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

The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.

Self- and Actin-Templated Assembly of Mammalian Septins

Open access

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

Open this paper in CoChat — free account Open PDF

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.

Integrity signals

Registry

Crossref · 10.1016/s1534-5807(02)00366-0

Cites

36 of 36 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

[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

Sorted by citations

Items 201–300 of 526

The WAVE complex associates with sites of saddle membrane curvature
Pipathsouk, A., Brunetti, R. M., Town, J. P., Graziano, B. R., Breuer, A., Pellett, P. A., Marchuk, K., Tran, N.-H., Krummel, M. F., Stamou, D. G., et al. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202003086 · Cited by 60
The MYO 6 interactome: selective motor‐cargo complexes for diverse cellular processes
de Jonge, J. J., Batters, C., O’Loughlin, T. A., Arden, S. D., & Buß, F. (2019) · FEBS Letters · doi:10.1002/1873-3468.13486 · Cited by 55
The MYO6 interactome reveals adaptor complexes coordinating early endosome and cytoskeletal dynamics
O’Loughlin, T. A., Masters, T. A., & Buß, F. (2018) · EMBO Reports · doi:10.15252/embr.201744884 · Cited by 55
Anillin regulates breast cancer cell migration, growth, and metastasis by non-canonical mechanisms involving control of cell stemness and differentiation
Wang, D., Naydenov, N. G., Dozmorov, M. G., Koblinski, J. E., & Ivanov, A. I. (2020) · Breast Cancer Research · doi:10.1186/s13058-019-1241-x · Cited by 53
Role of Septins in the Orientation of Forespore Membrane Extension during Sporulation in Fission Yeast
Onishi, M., Koga, T., Hirata, A., Nakamura, T., Asakawa, H., Shimoda, C., Bähler, J., Wu, J., Takegawa, K., Tachikawa, H., et al. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01529-09 · Cited by 53
Spatiotemporal association of DNAJB13 with the annulus during mouse sperm flagellum development
Guan, J., Kinoshita, M., & Yuan, L. (2009) · BMC Developmental Biology · doi:10.1186/1471-213x-9-23 · Cited by 52
Self-citation
Crystal Structure of a Schistosoma mansoni Septin Reveals the Phenomenon of Strand Slippage in Septins Dependent on the Nature of the Bound Nucleotide
Zeraik, A. E., Pereira, H. M., Santos, Y. V., Brandão-Neto, J., Spoerner, M., Santos, M. S., Colnago, L. A., Garratt, R. C., de Araújo, A. P. U., & Demarco, R. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.525352 · Cited by 50
The Borg family of Cdc42 effector proteins Cdc42EP1–5
Farrugia, A. J., & Calvo, F. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160219 · Cited by 56
The ER/PM microdomain, PI(4,5)P2 and the regulation of STIM1–Orai1 channel function
Cao, X., Choi, S., Maléth, J., Park, S., Ahuja, M., & Muallem, S. (2015) · Cell Calcium · doi:10.1016/j.ceca.2015.03.003 · Cited by 50
SEPT9_v4 expression induces morphological change, increased motility and disturbed polarity
Chacko, A. D., Hyland, P. L., McDade, S. S., Hamilton, P. W., Russell, S. H., & Hall, P. A. (2005) · The Journal of Pathology · doi:10.1002/path.1794 · Cited by 51
Platelet septin complexes form rings and associate with the microtubular network
Martı́nez, C., Corral, J., Dent, J. A., Sesma, L. G., Vicente, V., & Ware, J. L. (2006) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2006.01952.x · Cited by 51
Actin Assembly around the Shigella-Containing Vacuole Promotes Successful Infection
Kühn, S. C., Bergqvist, J., Gil, M., Valenzuela, C., Barrio, L., Lebreton, S., Zurzolo, C., & Enninga, J. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107638 · Cited by 51
An atomic model for the human septin hexamer by cryo-EM
Mendonça, D. C., Guimarães, S. L., Pereira, H. D., Pinto, A. P. A., de Farias, M. A., Godoy, A. S., de Araújo, A. P. U., van Heel, M., Portugal, R. V., & Garratt, R. C. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167096 · Cited by 49
