Anillin propels myosin-independent constriction of actin rings

J 2021

Anillin propels myosin-independent constriction of actin rings

KUCERA, Ondrej; Valerie SIAHAAN; Daniel JANDA; Sietske H DIJKSTRA; Eliska PILATOVA et al.

Základní údaje

Originální název

Anillin propels myosin-independent constriction of actin rings

Autoři

KUCERA, Ondrej; Valerie SIAHAAN; Daniel JANDA; Sietske H DIJKSTRA; Eliska PILATOVA; Eva ZATECKA; Stefan DIEZ; Marcus BRAUN a Zdenek LANSKY

Vydání

Nature Communications, Berlin, Nature, 2021, 2041-1723

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10601 Cell biology

Stát vydavatele

Německo

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 17.694

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:90043/21:00139234

Organizační jednotka

CIISB

Klíčová slova anglicky

DIFFUSIBLE CROSS-LINKERS; CONTRACTILE RINGF-ACTIN; CYTOKINESIS; FILAMENTS; LINKING; PROTEIN; STABILIZATION; MICROTUBULES; SUBSTRATE

Štítky

ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 29. 3. 2025 15:11, Mgr. Eva Dubská

Anotace

V originále

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.

Návaznosti

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

KUCERA, Ondrej; Valerie SIAHAAN; Daniel JANDA; Sietske H DIJKSTRA; Eliska PILATOVA; Eva ZATECKA; Stefan DIEZ; Marcus BRAUN a Zdenek LANSKY. Anillin propels myosin-independent constriction of actin rings. Nature Communications. Berlin: Nature, 2021, roč. 12, č. 1, s. 1-12. ISSN 2041-1723. Dostupné z: https://doi.org/10.1038/s41467-021-24474-1.

@article{2487404,
   author = {Kucera, Ondrej and Siahaan, Valerie and Janda, Daniel and Dijkstra, Sietske H and Pilatova, Eliska and Zatecka, Eva and Diez, Stefan and Braun, Marcus and Lansky, Zdenek},
   article_location = {Berlin},
   article_number = {1},
   doi = {https://doi.org/10.1038/s41467-021-24474-1},
   keywords = {DIFFUSIBLE CROSS-LINKERS; CONTRACTILE RINGF-ACTIN; CYTOKINESIS; FILAMENTS; LINKING; PROTEIN; STABILIZATION; MICROTUBULES; SUBSTRATE},
   language = {eng},
   issn = {2041-1723},
   journal = {Nature Communications},
   title = {Anillin propels myosin-independent constriction of actin rings},
   url = {https://www.nature.com/articles/s41467-021-24474-1},
   volume = {12},
   year = {2021}
}

TY  - JOUR
ID  - 2487404
AU  - Kucera, Ondrej - Siahaan, Valerie - Janda, Daniel - Dijkstra, Sietske H - Pilatova, Eliska - Zatecka, Eva - Diez, Stefan - Braun, Marcus - Lansky, Zdenek
PY  - 2021
TI  - Anillin propels myosin-independent constriction of actin rings
JF  - Nature Communications
VL  - 12
IS  - 1
SP  - 1-12
EP  - 1-12
PB  - Nature
SN  - 20411723
KW  - DIFFUSIBLE CROSS-LINKERS
KW  - CONTRACTILE RINGF-ACTIN
KW  - CYTOKINESIS
KW  - FILAMENTS
KW  - LINKING
KW  - PROTEIN
KW  - STABILIZATION
KW  - MICROTUBULES
KW  - SUBSTRATE
UR  - https://www.nature.com/articles/s41467-021-24474-1
N2  - 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.
ER  -

KUCERA, Ondrej; Valerie SIAHAAN; Daniel JANDA; Sietske H DIJKSTRA; Eliska PILATOVA; Eva ZATECKA; Stefan DIEZ; Marcus BRAUN a Zdenek LANSKY. Anillin propels myosin-independent constriction of actin rings. \textit{Nature Communications}. Berlin: Nature, 2021, roč.~12, č.~1, s.~1-12. ISSN~2041-1723. Dostupné z: https://doi.org/10.1038/s41467-021-24474-1.

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