ArticleNature communications2021
Anillin propels myosin-independent constriction of actin rings.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Myosin II-independent contraction of actin filaments in membrane nanotubes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Three types of actomyosin rings within a common cytoplasm exhibit distinct modes of contractility.Molecular biology of the cell · 2025Article
- Three types of actomyosin rings within a common cytoplasm exhibit distinct modes of contractility.bioRxiv : the preprint server for biology · 2025Article
- Actin organizes chromosomes and microtubules to ensure mitotic fidelity in the preimplantation embryo.Science (New York, N.Y.) · 2025Article
- ANLN promotes head and neck squamous cell carcinoma progression by upregulating PD-L1 via the ERK-MAPK pathway.iScience · 2025Article
- Deciphering Mechanochemical Influences of Emergent Actomyosin Crosstalk Using QCM-D.Cellular and molecular bioengineering · 2025Article
- Identification of novel molecular subtypes and construction of a prognostic signature via multi-omics analysis and machine learning in lung adenocarcinoma.Frontiers in oncology · 2025Article
- Mechanisms and therapeutic potential of disulphidptosis in cancer.Cell proliferation · 2025Review
- The role of ANLN in malignant tumors: pathogenesis, treatment resistance and targeted strategies.Frontiers in cell and developmental biology · 2025Review
- Measuring emergent mechanical changes in cytoskeletal ensemblesFrontiers in cell and developmental biology · 2025Article
- Benefits and challenges of reconstituting the actin cortex.Cytoskeleton (Hoboken, N.J.) · 2024Review
- Self-organized spatial targeting of contractile actomyosin rings for synthetic cell division.Nature communications · 2024Article
- Deciphering Mechanochemical Influences of Emergent Actomyosin Crosstalk using QCM-D.bioRxiv : the preprint server for biology · 2024Article
- Two Septin complexes mediate actin dynamics during cell wound repair.Cell reports · 2024Article
- Triggered contraction of self-assembled micron-scale DNA nanotube rings.Nature communications · 2024Article
- CKAP5 enables formation of persistent actin bundles templated by dynamically instable microtubules.Current biology : CB · 2024Article
- Dynamic remodeling of actin networks by cyclase-associated protein and CAP-Abp1 complexes.Current biology : CB · 2023Article
- Anillin forms linear structures and facilitates furrow ingression after septin and formin depletion.Cell reports · 2023Article
- The Rho1 GTPase controls anillo-septin assembly to facilitate contractile ring closure during cytokinesis.iScience · 2023Article
- Coordinated efforts of different actin filament populations are needed for optimal cell wound repair.Molecular biology of the cell · 2023Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
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 non-motor 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.
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