Amoeboid T lymphocytes require the septin cytoskeleton for cortical integrity and persistent motility
Open accessAbstract
The systems that refine actomyosin forces during motility remain poorly understood. Septins assemble on the T-cell cortex and are enriched at the mid-zone in filaments. Septin knockdown causes membrane blebbing, excess leading-edge protrusions and lengthening of the trailing-edge uropod. The associated loss of rigidity permits motility, but cells become uncoordinated and poorly persistent. This also relieves a previously unrecognized restriction to migration through small pores. Pharmacologically rigidifying cells counteracts this effect, and relieving cytoskeletal rigidity synergizes with septin depletion. These data suggest that septins tune actomyosin forces during motility and probably regulate lymphocyte trafficking in confined tissues.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The septin complex forms filaments associated with the microtubule cytoskeleton during interphase and diffuses within the cytoplasm upon cell rounding and microtubule de-polymerization.
“The septin complex forms filaments associated with the microtubule cytoskeleton during interphase [51, 52] and diffuses within the cytoplasm upon cell rounding and microtubule de-polymerization (not shown).”
From Tumor Treating Fields Perturb the Localization of Septins and Cause Aberrant Mitotic Exit (2015) · cites this paper as [52]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Two Distinct Actin Networks Drive the Protrusion of Migrating Cells
Ponti, A., Macháček, M., Gupton, S. L., Waterman, C. M., & Danuser, G. M. (2004) · Science · doi:10.1126/science.1100533 · Cited by 820 · cited 1× · see citing works
“A thin and uniform septin network prevents blebs at the leading edge where actin and myosin are highly dynami”
Divergent Signals and Cytoskeletal Assemblies Regulate Self-Organizing Polarity in Neutrophils
Xu, J., Wang, F., Keymeulen, A. V., Herzmark, P., Straight, A. F., Kelly, K., Takuwa, Y., Sugimoto, N., Mitchison, T. J., & Bourne, H. R. (2003) · Cell · doi:10.1016/s0092-8674(03)00555-5 · Cited by 687 · cited 1× · see citing works
“2) in the specific loss of septins 1, 6, and 9 when these were targeted by shRNA.”
Non-equilibration of hydrostatic pressure in blebbing cells
Charras, G., Yarrow, J. C., Horton, M. A., Mahadevan, L., & Mitchison, T. J. (2005) · Nature · doi:10.1038/nature03550 · Cited by 657 · see citing works
Leukocyte polarization in cell migration and immune interactions
Sánchez‐Madrid, F., & del Pozo, M. A. (1999) · The EMBO Journal · doi:10.1093/emboj/18.3.501 · Cited by 615 · cited 1× · see citing works
“This morphology is required for efficient migration within lymph nodes and peripheral tissues, for crossing barriers to enter new tissues and for their reactivity to antigen-bearing AP”
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 · see citing works
Self-citationStructural insight into filament formation by mammalian septins
Sirajuddin, M., Farkasovsky, M., Hauer, F., Kühlmann, D., Macara, I. G., Weyand, M., Stark, H., & Wittinghofer, A. (2007) · Nature · doi:10.1038/nature06052 · Cited by 481 · cited 1× · see citing works
“A recently reported crystal structure of complexed septins indicates that the essential subunit of septin superstructures is a linear hexamer of septin 2–septin 6–septin 7 with a 2:2:2 stoichiometr”
Takizawa, P. A., DeRisi, J. L., Wilhelm, J. E., & Vale, R. D. (2000) · Science · doi:10.1126/science.290.5490.341 · Cited by 440 · cited 1× · see citing works
“The Septin ring around the cytokinetic furrow in yeast functions as a diffusion barrier, maintaining cell fate determinants in the appropriate cell11,12.”
Andrew, N., & Insall, R. H. (2007) · Nature Cell Biology · doi:10.1038/ncb1536 · Cited by 378 · cited 1× · see citing works
“Large numbers of protrusions extending in many directions may allow cells to better survey their environments, and Dictyostelium have evolved to select certain protrusions, rather than restrict their initial numbe”
Snapper, S. B., Takeshima, F., Anton, I. M., Liu, C.-H., Thomas, S. Μ., Nguyen, D. D., Dudley, D. D., Fraser, H. B., Purich, D. L., Lopez-Ilasaca, M. A., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1001-897 · Cited by 332 · cited 1× · see citing works
“Their migration is characterized by actin polymerization at the leading edge ‘pseudopod’2–4, and myosin IIA-based contraction, predominantly away from the leading edge5.”
