Dresden 2014 – wissenschaftliches Programm

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CPP: Fachverband Chemische Physik und Polymerphysik

CPP 33: Cytoskeleton (original: BP, joined by CPP)

CPP 33.4: Vortrag

Mittwoch, 2. April 2014, 10:30–10:45, HÜL 386

Correlations in the random hydrolysis model of actin filaments and microtubules — •Thomas Niedermayer and Reinhard Lipowsky — Max Planck Institute of Colloids and Interfaces, Potsdam, Germany

The polymerization (assembly) and depolymerization (disassembly) of actin filaments and microtubules are pivotal for cell motility, cell adhesion, and cell division. These dynamic processes are controlled by analogous mechanisms: Actin monomers can bind ATP or ADP, whereas tubulin dimers bind either GTP or GDP. In both cases, the hydrolysis of the bound ATP/GTP within the filaments increases the subunit dissociation rate and thereby couples to the stochastic dynamics of filament growth and shrinkage. In the widely discussed random hydrolysis model, which appropriately describes actin and microtubule dynamics in vitro, the hydrolysis rate is identical at each filament subunit. We studied this model by a novel theoretical approach and stochastic simulations. While mean field solutions, which are considered in the recent literature, fail to describe the filament dynamics in physiologically relevant cases, our analytical approach matches the simulations, as it accounts for correlation effects.