Author
Listed:
- Ondřej Kučera
(Czech Academy of Sciences, BIOCEV, Vestec
Commissariat à l’énergie atomique et aux énergies alternatives (CEA))
- 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
Max Planck Institute of Molecular Cell Biology and Genetics
Cluster of Excellence Physics of Life, Technische Universität Dresden)
- Marcus Braun
(Czech Academy of Sciences, BIOCEV, Vestec)
- Zdenek Lansky
(Czech Academy of Sciences, BIOCEV, Vestec)
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.
Suggested Citation
Ondřej Kučera & Valerie Siahaan & Daniel Janda & Sietske H. Dijkstra & Eliška Pilátová & Eva Zatecka & Stefan Diez & Marcus Braun & Zdenek Lansky, 2021.
"Anillin propels myosin-independent constriction of actin rings,"
Nature Communications, Nature, vol. 12(1), pages 1-12, December.
Handle:
RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24474-1
DOI: 10.1038/s41467-021-24474-1
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