdf
Size
5.93 MB
Format
Adobe PDF
Checksum (MD5)
1c8c2872ae5cf356dd3d903a9f8d474c
Author(s) • • • • • • • • •
Fritzsche, M.
Li, D.
Colin-York, H.
Chang, V. T.
Felce, J. H.
Sezgin, E.
Charras, G.
Betzig, E.
Eggeling, C.
Moeendarbary, Emadaldin
Date Issued
February 2017
Journal
Nature Communications
Publisher
Nature Publishing Group
Citation
Fritzsche, M.; Li, D.; Colin-York, H.; Chang, V. T.; Moeendarbary, E.; Felce, J. H.; Sezgin, E.; Charras, G.; Betzig, E. and Eggeling, C. “Self-Organizing Actin Patterns Shape Membrane Architecture but Not Cell Mechanics.” Nature Communications 8 (February 2017): 14347 © 2017 The Authors
Version
Final published version
Abstract
Cell-free studies have demonstrated how collective action of actin-associated proteins can organize actin filaments into dynamic patterns, such as vortices, asters and stars. Using complementary microscopic techniques, we here show evidence of such self-organization of the actin cortex in living HeLa cells. During cell adhesion, an active multistage process naturally leads to pattern transitions from actin vortices over stars into asters. This process is primarily driven by Arp2/3 complex nucleation, but not by myosin motors, which is in contrast to what has been theoretically predicted and observed in vitro. Concomitant measurements of mechanics and plasma membrane fluidity demonstrate that changes in actin patterning alter membrane architecture but occur functionally independent of macroscopic cortex elasticity. Consequently, tuning the activity of the Arp2/3 complex to alter filament assembly may thus be a mechanism allowing cells to adjust their membrane architecture without affecting their macroscopic mechanical properties.
MIT Department
Massachusetts Institute of Technology. Department of Biological Engineering
Terms of Use
Creative Commons Attribution 4.0 International License
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1038/ncomms14347