SEPTIN12 Genetic Variants Confer Susceptibility to Teratozoospermia
Lin, Y., Wang, Y., Chen, H.-I., Kuo, Y., Chiou, Y.-W., Lin, H., Wu, C.-M., Hsu, C., Chiang, H., & Kuo, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034011 · Cited by 50
The septin cytoskeleton in myelinating glia
Buser, A., Erne, B., Werner, H. B., Nave, K., & Schaeren‐Wiemers, N. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2008.10.002 · Cited by 52
SEPT12/SPAG4/LAMINB1 Complexes Are Required for Maintaining the Integrity of the Nuclear Envelope in Postmeiotic Male Germ Cells
Yeh, C.-H., Kuo, P., Wang, Y., Wu, Y.-Y., Chen, M., Lin, D.-Y., Lai, T., Chiang, H., & Lin, Y. (2015) · PLoS ONE · doi:10.1371/journal.pone.0120722 · Cited by 55
Role of Nucleotide Binding in Septin-Septin Interactions and Septin Localization in Saccharomyces cerevisiae
Nagaraj, S., Rajendran, A., Jackson, C. E., & Longtine, M. S. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00786-08 · Cited by 49
Drosophila Orc6 Facilitates GTPase Activity and Filament Formation of the Septin Complex
Huijbregts, R. P. H., Svitin, A., Stinnett, M. W., Renfrow, M. B., & Chesnokov, I. N. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-07-0754 · Cited by 50
Coupling of septins to the axial landmark by Bud4 in budding yeast
Kang, P. J., Hood‐DeGrenier, J. K., & Park, H.-O. (2013) · Journal of Cell Science · doi:10.1242/jcs.118521 · Cited by 48
Septins Are Important for Cell Polarity, Septation and Asexual Spore Formation in Neurospora crassa and Show Different Patterns of Localisation at Germ Tube Tips
Berepiki, A., & Read, N. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063843 · Cited by 51
The final cut: cell polarity meets cytokinesis at the bud neck in S. cerevisiae
Juanes, M. A., & Piatti, S. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2220-3 · Cited by 47
Structure and function of Septin 9 and its role in human malignant tumors
Sun, J., Zheng, M., Li, Y., & Zhang, S. (2020) · World Journal of Gastrointestinal Oncology · doi:10.4251/wjgo.v12.i6.619 · Cited by 47
A theoretical model of cytokinesis implicates feedback between membrane curvature and cytoskeletal organization in asymmetric cytokinetic furrowing
Dorn, J. F., Zhang, L., Phi, T.-T., Lacroix, B., Maddox, P. S., Liu, J., & Maddox, A. S. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-06-0374 · Cited by 46
The role of septin 7 in physiology and pathological disease: A systematic review of current status
Wang, X., Fei, F., Qu, J., Li, C., Li, Y., & Zhang, S. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13623 · Cited by 46
Septins at a glance
Beise, N., & Trimble, W. S. (2011) · Journal of Cell Science · doi:10.1242/jcs.087007 · Cited by 50
The Unsolved Problem of How Cells Sense Micron-Scale Curvature
Cannon, K. S., Woods, B. L., & Gladfelter, A. S. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.10.001 · Cited by 45
Anillin is an emerging regulator of tumorigenesis, acting as a cortical cytoskeletal scaffold and a nuclear modulator of cancer cell differentiation
Naydenov, N. G., Koblinski, J. E., & Ivanov, A. I. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03605-9 · Cited by 45
Actomyosin Tube Formation in Polar Body Cytokinesis Requires Anillin in C. elegans
Dorn, J. F., Zhang, L., Paradis, V., Edoh-Bedi, D., Jusu, S., Maddox, P. S., & Maddox, A. S. (2010) · Current Biology · doi:10.1016/j.cub.2010.10.030 · Cited by 43
Regulating Contractility of the Actomyosin Cytoskeleton by pH
Köhler, S., Schmoller, K. M., Crevenna, Á. H., & Bausch, A. R. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.08.014 · Cited by 44
Mammalian SEPT9 isoforms direct microtubule-dependent arrangements of septin core heteromers
Sellin, M. E., Stenmark, S., & Gullberg, M. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-06-0486 · Cited by 47
Characterization of Mid1 domains for targeting and scaffolding in fission yeast cytokinesis
Lee, I., & Wu, J. (2012) · Journal of Cell Science · doi:10.1242/jcs.102574 · Cited by 44
