Eliška Pilátová
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Eliška Pilátová has a total of 8 co-authors. Here are the top co-authors by number of shared publications:
- Daniel Janda
Institute of Biotechnology of the Czech Academy of Sciences
1 shared publication - Eva Zatecka
Laboratory of Reproductive Biology, Institute of Biotechnology, Czech Academy of Sciences, BIOCEV, Vestec, Czech Republic
1 shared publication - Marcus Braun
Institute of Biotechnology, Czech Academy of Sciences, BIOCEV, Prague, Czechia
1 shared publication - Ondřej Kučera
Bioelectrodynamics Research Team, Institute of Photonics and Electronics of the Czech Academy of Sciences, Prague, Czechia
1 shared publication - Sietske H. Dijkstra
Institute of Biotechnology of the Czech Academy of Sciences
1 shared publication - Stefan Diez
B CUBE – Center for Molecular Bioengineering TUD Dresden University of Technology Dresden Germany
1 shared publication
Latest Publications
- Open Access
- 23 January 2020
- Published by Cold Spring Harbor Laboratory in bioRxiv
Anillin propels myosin-independent constriction of actin rings
Constriction of the actin cytokinetic ring 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, localising to 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-generated forces maximising the overlap lengths between the filaments. Actin disassembly promoted constriction. We propose that actin crosslinkers, generating forces complementary to molecular motors, contribute to the contractility of diverse actin structures, including the cytokinetic ring.
- 23 January 2020
- Published by Cold Spring Harbor Laboratory in bioRxiv
Open AccessAnillin propels myosin-independent constriction of actin rings
Constriction of the actin cytokinetic ring 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, localising to 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-generated forces maximising the overlap lengths between the filaments. Actin disassembly promoted constriction. We propose that actin crosslinkers, generating forces complementary to molecular motors, contribute to the contractility of diverse actin structures, including the cytokinetic ring.