More ATP Does Not Equal More Contractility: Power And Remodelling In Reconstituted Actomyosin

• Published in: arXiv.org
• Main Authors: Al-Izzi, Sami C, Köster, Darius V, Morris, Richard G
• Format: Paper
• Language: English
• Published: Ithaca Cornell University Library, arXiv.org 05.04.2023
• Subjects: Actomyosin; Adenosine triphosphate; Filaments; Myosin
• ISSN: 2331-8422

The cytoskeletal component actomyosin is a canonical example of active matter since the powerstroke cycle locally converts chemical energy in the form of adenoside triphosphate (ATP) into mechanical work for remodelling. Observing myosin II minifilaments as they remodel actin {\it in vitro}, we now report that, at high concentrations of ATP, myosin minifilaments form meta-stable swirling patterns that are characterised by recurrent vortex- and spiral-like motifs, whereas at low concentrations of ATP, such structures give way to aster-like patterns. This is shown to be consistent with the (quasi-)steady states of a polar active hydrodynamic theory of actomyosin whose ATP-scaling is obtained from a microscopic description for the ATP-dependent binding statistics of the headgroups of single myosin II minifilaments. The latter codifies the heuristic that, since the powerstroke cycle involves the unbinding of myosin II headgroups from actin, increases in the concentration of ATP reduce the likelihood that a given myosin II minifilament has more than one headgroup bound simultaneously, reducing its ability to generate contractile forces and increasing the relative likelihood of processive motion. As a result, our work demonstrates how ATP not only controls the rate at which work is done -- \textit{i.e.,} the power -- but also the mode by which this occurs.