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Rheology of membrane-attached minimal actin cortices

MPG-Autoren
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Steinem,  Claudia
Max Planck Fellow Group Membrane-based biomimetic nano- and micro-compartments, Max Planck Institute for Dynamics and Self-Organization, Max Planck Society;

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Zitation

Nöding, H., Schön, M., Reinermann, C., Dörrer, N., Kürschner, A., Geil, B., et al. (2018). Rheology of membrane-attached minimal actin cortices. The Journal of Physical Chemistry B, 122(16), 4537-4545. doi:10.1021/acs.jpcb.7b11491.


Zitierlink: https://hdl.handle.net/21.11116/0000-0001-4712-B
Zusammenfassung
The actin cortex is a thin cross-linked network attached to the plasma membrane, which is responsible for the cell's shape during migration, division, and growth. In a reductionist approach, we created a minimal actin cortex (MAC) attached to a lipid membrane to correlate the filamentous actin architecture with its viscoelastic properties. The system is composed of a supported 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine bilayer doped with the receptor lipid phosphatidylinositol(4,5)-bisphosphate (PtdIns(4,5)P-2) to which a constitutively active mutant of ezrin, which is a direct membrane-cytoskeleton linker, is bound. The formation of the MAC on the supported lipid bilayer is analyzed as a function of increasing PtdIns(4,5)P-2/ezrin pinning points, revealing an increase in the intersections between actin filaments, that is, the node density of the MAC. Bead tracking microrheology on the membrane-attached actin network provides information about its viscoelastic properties. The results show that ezrin serves as a dynamic cross-linker for the actin cortex attached to the lipid bilayer and that the stiffness of the network is influenced by the pinning point density, relating the plateau storage modulus G(0) to the node density of the MAC.