Septins suppress the release of vaccinia virus from infected cells
Pfanzelter, J., Mostowy, S., & Way, M. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201708091 · Cited by 48
Regulation of mechanotransduction: Emerging roles for septins
Lam, M. S. Y., & Calvo, F. (2018) · Cytoskeleton · doi:10.1002/cm.21485 · Cited by 43
Insights into animal septins using recombinant human septin octamers with distinct SEPT9 isoforms
Iv, F., Martins, C. S., Castro-Linares, G., Taveneau, C., Barbier, P., Verdier‐Pinard, P., Camoin, L., Audebert, S., Tsai, F., Ramond, L., et al. (2021) · Journal of Cell Science · doi:10.1242/jcs.258484 · Cited by 41
PI(4,5)P2 diffuses freely in the plasma membrane even within high-density effector protein complexes
Pacheco, J. E., Cassidy, A. C., Zewe, J. P., Wills, R. C., & Hammond, G. R. V. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202204099 · Cited by 44
Septin filament coalignment with microtubules depends on SEPT9_i1 and tubulin polyglutamylation, and is an early feature of acquired cell resistance to paclitaxel
Targa, B., Klipfel, L., Cantaloube, I., Salameh, J., Benoit, B., Poüs, C., & Baillet, A. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1318-6 · Cited by 42
A complete compendium of crystal structures for the human SEPT3 subgroup reveals functional plasticity at a specific septin interface
Castro, D. K. S. D. V., da Silva, S. M. D. O., Pereira, H. M., Macêdo, J. N. A., Leonardo, D. A., Valadares, N. F., Kumagai, P. S., Brandão-Neto, J., de Araújo, A. P. U., & Garratt, R. C. (2020) · IUCrJ · doi:10.1107/s2052252520002973 · Cited by 37
PAR-4/LKB1 Mobilizes Nonmuscle Myosin through Anillin to Regulate C. elegans Embryonic Polarization and Cytokinesis
Chartier, N. T., Ospina, D. P. S., Benkemoun, L., Mayer, M., Grill, S. W., Maddox, A. S., & Labbé, J.-C. (2011) · Current Biology · doi:10.1016/j.cub.2011.01.010 · Cited by 39
Sep(t)arate or not – how some cells take septin-independent routes through cytokinesis
Menon, M., & Gaestel, M. (2015) · Journal of Cell Science · doi:10.1242/jcs.164830 · Cited by 40
3D Reconstruction of Mammalian Septin Filaments
Lukoyanova, N., Baldwin, S. A., & Trinick, J. A. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.11.029 · Cited by 42
The Drosophila Fragile X Protein dFMR1 Is Required During Early Embryogenesis for Pole Cell Formation and Rapid Nuclear Division Cycles
Deshpande, G., Calhoun, G., & Schedl, P. D. (2006) · Genetics · doi:10.1534/genetics.106.062414 · Cited by 39
Septin-microtubule association via a motif unique to isoform 1 of septin 9 tunes stress fibers
Kuzmić, M., Castro-Linares, G., Fialová, J. L., Iv, F., Salaün, D., Llewellyn, A., Gomes, M., Belhabib, M., Liu, Y., Asano, K., et al. (2021) · Journal of Cell Science · doi:10.1242/jcs.258850 · Cited by 40
Uncovering Principles That Control Septin-Septin Interactions
Kim, M. S., Froese, C. D., Xie, H., & Trimble, W. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.387464 · Cited by 43
Septin cooperation with tubulin polyglutamylation contributes to cancer cell adaptation to taxanes
Klipfel, L., Targa, B., Cantaloube, I., Ahmed-Zaïd, H., Poüs, C., & Baillet, A. (2015) · Oncotarget · doi:10.18632/oncotarget.5373 · Cited by 44
Animal Cell Cytokinesis: The Rho-Dependent Actomyosin-Anilloseptin Contractile Ring as a Membrane Microdomain Gathering, Compressing, and Sorting Machine
Carim, S. C., Kechad, A., & Hickson, G. R. X. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.575226 · Cited by 37
Cytoskeleton rearrangements during Listeria infection: Clathrin and septins as new players in the game
Mostowy, S., & Cossart, P. (2009) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20353 · Cited by 42
Borg5 is required for angiogenesis by regulating persistent directional migration of the cardiac microvascular endothelial cells
Liu, Z., Vong, Q. P., Liu, C., & Zheng, Y. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-09-0543 · Cited by 40
