The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Anillin Binds Nonmuscle Myosin II and Regulates the Contractile Ring
Open accessAbstract
We demonstrate that the contractile ring protein anillin interacts directly with nonmuscle myosin II and that this interaction is regulated by myosin light chain phosphorylation. We show that despite their interaction, anillin and myosin II are independently targeted to the contractile ring. Depletion of anillin in Drosophila or human cultured cells results in cytokinesis failure. Human cells depleted for anillin fail to properly regulate contraction by myosin II late in cytokinesis and fail in abscission. We propose a role for anillin in spatially regulating the contractile activity of myosin II during cytokinesis.
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“Anillin is delivered to the CCF where it normally binds to both Myosin II and Septin [20, 25]”
From Tumor Treating Fields Perturb the Localization of Septins and Cause Aberrant Mitotic Exit (2015) · cites this paper as [25]
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Cites
Phosphorylation and Activation of Myosin by Rho-associated Kinase (Rho-kinase)
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Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor
Straight, A. F., Cheung, A., Limouze, J., Chen, I., Westwood, N. J., Sellers, J. R., & Mitchison, T. J. (2003) · Science · doi:10.1126/science.1081412 · Cited by 1,412
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Chapter 30 Cell Cycle Extracts
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Self- and actin-templated assembly of Mammalian septins
Kinoshita, M., Field, C. M., Coughlin, M. L., Straight, A. F., & Mitchison, T. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00366-0 · Cited by 526
Anillin, a contractile ring protein that cycles from the nucleus to the cell cortex.
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Reassembly of contractile actin cortex in cell blebs
Charras, G., Hu, C., Coughlin, M. L., & Mitchison, T. J. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200602085 · Cited by 640
Green, R. A., Paluch, E. K., & Oegema, K. (2012) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155718 · Cited by 586
Regulation of the Actin Cytoskeleton-Plasma Membrane Interplay by Phosphoinositides
Saarikangas, J., Zhao, H., & Lappalainen, P. (2010) · Physiological Reviews · doi:10.1152/physrev.00036.2009 · Cited by 515
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Metadata
- Authors
- Straight, A. F., Field, C. M., & Mitchison, T. J.
- Affiliations
- Stanford Medicine (US)
- Harvard University (US)
- Venue
- Molecular Biology of the Cell
- Published
- 2005-01
- Volume
- 16
- Issue
- 1
- Pages
- 193-201
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC539163
- OpenAlex
- W2127504108
- Cited by
- 283
- References
- 41
- Citations by year
- 2026: 3 · 2025: 9 · 2024: 8 · 2023: 10 · 2022: 14 · 2021: 13 · 2020: 16 · 2019: 14 · 2018: 11 · 2017: 15 · 2016: 16 · 2015: 11 · 2014: 13 · 2013: 13 · 2012: 13
- FWCI
- 5.10
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Biology of the Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Damon Runyon Cancer Research Foundation
- National Institute of General Medical Sciences (GM-023928, R01GM023928)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- anillin, non-muscle myosin II, contractile ring, cytokinesis, myosin light chain phosphorylation, abscission, cytokinesis failure, protein-protein interaction, Drosophila
- MeSH terms
- Amino Acid Sequence, Animals, Cell Line, Chromatography, Chromatography, Affinity, Cloning, Molecular, Contractile Proteins, Cytoskeleton, DNA, Drosophila, HeLa Cells, Humans, Interphase, Metaphase, Microscopy, Fluorescence, Molecular Sequence Data, Muscle Contraction, Myosins, Phosphorylation, Protein Binding, RNA, RNA, Double-Stranded, Xenopus laevis, Blotting, Western, Sequence Homology, Amino Acid, Myosin Type II, RNA Interference, Immunoprecipitation, Cytokinesis
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