Publications by authors named "Harmen Wierenga"

Cell polarization underlies many cellular processes, such as differentiation, migration, and budding. Many living cells, such as budding yeast and fission yeast, use cytoskeletal structures to actively transport proteins to one location on the membrane and create a high-density spot of membrane-bound proteins. Yet, the thermodynamic constraints on filament-based cell polarization remain unknown.

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SignificanceComplex cellular processes such as cell migration require coordinated remodeling of both the actin and the microtubule cytoskeleton. The two networks for instance exert forces on each other via active motor proteins. Here we show that, surprisingly, coupling via passive cross-linkers can also result in force generation.

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The friction between cytoskeletal filaments is of central importance for the formation of cellular structures such as the mitotic spindle and the cytokinetic ring. This friction is caused by passive cross-linkers, yet the underlying mechanism and the dependence on cross-linker density are poorly understood. Here, we use theory and computer simulations to study the friction between two filaments that are cross-linked by passive proteins, which can hop between discrete binding sites while physically excluding each other.

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Article Synopsis
  • Transiently crosslinked actin filament networks offer a unique combination of stiffness and flexibility, enabling cells to adapt under stress.
  • Current research examines the stress relaxation timescale of these networks in relation to the dynamics of crosslinkers that bind the filaments together.
  • Findings reveal that the unbinding rate of crosslinkers—indicating how quickly they detach from the actin filaments—is significantly slower than previously thought, and this behavior is explained by a model considering different binding states of the crosslinkers.
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Biochemical reactions are fundamentally noisy at a molecular scale. This limits the precision of reaction networks, but it also allows fluctuation measurements that may reveal the structure and dynamics of the underlying biochemical network. Here, we study nonequilibrium reaction cycles, such as the mechanochemical cycle of molecular motors, the phosphorylation cycle of circadian clock proteins, or the transition state cycle of enzymes.

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