Cancer-Related Functions and Subcellular Localizations of Septins
Poüs, C., Klipfel, L., & Baillet, A. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00126 · Cited by 40
Cdc42 regulates Cdc42EP3 function in cancer-associated fibroblasts
Farrugia, A. J., & Calvo, F. (2016) · Small GTPases · doi:10.1080/21541248.2016.1194952 · Cited by 40
Mammalian Septin Function in Hemostasis and Beyond
Martı́nez, C., & Ware, J. L. (2004) · Experimental Biology and Medicine · doi:10.1177/153537020422901105 · Cited by 39
Guides to the final frontier of the cytoskeleton: septins in filamentous fungi
Gladfelter, A. S. (2010) · Current Opinion in Microbiology · doi:10.1016/j.mib.2010.09.012 · Cited by 39
The actin-binding and bundling protein, EPLIN, is required for cytokinesis
Oakes, V., Graham, M. E., Ma, M. P. C., Smith, C. M., Robinson, P. J., & Khanna, K. K. (2009) · Cell Cycle · doi:10.4161/cc.8.5.7878 · Cited by 38
Septins are involved in nuclear division, morphogenesis and pathogenicity in Fusarium graminearum
Chen, A., Xie, Q., Lin, Y., Xu, H., Shang, W., Zhang, J., Zhang, D., Zheng, W., Li, G., & Wang, Z. (2016) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2016.07.005 · Cited by 38
Septins as membrane influencers: direct play or in association with other cytoskeleton partners
Benoit, B., Poüs, C., & Baillet, A. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1112319 · Cited by 36
The germinal centre kinase Don3 triggers the dynamic rearrangement of higher‐order septin structures during cytokinesis in Ustilago maydis
Böhmer, C., Ripp, C., & Bölker, M. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06948.x · Cited by 38
Molecular Recognition at Septin Interfaces: The Switches Hold the Key
Rosa, H. V. D., Leonardo, D. A., Brognara, G., Brandão-Neto, J., Pereira, H. M., de Araújo, A. P. U., & Garratt, R. C. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.09.001 · Cited by 33
Src64 is involved in fusome development and karyosome formation during Drosophila oogenesis
Djagaeva, I., Doronkin, S., & Beckendorf, S. K. (2005) · Developmental Biology · doi:10.1016/j.ydbio.2005.05.012 · Cited by 36
Septin 7 is required for orderly meiosis in mouse oocytes
Li, S., Ou, X.-H., Liang, W. P., Wang, Z.-B., Zhang, Q.-H., Ouyang, Y., Hou, Y., Schatten, H., & Sun, Q. (2012) · Cell Cycle · doi:10.4161/cc.21553 · Cited by 34
The Coprinopsis cinerea septin Cc.Cdc3 is involved in stipe cell elongation
Shioya, T., Nakamura, H., Ishii, N., Takahashi, N., Sakamoto, Y., Ozaki, N., Kobayashi, M., Okano, K., Kamada, T., & Muraguchi, H. (2013) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2013.08.007 · Cited by 34
Septin remodeling is essential for the formation of cell membrane protrusions (microtentacles) in detached tumor cells
Østevold, K., Meléndez, A. V., Lehmann, F., Schmidt, G., Aktories, K., & Schwan, C. (2017) · Oncotarget · doi:10.18632/oncotarget.20805 · Cited by 34
Promiscuous interactions of human septins: The GTP binding domain of SEPT7 forms filaments within the crystal
Serrão, V. H. B., Alessandro, F., Caldas, V. E. A., Marçal, R. L., Pereira, H. M., Thiemann, O. H., & Garratt, R. C. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.10.043 · Cited by 33
Cdc42 and its BORG2 and BORG3 effectors control the subcellular localization of septins between actin stress fibers and microtubules
Salameh, J., Cantaloube, I., Benoit, B., Poüs, C., & Baillet, A. (2021) · Current Biology · doi:10.1016/j.cub.2021.07.004 · Cited by 33
Comparison of hippocampal synaptosome proteins in young-adult and aged rats
Sato, Y., Yamanaka, H., Toda, T., Shinohara, Y., & Endo, T. (2005) · Neuroscience Letters · doi:10.1016/j.neulet.2005.02.053 · Cited by 33
What Drosophila spermatocytes tell us about the mechanisms underlying cytokinesis
Giansanti, M. G., & Fuller, M. T. (2012) · Cytoskeleton · doi:10.1002/cm.21063 · Cited by 33
Cellular requirements for the small molecule forchlorfenuron to stabilize the septin cytoskeleton
