Dresden 2020 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 39: Cytoskeletal Filaments II
BP 39.5: Vortrag
Freitag, 20. März 2020, 10:30–10:45, SCH A251
Anillin Propels Myosin-Independent Constriction of Actin Rings — Ondřej Kučera1, Daniel Janda1, Valerie Siahaan1, Sietske H. Dijkstra1, Eva Zatecka1, Stefan Diez2,3, •Marcus Braun1, and Zdenek Lansky1 — 1Institute of Biotechnology of the Czech Academy of Sciences, BIOCEV, Prague West, Czechia — 2B CUBE - Center for Molecular Bioengineering, Technische Universität Dresden, 01307 Dresden, Germany — 3Cluster of Excellence Physics of Life, Technische Universität Dresden, 01062 Dresden, Germany
Constriction of the cytokinetic ring, a circular structure of actin filaments, is an essential step of cell division. In a generally accepted view, the constriction is driven by relative sliding of actin filaments propelled by myosin motors. However, in multiple organisms, the ring constriction is myosin independent. How actin rings constrict in the absence of motor activity remains unclear. Here, we demonstrate that actin contractility can be propelled by anillin, a diffusible non-motor actin crosslinker, colocalising with the cytokinetic ring. We in vitro observed the formation and constriction of rings comprising multiple actin filaments bundled by anillin. Rings constricted due to anillin- driven maximisation of overlaps between the filaments. Actin disassembly promoted constriction. Optical trapping demonstrated that anillin molecules, crosslinking bundles of several actin filaments, collectively, generate forces of tens of pico-Newtons. We propose that diffusible non-motor actin crosslinkers, generating forces complementary to the activity of molecular motors, may contribute to the contractility of diverse actin structures, including the cytokinetic ring.