Self-organizing actin patterns shape membrane architecture but not cell mechanics

M. Fritzsche (), D. Li, H. Colin-York, V. T. Chang, E. Moeendarbary, J. H. Felce, E. Sezgin, G. Charras, E. Betzig and C. Eggeling ()
Additional contact information
M. Fritzsche: MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford
D. Li: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
H. Colin-York: MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford
V. T. Chang: MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford
E. Moeendarbary: Massachusetts Institute of Technology
J. H. Felce: MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford
E. Sezgin: MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford
G. Charras: University College London
E. Betzig: Howard Hughes Medical Institute, Janelia Research Campus
C. Eggeling: MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford

Nature Communications, 2017, vol. 8, issue 1, 1-14

Abstract: 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.

Date: 2017
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/ncomms14347 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14347

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms14347

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().