The pathobiology of the septin gene family
Hall, P. A., & Russell, S. H. (2004) · The Journal of Pathology · doi:10.1002/path.1654 · Cited by 323 · cited 1× · see citing works
“Since septin expression is frequently altered in human and mouse tumors22,36,37 and Sept2 (Diff6) was first identified as an over-expressed gene in a tumor line selected for metastasis38, we speculate that destabilization of the cell cortex due to stoichiometric changes in septin complexes may…”
Barral, Y., Mermall, V., Mooseker, M. S., & Snyder, M. P. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80324-x · Cited by 322 · cited 1× · see citing works
“MSF (MLL septin-like fusion), a fusion partner gene of MLL, in a therapy-related acute myeloid leukemia with a t(11;17) (q23;q25).”
Genetic analysis of the mitotic transmission of minichromosomes
Koshland, D. E. (1985) · Cell · doi:10.1016/0092-8674(85)90153-9 · Cited by 304 · cited 1× · see citing works
“Septins were first identified as cell division cycle (cdc) mutant”
Ihara, M., Kinoshita, A., Yamada, S., Tanaka, H., Tanigaki, A., Kitano, A., Goto, M., Okubo, K., Nishiyama, H., Ogawa, O., et al. (2005) · Developmental Cell · doi:10.1016/j.devcel.2004.12.005 · Cited by 294 · cited 1× · see citing works
“Since their identification in mammals, septins have been shown to play important roles in many cell types, including neurons, platelets, and spermatozoa 16– 18.”
Self-citationRole of Septin Cytoskeleton in Spine Morphogenesis and Dendrite Development in Neurons
Tada, T., Simonetta, A., Batterton, M. N., Kinoshita, M., Edbauer, D., & Sheng, M. (2007) · Current Biology · doi:10.1016/j.cub.2007.09.039 · Cited by 284 · see citing works
Self-citationThe Mammalian Septin MSF Localizes with Microtubules and Is Required for Completion of Cytokinesis
Surka, M. C., Tsang, C. W., & Trimble, W. S. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-01-0042 · Cited by 266 · cited 1× · see citing works
“As septins are known to form heteromeric complexes23–26, we looked for septin complexes in lysates from D10 T cells.”
Self-citationPhosphorylation-Dependent Regulation of Septin Dynamics during the Cell Cycle
Dobbelaere, J., Gentry, M. S., Hallberg, R. L., & Barral, Y. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00061-3 · Cited by 259 · cited 1× · see citing works
“We hypothesize that the dynamic turnover of actomyosin filaments and their short length may be complemented by the stays of long septin filaments which are probably stable over time31,32.”
