Journal
NATURE COMMUNICATIONS
Volume 8, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms14347
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Funding
- Wellcome Trust [104924/14/Z/14]
- Medical Research Council (MRC) [MC_UU_12010, G0902418, MC_UU_12025]
- MRC/BBSRC/EPSRC [MR/K01577X/1]
- University of Oxford (John-Fell-Fund)
- University of Oxford (EP Abraham Cephalosporin Trust Fund)
- University of Oxford (Wellcome Trust Institutional Strategic Support Fund)
- EPSRC
- Wellcome Trust-Massachusetts Institute of Technology Fellowship [WT103883]
- EMBO Long Term Fellowship (MEMBRANE DYNAMICS)
- Marie Curie Intra-European Fellowship (MEMBRANE DYNAMICS)
- Engineering and Physical Sciences Research Council [1230489] Funding Source: researchfish
- Medical Research Council [MC_UU_00008/9, MR/K01577X/1, MC_UU_12010/9] Funding Source: researchfish
- MRC [MC_UU_00008/9, MC_UU_12010/9, MR/K01577X/1] Funding Source: UKRI
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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.
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