Cited by 526Microtubule and mitosis dynamicsCellular Mechanics and InteractionsProtein Kinase Regulation and GTPase Signaling

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Self- and Actin-Templated Assembly of Mammalian Septins

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Kinoshita, Makoto, Field, Christine M., Coughlin, Margaret L., Straight, Aaron F., Mitchison, Timothy J.·2002·Developmental Cell

DOI 10.1016/s1534-5807(02)00366-0

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Abstract

Septins are polymerizing GTPases required for cytokinesis and cortical organization. The principles by which they are targeted to, and assemble at, specific cell regions are unknown. We show that septins in mammalian cells switch between a linear organization along actin bundles and cytoplasmic rings, approximately 0.6 microm in diameter. A recombinant septin complex self-assembles into rings resembling those in cells. Linear organization along actin bundles was reconstituted by adding an adaptor protein, anillin. Perturbation of septin organization in cells by expression of a septin-interacting fragment of anillin or by septin depletion via siRNA causes loss of actin bundles. We conclude that septins alone self-assemble into rings, that adaptor proteins recruit septins to actin bundles, and that septins help organize these bundles.

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[18] Purification of muscle actin
Pardee, J. D., & Aspudich, J. (1982) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(82)85020-9 · Cited by 1,190
RNA interference by expression of short-interfering RNAs and hairpin RNAs in mammalian cells
Yu, J., DeRuiter, S. L., & Turner, D. L. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092143499 · Cited by 1,041
Anillin, a contractile ring protein that cycles from the nucleus to the cell cortex.
Field, C. M., & Alberts, B. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.1.165 · Cited by 440
A highly ordered ring of membrane-associated filaments in budding yeast.
Byers, B., & Goetsch, L. (1976) · The Journal of Cell Biology · doi:10.1083/jcb.69.3.717 · Cited by 420
Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures.Preprint
Kinoshita, M., Kumar, S., Mizoguchi, A., Idé, C., Kinoshita, A., Haraguchi, T., Hiraoka, Y., & Noda, M. (1997) · Genes & Development · doi:10.1101/gad.11.12.1535 · Cited by 380
Self-citation
The septin CDCrel-1 binds syntaxin and inhibits exocytosis
Beites, C. L., Xie, H., Bowser, R. P., & Trimble, W. S. (1999) · Nature Neuroscience · doi:10.1038/8100 · Cited by 377
The Drosophila peanut gene is required for cytokinesis and encodes a protein similar to yeast putative bud neck filament proteins
Neufeld, T. P. (1994) · Cell · doi:10.1016/0092-8674(94)90152-x · Cited by 360
Subunit Composition, Protein Interactions, and Structures of the Mammalian Brain sec6/8 Complex and Septin Filaments
Hsu, S.-C., Hazuka, C. D., Roth, R. A., Foletti, D. L., Heuser, J., & Scheller, R. H. (1998) · Neuron · doi:10.1016/s0896-6273(00)80493-6 · Cited by 358
The septin cortex at the yeast mother–bud neck
Gladfelter, A. S. (2001) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(01)00269-7 · Cited by 331
A purified Drosophila septin complex forms filaments and exhibits GTPase activity.
Field, C. M., Al-Awar, O. S., Rosenblatt, J., Wong, M., Alberts, B., & Mitchison, T. J. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.133.3.605 · Cited by 326

Show all 36 references

Research works printed but not linked: 1

Field, 1999, The contractile ring anillin is essential for cell division-associated contractile events in the early Drosophila embryo, Mol. Biol. Cell. Suppl., 10, 239a

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Maimaitiyiming, M., Kumanogoh, H., Nakamura, S., Nagata, K., Suzaki, T., & Maékawa, S. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05450.x · Cited by 9
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Authors: Kinoshita, M., Field, C. M., Coughlin, M. L., Straight, A. F., & Mitchison, T. J.
Affiliations: Harvard University (US)
Corresponding author: Kinoshita, Makoto
ORCID: Kinoshita, Makoto
Field, Christine M.
Straight, Aaron F.
Venue: Developmental Cell
Publisher: Elsevier BV
Published: 2002-12
Volume: 3
Issue: 6
Pages: 791-802
ISSN: 1534-5807 (ISSN-L)
DOI: 10.1016/s1534-5807(02)00366-0
OpenAlex: W2055376777
Cited by: 526
References: 36
Citations by year: 2026: 13 · 2025: 9 · 2024: 15 · 2023: 14 · 2022: 23 · 2021: 20 · 2020: 26 · 2019: 21 · 2018: 25 · 2017: 17 · 2016: 23 · 2015: 23 · 2014: 24 · 2013: 21 · 2012: 24
FWCI: 8.49
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3881 d)
Locations: Developmental Cell (publishedVersion)
PubMed (publishedVersion)
Funders: Ministério da Educação e Ciência
National Institutes of Health (GM23928)
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: septins, actin bundles, anillin, septin ring, cytokinesis, cortical organization, GTPase, adaptor proteins, actin cytoskeleton organization, mammalian cells
MeSH terms: Animals, Binding Sites, Blood Proteins, Carrier Proteins, Cell Compartmentation, Contractile Proteins, Cytoskeletal Proteins, Eukaryotic Cells, HeLa Cells, Humans, Luminescent Proteins, Actin Cytoskeleton, Recombinant Fusion Proteins, 3T3 Cells, RNA-Binding Proteins, Protein Structure, Tertiary, GTP-Binding Proteins, GTP Phosphohydrolase Activators, GTP-Binding Protein Regulators, GTP Phosphohydrolases, rho GTP-Binding Proteins, cdc42 GTP-Binding Protein, Adaptor Proteins, Signal Transducing, Green Fluorescent Proteins, Mice, Septins

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Self- and Actin-Templated Assembly of Mammalian Septins

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