Anillin propels myosin-independent constriction of actin rings

0550571 - BTÚ 2022 RIV GB eng J - Článek v odborném periodiku
Kučera, Ondřej - Siahaan, Valerie - Janda, Daniel - Dijkstra, Sietske H. - Pilátová, Eliška - Žatecká, Eva - Diez, S. - Braun, Marcus - Lánský, Zdeněk
Anillin propels myosin-independent constriction of actin rings.
Nature Communications. Roč. 12, č. 1 (2021), č. článku 4595. E-ISSN 2041-1723
Grant CEP: GA MŠMT(CZ) LM2018127; GA ČR(CZ) GX19-27477X; GA ČR(CZ) GA20-04068S; GA MŠMT(CZ) ED2.1.00/19.0390; GA MŠMT(CZ) ED1.1.00/02.0109
Institucionální podpora: RVO:86652036
Klíčová slova: diffusible cross-linkers * contractile ring * f-actin * cytokinesis * filaments
Obor OECD: Biophysics
Impakt faktor: 17.694, rok: 2021
Způsob publikování: Open access
https://www.nature.com/articles/s41467-021-24474-1

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. Cytokinetic ring constriction during cell division requires actin but curiously is independent of myosin in many organisms. Here, the authors show that anillin, a protein enriched in the contractile ring, is a non-motor actin crosslinker that generates contractile force in lieu of a molecular motor.
Trvalý link: http://hdl.handle.net/11104/0328901