A Mitotic Septin Scaffold Required for Mammalian Chromosome Congression and Segregation
Spiliotis, E. T., Kinoshita, M., & Nelson, W. J. (2005) · Science · doi:10.1126/science.1106823 · Cited by 256 · cited 1× · see citing works
“This result was specific for septin 7 knockdown ( septin 7 KD ), as the reciprocal was not observed when other septins were targeted, supporting the hypothesis that septin 7 is crucial for septin assembl”
Self-citationThe Role of Cdc42p GTPase-activating Proteins in Assembly of the Septin Ring in Yeast
Caviston, J. P., Longtine, M. S., Pringle, J. R., & Bi, E. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-04-0247 · Cited by 248 · see citing works
G protein–independent Ras/PI3K/F-actin circuit regulates basic cell motility
Sasaki, A. T., Janetopoulos, C., Lee, S. D., Charest, P. G., Takeda, K., Sundheimer, L. W., Meili, R., Devreotes, P. N., & Firtel, R. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611138 · Cited by 227 · cited 4× · see citing works
“Some of the polarity circuits restricting leading edge extensions to the pseudopods and retraction to the uropod are likely Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.c…”
InfluentialSome assembly required: yeast septins provide the instruction manual
Versele, M., & Thorner, J. W. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.06.007 · Cited by 227 · see citing works
A single class II myosin modulates T cell motility and stopping, but not synapse formation
Jacobelli, J., Chmura, S. A., Buxton, D. B., et al. (2004) · Nature Immunology · doi:10.1038/ni1065 · Cited by 211 · see citing works
Self-citationKremer, B. E., Haystead, T., & Macara, I. G. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-03-0267 · Cited by 208 · see citing works
Expression profiling the human septin gene family
Hall, P. A., Jung, K., Hillan, K. J., & Russell, S. H. (2005) · The Journal of Pathology · doi:10.1002/path.1789 · Cited by 195 · cited 1× · see citing works
“This RNA expression pattern is consistent with expression profiling of human septin”
WAVE2 deficiency reveals distinct roles in embryogenesis and Rac‐mediated actin‐based motility
Yan, C., Martinez‐Quiles, N., Eden, S., Shibata, T., Takeshima, F., Shinkura, R., Fujiwara, Y., Bronson, R., Snapper, S. B., Kirschner, M. W., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg350 · Cited by 186 · see citing works
Nagata, K., Kawajiri, A., Matsui, S., Takagishi, M., Shiromizu, T., Saitoh, N., Izawa, I., Kiyono, T., Itoh, T. J., Hotani, H., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m205246200 · Cited by 186 · cited 1× · see citing works
“Although septin knockdown causes cell division defects in other system”
Actin and Septin Ultrastructures at the Budding Yeast Cell Cortex
Rodal, A. A., Kozubowski, L., Goode, B. L., Drubin, D. G., & Hartwig, J. H. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0734 · Cited by 182 · cited 1× · see citing works
“Septins are cytoskeletal proteins that polymerize to form rings and gauze”
Kinoshita, M. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.12.005 · Cited by 174 · cited 1× · see citing works
“Septins were first identified as cell division cycle (cdc) mutants8 in yeast and assemble into concentric filaments at the mother-bud neck during cell division (reviewed in 9,10).”
Self-citationOsaka, M., Rowley, J. D., & Zeleznik‐Le, N. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6428 · Cited by 172 · see citing works
Field, C. M., Coughlin, M., Doberstein, S., Marty, T., & Sullivan, W. (2005) · Development · doi:10.1242/dev.01843 · Cited by 156 · cited 1× · see citing works
“Indeed, septins interact with anillin, which, before cell division, is associated with the nuclear envelop”
WASP deficiency leads to global defects of directed leukocyte migration in vitro and in vivo
Snapper, S. B., Meelu, P., Nguyen, D. D., Stockton, B. M., Bozza, P. T., Alt, F. W., Rosen, F. S., von Andrian, U. H., & Klein, C. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.0804444 · Cited by 152 · cited 1× · see citing works
“Their migration is characterized by actin polymerization at the leading-edge 'pseudopod”
Biochemical and Cell Biological Analyses of a Mammalian Septin Complex, Sept7/9b/11
Nagata, K., Asano, T., Nozawa, Y., & Inagaki, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406153200 · Cited by 146 · see citing works
Montagna, C., Lyu, M. S., Hunter, K. W., Lukes, L., Lowther, W. J., Reppert, T., Hissong, B. D., Weaver, Z., & Ried, T. (2003) · PubMed · Cited by 142 · see citing works
A prototypic platelet septin and its participation in secretion
Dent, J. A., Kato, K., Peng, X., Martı́nez, C., Cattaneo, M., Poujol, C., Nurden, P., Nurden, A. T., Trimble, W. S., & Ware, J. L. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052715199 · Cited by 129 · cited 1× · see citing works
“Since their identification in mammals, septins have been shown to play important roles in many cell types, including neurons, platelets, and spermatozoa 16– 18.”
Self-citationMicrotubule retraction into the uropod and its role in T cell polarization and motility
Ratner, S., Sherrod, W. S., & Lichlyter, D. J. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.159.3.1063 · Cited by 121 · see citing works
Do septins have a role in cancer?