DeMay, B. S., Meseroll, R. A., Occhipinti, P., & Gladfelter, A. S. (2010) · Cytoskeleton · doi:10.1002/cm.20452 · Cited by 37
Sept7bis essential for pronephric function and development of left-right asymmetry in zebrafish embryogenesis
Dash, S. N., Lehtonen, E., Wasik, A. A., Schepis, A., Paavola, J., Panula, P., Nelson, W. J., & Lehtonen, S. H. (2014) · Journal of Cell Science · doi:10.1242/jcs.138495 · Cited by 33
Septin Remodeling During Mammalian Cytokinesis
Russo, G., & Krauss, M. I. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.768309 · Cited by 31
Common mechanisms regulating cell cortex properties during cell division and cell migration
Roubinet, C., Tran, P. T., & Piel, M. (2012) · Cytoskeleton · doi:10.1002/cm.21086 · Cited by 33
Septins localize to microtubules during nutritional limitation in Saccharomyces cerevisiae
Pablo-Hernando, M. E., Arnáiz‐Pita, Y., Tachikawa, H., del Rey, F., Neiman, A. M., & de Aldana, C. R. V. (2008) · BMC Cell Biology · doi:10.1186/1471-2121-9-55 · Cited by 33
Cytoskeleton: What Does GTP Do for Septins?
Mitchison, T. J., & Field, C. M. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01295-2 · Cited by 32
A SEPT1-based scaffold is required for Golgi integrity and function
Song, K., Gras, C., Capin, G., Gimber, N., Lehmann, M., Mohd, S., Puchkov, D., Rödiger, M., Wilhelmi, I., Daumke, O., et al. (2019) · Journal of Cell Science · doi:10.1242/jcs.225557 · Cited by 33
Actomyosin-Driven Division of a Synthetic Cell
Baldauf, L., van Buren, L., Fanalista, F., & Koenderink, G. H. (2022) · ACS Synthetic Biology · doi:10.1021/acssynbio.2c00287 · Cited by 30
A Simple Method for GFP- and RFP-based Dual Color Single-Molecule Localization Microscopy
Platonova, E., Winterflood, C. M., & Ewers, H. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00046 · Cited by 35
Septin ring size scaling and dynamics require the coiled-coil region of Shs1p
Meseroll, R. A., Howard, L., & Gladfelter, A. S. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-03-0207 · Cited by 33
Septins regulate junctional integrity of endothelial monolayers
Kim, J., & Cooper, J. A. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-02-0136 · Cited by 31
Septins: New Microtubule Interacting Partners
Silverman-Gavrila, R., & Silverman‐Gavrila, L. B. (2008) · The Scientific World JOURNAL · doi:10.1100/tsw.2008.87 · Cited by 34
Importin β2 Mediates the Spatio-temporal Regulation of Anillin through a Noncanonical Nuclear Localization Signal
Chen, A., Akhshi, T. K., Lavoie, B. D., & Wilde, A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.649160 · Cited by 28
A septin-Hof1 scaffold at the yeast bud neck binds and organizes actin cables
Garabedian, M. V., Wirshing, A. C. E., Vakhrusheva, A., Turegun, B., Sokolova, O. S., & Goode, B. L. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-12-0693 · Cited by 29
Production and analysis of a mammalian septin hetero‐octamer complex
DeRose, B. T., Kelley, R. S., Ravi, R., Kokona, B., Beld, J., Spiliotis, E. T., & Padrick, S. B. (2020) · Cytoskeleton · doi:10.1002/cm.21643 · Cited by 28
Proteomic analysis of optic nerve lipid rafts reveals new paranodal proteins
Ogawa, Y., & Rasband, M. N. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.21984 · Cited by 29
A septin requirement differentiates autonomous and contact-facilitated T cell proliferation
Mujal, A. M., Gilden, J. K., Gérard, A., Kinoshita, M., & Krummel, M. F. (2015) · Nature Immunology · doi:10.1038/ni.3330 · Cited by 29
Self-citation
SEPT14 Mutations and Teratozoospermia: Genetic Effects on Sperm Head Morphology and DNA Integrity
Wang, Y.-Y., Lai, T., Chen, M.-F., Lee, H.-L., Kuo, P.-L., & Lin, Y.-H. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8091297 · Cited by 23
Probing the role of septins in cardiomyocytes
Ahuja, P., Perriard, E. R., Trimble, W. S., Perriard, J., & Ehler, E. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.01.029 · Cited by 28
