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BP: Fachverband Biologische Physik

BP 17: Poster Session II

BP 17.53: Poster

Dienstag, 18. März 2025, 18:00–20:30, P4

Processivity of myosin assemblies: ATP dependence and effect on network dynamics — •Jaskaran Singh and Stefan Klumpp — University of Göttingen, Institute for the Dynamics of Complex Systems, Göttingen,Germany

Motors proteins like myosin, kinesin are a major source of activity in cellular mechanisms like cell division and perform tasks such as maintaining cellular structure and transporting cargo within the cell. These motors form complexes of multiple motors and cooperate and give rise to complex behaviors not seen in single-motor dynamics. Myosin motors form medium sized (~100 motors) assemblies called myosin minifilaments that bind to and move along actin filaments. The mechano-chemical cycle of individual motors in the motor assembly is dependent on ATP. We are exploring the concentration of ATP as a control parameter for the processivity (walking distance) of myosin minifilaments through stochastic modelling. Here we propose processivity as a parameter to tune the activity in system. On the cellular scale, we explore the effect of processivity on cytoskeletal network structures at large. Preliminary results show that decrease in ATP concentration increases the processivity of myosin assemblies. However, the velocity of motor assembly decreases with decreasing ATP. Thus, an optimal trade-off between processivity and velocity must be maintained for efficient assembly performance. To study the effect of processivity on network level structures, we use the simulation package Cytosim. The simulation shows that higher processivity leads to a more pronounced contraction of the actin network.

Keywords: Molecular Motor; Stochastic Modelling; Myosin; Actin; Processivity