Russell, S. E. H., & Hall, P. A. (2005) · British Journal of Cancer · doi:10.1038/sj.bjc.6602753 · Cited by 90 · cited 1× · see citing works
“Since septin expression is frequently altered in human and mouse tumors22,36,37 and Sept2 (Diff6) was first identified as an over-expressed gene in a tumor line selected for metastasis38, we speculate that destabilization of the cell cortex due to stoichiometric changes in septin complexes may…”
Lymphocyte HEV adhesion variants differ in the expression of multiple gene sequences
Nottenburg, C., Gallatin, W. M., & John, T. S. (1990) · Gene · doi:10.1016/0378-1119(90)90372-x · Cited by 49 · cited 1× · see citing works
“, and septin 1 ( Diff6 ) was first identified as an overexpressed gene in a tumour line selected for metastasi”
Sørensen, A. B., Lund, A. H., Ethelberg, S., et al. (2000) · Journal of Virology · doi:10.1128/jvi.74.5.2161-2168.2000 · Cited by 41 · cited 1× · see citing works
“Additionally, the septin 9 locus is a site of frequent retroviral insertion, leading to generation of T-cell lymphoma”
T cell synapse assembly: proteins, motors and the underlying cell biology
Tooley, A. J., Jacobelli, J., MOLDOVAN, M., et al. (2004) · Seminars in Immunology · doi:10.1016/j.smim.2004.09.006 · Cited by 16 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Actin cortex mechanics and cellular morphogenesis
Salbreux, G., Charras, G., & Paluch, E. K. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.07.001 · Cited by 871 · see citing works
Septins: the fourth component of the cytoskeleton
Mostowy, S., & Cossart, P. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3284 · Cited by 801 · see citing works
Mechanical modes of ‘amoeboid’ cell migration
Lämmermann, T., & Sixt, M. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.05.003 · Cited by 669 · see citing works
Use the force: membrane tension as an organizer of cell shape and motility
Diz-Muñoz, A., Fletcher, D. A., & Weiner, O. D. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.09.006 · Cited by 574 · see citing works
Breaching multiple barriers: leukocyte motility through venular walls and the interstitium
Nourshargh, S., Hordijk, P. L., & Sixt, M. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2889 · Cited by 561 · see citing works
“Of interest, septin deficiency is associated with loss of cortical stability and the ability of T cells to migrate through small pores, suggesting an important role for the septin cytoskeleton in cortical rigidity and cell migration through confined tissue”
Planar Cell Polarity Acts Through Septins to Control Collective Cell Movement and Ciliogenesis
Kim, S. K., Shindo, A., Park, T. J., Oh, E. C. T., Ghosh, S., Gray, R. S., Lewis, R. A., Johnson, C. A., Attié‐Bitach, T., Katsanis, N., et al. (2010) · Science · doi:10.1126/science.1191184 · Cited by 348 · see citing works
Biomechanical regulation of contractility: spatial control and dynamics
Levayer, R., & Lecuit, T. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.10.001 · Cited by 324 · see citing works
Septins promote F-actin ring formation by crosslinking actin filaments into curved bundles
Mavrakis, M., Azou, Y., Tsai, F., Alvarado, J., Bertin, A., Iv, F., Kress, A., Brasselet, S., Koenderink, G. H., & Lecuit, T. (2014) · Nature Cell Biology · doi:10.1038/ncb2921 · Cited by 234 · see citing works
Distinct roles of septins in cytokinesis: SEPT9 mediates midbody abscission
Estey, M. P., Di Ciano-Oliveira, C., Froese, C. D., Bejide, M. T., & Trimble, W. S. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201006031 · Cited by 231 · see citing works
Self-citationMicron-scale plasma membrane curvature is recognized by the septin cytoskeleton
Bridges, A. A., Jentzsch, M. S., Oakes, P. W., Occhipinti, P., & Gladfelter, A. S. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201512029 · Cited by 236 · see citing works
Tumor Treating Fields Perturb the Localization of Septins and Cause Aberrant Mitotic Exit
Gera, N., Yang, A., Holtzman, T. S., Lee, S. X., Wong, E. T., & Swanson, K. D. (2015) · PLOS ONE · doi:10.1371/journal.pone.0125269 · Cited by 217 · see citing works
“The septin complex forms filaments associated with the microtubule cytoskeleton during interphase [51, 52] and diffuses within the cytoplasm upon cell rounding and microtubule de-polymerization (not shown).”