Animal cell division: a fellowship of the double ring?
Saint, R. B., & Somers, W. G. (2003) · Journal of Cell Science · doi:10.1242/jcs.00816 · Cited by 28
Turning it inside out: The organization of human septin heterooligomers
McMurray, M. A., & Thorner, J. W. (2019) · Cytoskeleton · doi:10.1002/cm.21571 · Cited by 30
Developmental and postdevelopmental roles of septins in the brain
Ageta‐Ishihara, N., & Kinoshita, M. (2020) · Neuroscience Research · doi:10.1016/j.neures.2020.08.006 · Cited by 27
Self-citation
Unraveling the Equine Lymphocyte Proteome: Differential Septin 7 Expression Associates with Immune Cells in Equine Recurrent Uveitis
Degroote, R. L., Hauck, S. M., Amann, B., Hirmer, S., Ueffing, M., & Deeg, C. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0091684 · Cited by 30
The septins FaCdc3 and FaCdc12 are required for cytokinesis and affect asexual and sexual development, lipid metabolism and virulence in Fusarium asiaticum
Zhang, Y., Gao, T., Shao, W., Zheng, Z., Zhou, M., & Chen, C. (2016) · Molecular Plant Pathology · doi:10.1111/mpp.12492 · Cited by 27
Functional insight into the role of Orc6 in septin complex filament formation inDrosophila
Akhmetova, K., Balasov, M., Huijbregts, R. P. H., & Chesnokov, I. N. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-02-0734 · Cited by 27
Network Contractility during Cytokinesis—From Molecular to Global Views
Leite, J., Osório, D. S., Sobral, A. F., Silva, A. M., & Carvalho, A. X. (2019) · Biomolecules · doi:10.3390/biom9050194 · Cited by 25
Adhesion of Active Cytoskeletal Vesicles
Maan, R., Loiseau, É., & Bausch, A. R. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.10.013 · Cited by 26
Septins, a cytoskeletal protein family, with emerging role in striated muscle
Gönczi, M., Dienes, B., Dobrosi, N., Fodor, J., Balogh, N., Oláh, T., & Csernoch, L. J. (2020) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-020-09573-8 · Cited by 23
Septin7 is indispensable for proper skeletal muscle architecture and function
Gönczi, M., Ráduly, Z., Szabó, L. Z., Fodor, J., Telek, A., Dobrosi, N., Balogh, N., Szentesi, P., Kis, G. N., Antal, M., et al. (2022) · eLife · doi:10.7554/elife.75863 · Cited by 23
Mammalian septins in health and disease
Montagna, C., Weiler‐Sagie, M., & Zechmeister, J. R. (2015) · Research and Reports in Biochemistry · doi:10.2147/rrbc.s59060 · Cited by 29
SEPT12-Microtubule Complexes Are Required for Sperm Head and Tail Formation
Kuo, P., Chiang, H., Wang, Y., Kuo, Y., Chen, M., Yu, I., Teng, Y., Lin, S., & Lin, Y. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms141122102 · Cited by 26
Dynamin regulates metaphase furrow formation and plasma membrane compartmentalization in the syncytial Drosophila embryo
Rikhy, R., Mavrakis, M., & Lippincott‐Schwartz, J. (2015) · Biology Open · doi:10.1242/bio.20149936 · Cited by 25
Syndapin promotes pseudocleavage furrow formation by actin organization in the syncytialDrosophilaembryo
Sherlekar, A., & Rikhy, R. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-09-0656 · Cited by 24
Multimodal and Polymorphic Interactions between Anillin and Actin: Their Implications for Cytokinesis
Jananji, S., Risi, C. M., Lindamulage, I. K. S., Picard, L.-P., Sciver, R. E. V., Laflamme, G., Albaghjati, A., Hickson, G. R. X., Kwok, B. H. B., & Galkin, V. E. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.01.020 · Cited by 25
A versatile set of Lifeact-RFP expression plasmids for live-cell imaging of F-actin in filamentous fungi
Lichius, A., & Read, N. D. (2010) · Fungal Genetics Reports · doi:10.4148/1941-4765.1070 · Cited by 26
Suppression of centrosome duplication and amplification by deacetylases
Ling, H., Peng, L., Seto, E., & Fukasawa, K. (2012) · Cell Cycle · doi:10.4161/cc.21985 · Cited by 25

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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Self- and Actin-Templated Assembly of Mammalian Septins

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks