Structure and dynamics of cross-linked actin networks

Lieleg, Oliver; Claessens, Mireille Maria Anna Elisabeth; Bausch, Andreas R.

doi:10.1039/b912163n

Cited by 223 publications

(267 citation statements)

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“…To test if the high binding propensity of α-actinin is a precondition for the observed reorganization and cyclic hardening behavior 12,14 , we also utilize the actin crosslinking protein filamin, a protein that kinetically traps actin networks similar to α-actinin 15 . The architecture of the bundled actin/filamin networks, at the concentrations chosen, resembles that of actin/α-actinin networks.…”

Section: Cyclic Hardening In Actin Network Bundled By Filaminmentioning

confidence: 99%

Cyclic hardening in bundled actin networks

et al. 2010

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nonlinear deformations can irreversibly alter the mechanical properties of materials. most soft materials, such as rubber and living tissues, display pronounced softening when cyclically deformed. Here we show that, in contrast, reconstituted networks of crosslinked, bundled actin filaments harden when subject to cyclical shear. As a consequence, they exhibit a mechanomemory where a significant stress barrier is generated at the maximum of the cyclic shear strain. This unique response is crucially determined by the network architecture: at lower crosslinker concentrations networks do not harden, but soften showing the classic mullins effect known from rubber-like materials. By simultaneously performing macrorheology and confocal microscopy, we show that cyclic shearing results in structural reorganization of the network constituents such that the maximum applied strain is encoded into the network architecture.

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Section: Cyclic Hardening In Actin Network Bundled By Filaminmentioning

confidence: 99%

Cyclic hardening in bundled actin networks

et al. 2010

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“…Actin filaments are a key component in the cellular toolbox as they can be organized into networks with different morphologies and thus different viscoelastic properties [2][3][4][5]. A prominent example of such an actin filament structure is given by filopodia -hair-like protuberances in migrating cells in which the actin filaments are ordered into bundles.…”

Section: Introductionmentioning

confidence: 99%

A single charge in the actin binding domain of fascin can independently tune the linear and non-linear response of an actin bundle network

Maier

Müller

Heussinger³

et al. 2015

Eur. Phys. J. E

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Abstract. Actin binding proteins (ABPs) not only set the structure of actin filament assemblies but also mediate the frequency-dependent viscoelastic moduli of cross-linked and bundled actin networks. Point mutations in the actin binding domain of those ABPs can tune the association and dissociation dynamics of the actin/ABP bond and thus modulate the network mechanics both in the linear and non-linear response regime. We here demonstrate how the exchange of a single charged amino acid in the actin binding domain of the ABP fascin triggers such a modulation of the network rheology. Whereas the overall structure of the bundle networks is conserved, the transition point from strain-hardening to strain-weakening sensitively depends on the cross-linker off-rate and the applied shear rate. Our experimental results are consistent both with numerical simulations of a cross-linked bundle network and a theoretical description of the bundle network mechanics which is based on non-affine bending deformations and force-dependent crosslink dynamics.

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“…The difference between the absolute value of G 0 (on the order of ≈ 1Pa) and that of the weakly frequency-dependent shear modulus () G ω o f ce lls ( s e e S e c. 3 .3 b e lo w ; o n t h e o r d e r o f ≈ 1k P a ) is n o w u n d e rst o o d a s a consequence of the different network elasticity in the absence or presence of crosslinkers and prestress. Networks of F-actin can be crosslinked using specific actin-binding-proteins (ABPs), and increasingly sophisticated studies have demonstrated that the relative crosslinker concentration, the type of crosslinker and even its molecular details provide finegrained control over elastic and structural properties of the network (Gardel et al, 2004;Lieleg et al, 2010). Network elasticity is also determined by the flexibility of crosslinkers (Wagner et al, 2006).…”

Section: Importance Of Crosslinkersmentioning

confidence: 99%