Septin-Mediated Uniform Bracing of Phospholipid Membranes
Tanaka-Takiguchi, Y., Kinoshita, M., & Takiguchi, K. (2009) · Current Biology · doi:10.1016/j.cub.2008.12.030 · Cited by 203 · see citing works
Self-citationSeptin assemblies form by diffusion-driven annealing on membranes
Bridges, A. A., Zhang, H., Mehta, S. B., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314138111 · Cited by 195 · see citing works
Cancer Dissemination—Lessons from Leukocytes
Madsen, C. D., & Sahai, E. A. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.06.013 · Cited by 194 · see citing works
Deciphering the rules governing assembly order of mammalian septin complexes
Sellin, M. E., Sandblad, L., Stenmark, S., & Gullberg, M. H. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-03-0253 · Cited by 187 · see citing works
“…septins, SEPT3, SEPT5, and SEPT7, seems contradictory to our data and to previous studies in which immunoprecipitation of individual septins from mouse brain or mammalian cell lines was shown to result in coprecipitation of every other septin (Kinoshita et al., 2002; Tooley et al., 2009).”
Septin functions in organ system physiology and pathology
Dolat, L., Hu, Q., & Spiliotis, E. T. (2013) · Biological Chemistry · doi:10.1515/hsz-2013-0233 · Cited by 187 · see citing works
“In T cells, septins localize to the middle of the cell cortex and are distinctly absent from the protruding pseudopod and uropod (Tooley et al., 2009).”
Bringing up the rear: defining the roles of the uropod
Sánchez‐Madrid, F., & Serrador, J. M. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2680 · Cited by 174 · see citing works
The multiple faces of leukocyte interstitial migration
Lämmermann, T., & Germain, R. N. (2014) · Seminars in Immunopathology · doi:10.1007/s00281-014-0418-8 · Cited by 169 · see citing works
Founounou, N., Loyer, N., & Borgne, R. L. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.01.008 · Cited by 169 · see citing works
Microtubules Regulate Migratory Polarity through Rho/ROCK Signaling in T Cells
Takesono, A., Heasman, S. J., Wojciak-Stothard, B., Garg, R., & Ridley, A. J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008774 · Cited by 170 · see citing works
“MT depolymerization has previously been reported to induce bleb-based migration in neutrophils [57] and bleb-like protrusions in the KE-37 T-ALL cell line in suspension [58,59] or in a mouse T cell line in agarose [60], but its effects on chemokine-stimulated T cell migration or migratory polarity have not previously…”
Septin Form and Function at the Cell Cortex
Bridges, A. A., & Gladfelter, A. S. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.634444 · Cited by 146 · see citing works
“ments on the rigidity or composition of the plasma membrane (1, 60).”
Cellular functions of actin- and microtubule-associated septins
Spiliotis, E. T., & Νάκος, Κ. (2021) · Current Biology · doi:10.1016/j.cub.2021.03.064 · Cited by 145 · see citing works
Tabdanov, E. D., Rodríguez-Merced, N. J., Cartagena‐Rivera, A. X., Puram, V. V., Callaway, M. K., Ensminger, E. A., Pomeroy, E. J., Yamamoto, K., Lahr, W. S., Webber, B. R., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22985-5 · Cited by 142 · see citing works
“Indeed, although flat 2D systems can have great utility for studying T cell motility (Krummel et al., 2016; Tooley et al., 2009), they lack the capacity”
Septins promote stress fiber–mediated maturation of focal adhesions and renal epithelial motility
Dolat, L., Hunyara, J. L., Bowen, J. R., Karasmanis, E. P., Elgawly, M., Galkin, V. E., & Spiliotis, E. T. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201405050 · Cited by 131 · see citing works
“Previous studies have implicated septins in the amoeboid motility of T cells and neuronal migration (Tooley et al., 2009; Shinoda et al., 2010), which are mechanistically different from the stress fiber–driven mode of mesenchymal migration.”
