Anillin propels myosin-independent constriction of actin rings

Ondřej Kučera, Valerie Siahaan, Daniel Janda, Sietske H. Dijkstra, Eliška Pilátová, Eva Zatecka, Stefan Diez, Marcus Braun () and Zdenek Lansky ()
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Ondřej Kučera: Czech Academy of Sciences, BIOCEV, Vestec
Valerie Siahaan: Czech Academy of Sciences, BIOCEV, Vestec
Daniel Janda: Czech Academy of Sciences, BIOCEV, Vestec
Sietske H. Dijkstra: Czech Academy of Sciences, BIOCEV, Vestec
Eliška Pilátová: Czech Academy of Sciences, BIOCEV, Vestec
Eva Zatecka: Czech Academy of Sciences, BIOCEV, Vestec
Stefan Diez: B CUBE – Center for Molecular Bioengineering, TU Dresden
Marcus Braun: Czech Academy of Sciences, BIOCEV, Vestec
Zdenek Lansky: Czech Academy of Sciences, BIOCEV, Vestec

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: Abstract Constriction of the cytokinetic ring, a circular structure of actin filaments, is an essential step during cell division. Mechanical forces driving the constriction are attributed to myosin motor proteins, which slide actin filaments along each other. However, in multiple organisms, ring constriction has been reported to be myosin independent. How actin rings constrict in the absence of motor activity remains unclear. Here, we demonstrate that anillin, a non­motor actin crosslinker, indispensable during cytokinesis, autonomously propels the contractility of actin bundles. Anillin generates contractile forces of tens of pico-Newtons to maximise the lengths of overlaps between bundled actin filaments. The contractility is enhanced by actin disassembly. When multiple actin filaments are arranged into a ring, this contractility leads to ring constriction. Our results indicate that passive actin crosslinkers can substitute for the activity of molecular motors to generate contractile forces in a variety of actin networks, including the cytokinetic ring.

Date: 2021
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DOI: 10.1038/s41467-021-24474-1

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