Characterization of anillin mutants reveals essential roles in septin localization and plasma membrane integrity
Open accessAbstract
Anillin is a conserved component of the contractile ring that is essential for cytokinesis, and physically interacts with three conserved cleavage furrow proteins, F-actin, myosin II and septins in biochemical assays. We demonstrate that the Drosophila scraps gene, identified as a gene involved in cellularization, encodes Anillin. We characterize defects in cellularization, pole cell formation and cytokinesis in a series of maternal effect and zygotic anillin alleles. Mutations that result in amino acid changes in the C-terminal PH domain of Anillin cause defects in septin recruitment to the furrow canal and contractile ring. These mutations also strongly perturb cellularization, altering the timing and rate of furrow ingression. They cause dramatic vesiculation of new plasma membranes, and destabilize the stalk of cytoplasm that normally connects gastrulating cells to the yolk mass. A mutation closer to the N terminus blocks separation of pole cells with less effect on cellularization, highlighting mechanistic differences between contractile processes. Cumulatively, our data point to an important role for Anillin in scaffolding cleavage furrow components, directly stabilizing intracellular bridges, and indirectly stabilizing newly deposited plasma membrane during cellularization.
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Anillin is delivered to the CCF where it normally binds to both Myosin II and Septin.
“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 [20]
Septin binds to Anillin and is important for its function during mitosis.
“Septin binds to Anillin and is important for its function during mitosis [20].”
From Tumor Treating Fields Perturb the Localization of Septins and Cause Aberrant Mitotic Exit (2015) · cites this paper as [20]
Anillin is required for Septin localization to mitotic structures.
“whereas Anillin is required for Septin localization to mitotic structures [20]”
From Tumor Treating Fields Perturb the Localization of Septins and Cause Aberrant Mitotic Exit (2015) · cites this paper as [20]
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- Authors
- Field, C. M., Coughlin, M., Doberstein, S., Marty, T., & Sullivan, W.
- Affiliations
- Harvard University (US)
- Five Prime Therapeutics (United States) (US)
- Howard Hughes Medical Institute (US)
- Department of Molecular, Cell and Developmental Biology, Sinsheimer Laboratory, University of Santa Cruz, Santa Cruz, CA 95064, USA
- Corresponding author
- Field, Christine M.
- Venue
- Development
- Publisher
- The Company of Biologists
- Published
- 2005-06-15
- Volume
- 132
- Issue
- 12
- Pages
- 2849-2860
- ISSN
- 0950-1991 (ISSN-L)
- 1477-9129
- OpenAlex
- W1973720620
- Cited by
- 156
- References
- 44
- Citations by year
- 2026: 2 · 2025: 9 · 2024: 7 · 2023: 5 · 2022: 9 · 2021: 8 · 2020: 8 · 2019: 6 · 2018: 11 · 2017: 3 · 2016: 9 · 2015: 10 · 2014: 7 · 2013: 8 · 2012: 7
- FWCI
- 3.40
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Development (publishedVersion)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- National Institutes of Health (5r25gm058903-20)
- National Institute of General Medical Sciences (GM 23928, GM 58903, R01GM023928)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- anillin, septins, cleavage furrow, contractile ring, cytokinesis, cellularization, plasma membrane integrity, pleckstrin homology domain, Drosophila, furrow ingression, membrane vesiculation, gastrulation
- MeSH terms
- Actins, Alleles, Amino Acid Sequence, Animals, Cell Membrane, Cell Nucleus, Contractile Proteins, Cytoskeletal Proteins, Drosophila melanogaster, Humans, Molecular Sequence Data, Mutation, Zygote, Sequence Alignment, Gene Expression Regulation, Developmental, Drosophila Proteins, Microscopy, Electron, Transmission, Cytokinesis
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