DeNucci, C. C., Mitchell, J. S., & Shimizu, Y. (2009) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.v29.i2.10 · Cited by 131 · see citing works
Ageta‐Ishihara, N., Miyata, T., Ohshima, C., Watanabe, M., Sato, Y., Hamamura, Y., Higashiyama, T., Mazitschek, R., Bito, H., & Kinoshita, M. (2013) · Nature Communications · doi:10.1038/ncomms3532 · Cited by 130 · see citing works
Self-citationThe emerging functions of septins in metazoans
Saarikangas, J., & Barral, Y. (2011) · EMBO Reports · doi:10.1038/embor.2011.193 · Cited by 129 · see citing works
“…membrane Ciliary membrane Basal body Mother Spindle pole body Phagosome Huang et al, 2008 Kissel et al, 2005 Estey et al, 2010 Buser et al, 2009 Tooley et al, 2009 Tada et al, 2007 Hu et al, 2010 Mostowy et al, 2010 Yeast bud neck Septins Spermatozoa annulus Cytokinetic furrow Node of Ranvier…”
Ghossoub, R., Hu, Q., Failler, M., Rouyez, M.-C., Spitzbarth, B., Mostowy, S., Wolfrum, U., Saunier, S., Cossart, P., Nelson, W. J., et al. (2013) · Journal of Cell Science · doi:10.1242/jcs.111377 · Cited by 128 · see citing works
“SiRNAtargeted depletion of SEPT9 affected SEPT9 levels but not those of SEPT2 or SEPT7 (see also Tooley et al., 2009; Estey et al., 2010; Sellin et al., 2011), and resulted in little or no effect on ciliogenesis, although the primary cilia were shorter.”
Septin filaments exhibit a dynamic, paired organization that is conserved from yeast to mammals
DeMay, B. S., Bai, X., Howard, L., Occhipinti, P., Meseroll, R. A., Spiliotis, E. T., Oldenbourg, R., & Gladfelter, A. S. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201012143 · Cited by 122 · see citing works
“JCB: Article”
Actomyosin Cortical Mechanical Properties in Nonadherent Cells Determined by Atomic Force Microscopy
Cartagena‐Rivera, A. X., Logue, J. S., Waterman, C. M., et al. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.04.034 · Cited by 123 · see citing works
Pointing in the right direction: new developments in the field of planar cell polarity
Bayly, R. D., & Axelrod, J. D. (2011) · Nature Reviews Genetics · doi:10.1038/nrg2956 · Cited by 122 · see citing works
“, a family of proteins that provide resilience to the plasma membrane and increase the overall structural integrity of the cel”
Cell and Molecular Biology of Septins
Fung, K., Dai, L., & Trimble, W. S. (2014) · International review of cytology · doi:10.1016/b978-0-12-800180-6.00007-4 · Cited by 118 · see citing works
Self-citationControl of cortical rigidity by the cytoskeleton: Emerging roles for septins
Gilden, J. K., & Krummel, M. F. (2010) · Cytoskeleton · doi:10.1002/cm.20461 · Cited by 119 · see citing works
“…assemble along the cortex of amoeboid T cells in a collar-like distribution that bridges the region between the cell body and the trailing uropod [Tooley et al., 2009]. shRNA knockdown of septin complexes in T-cells resulted in dramatic increases in cortical protrusions and blebbing, elongation…”
InfluentialSelf-citationThe septin cytoskeleton facilitates membrane retraction during motility and blebbing
Gilden, J. K., Peck, S., M. Chen, Y.-C., & Krummel, M. F. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201105127 · Cited by 113 · see citing works
“This appears at odds with the observation that the majority of septin aggregates are present along the T cell uropod (Tooley et al., 2009).”
InfluentialSelf-citationMenon, M., Sawada, A., Chaturvedi, A., Mishra, P., Schuster-Gossler, K., Galla, M., Schambach, A., Gossler, A., Förster, R., Heuser, M., et al. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004558 · Cited by 105 · see citing works
“Further, mitosis is completely unaffected in T lymphocytes depleted for the pivotal subunit SEPT7 [20].”
Self-citationSeptin/anillin filaments scaffold central nervous system myelin to accelerate nerve conduction
Patzig, J., Erwig, M. S., Tenzer, S., Kusch, K., Dibaj, P., Möbius, W., Goebbels, S., Schaeren‐Wiemers, N., Nave, K., & Werner, H. B. (2016) · eLife · doi:10.7554/elife.17119 · Cited by 99 · see citing works
“The formation of myelin septin filaments is a late stage of myelin maturation, thereby avoiding that the property of septins to rigidify the membranes they are associated with (Gilden and Krummel, 2010; Tooley et al., 2009) could hinder the normal developmental ensheathment of axons.”
Connolly, D., Abdesselam, I., Verdier‐Pinard, P., & Montagna, C. (2011) · Biological Chemistry · doi:10.1515/bc.2011.073 · Cited by 99 · see citing works
Huth, J., Buchholz, M., Kraus, J. M., Schmücker, M., von Wichert, G., Krndija, D., Seufferlein, T. T. W., Gress, T. M., & Kestler, H. A. (2010) · BMC Cell Biology · doi:10.1186/1471-2121-11-24 · Cited by 93 · see citing works
“In the developed organism, cell motility is critical in processes such as wound healing, which requires fibroblasts and keratinocytes to migrate into wound sites [3,4], or the immune response, which involves extensive migratory activity of immune cells to and from lymphoid tissues and distant sites of infection [5-8].”
Septin Dynamics Are Essential for Exocytosis
Tokhtaeva, E., Capri, J., Marcus, E. A., Whitelegge, J. P., Khuzakhmetova, V. F., Bukharaeva, E. A., Deiss‐Yehiely, N., Dada, L. A., Sachs, G. M., Fernández‐Salas, E., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.616201 · Cited by 83 · see citing works
Submembranous septins as relatively stable components of actin‐based membrane skeleton
Hagiwara, A., Tanaka, Y., Hikawa, R., Morone, N., Kusumi, A., Kimurâ, H., & Kinoshita, M. (2011) · Cytoskeleton · doi:10.1002/cm.20528 · Cited by 79 · see citing works
“Relatively stable cortical septin assemblies found in diverse species may lend structural rigidity to the cell cortex against mechanical stress, perhaps in conjunction with nonmuscle myosin II and other cortical components [Joo et al., 2007; Huang et al., 2008; Tooley et al., 2009; Gilden and Krummel, 2010].”
InfluentialSelf-citationSpatial Guidance of Cell Asymmetry: Septin GTP ases Show the Way
Spiliotis, E. T., & Gladfelter, A. S. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01268.x · Cited by 78 · see citing works
“In moving T cells, septins localize to the middle zone of the plasma membrane, where they suppress the formation of blebs and protrusions (50).”
InfluentialRegulation of microtubule organization and functions by septin GTPases
Spiliotis, E. T. (2010) · Cytoskeleton · doi:10.1002/cm.20448 · Cited by 71 · see citing works
“In support of these possibilities, septins are required for both asymmetric furrow ingression and cell motility [Chacko et al., 2005; Maddox et al., 2007; Hu et al., 2008; Tooley et al., 2009].”
Membrane binding controls ordered self-assembly of animal septins
Szuba, A., Bano, F., Castro-Linares, G., Iv, F., Mavrakis, M., Richter, R. P., Bertin, A., & Koenderink, G. H. (2021) · eLife · doi:10.7554/elife.63349 · Cited by 70 · see citing works
“regions of the cell cortex, where they influence the rigidity and contractility of the actin-myosin cortex 46 within single cells [25-27] and within multicellular tissues [28-30].”
InfluentialSwanson, K. D., Lok, E., & Wong, E. T. (2016) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-015-0606-5 · Cited by 65 · see citing works
CDC42EP5/BORG3 modulates SEPT9 to promote actomyosin function, migration, and invasion
Farrugia, A. J., Rodríguez, J., Orgaz, J. L., et al. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201912159 · Cited by 66 · see citing works
“In addition, septins form a uniform network at the cell cortex in leukocytes, and SEPT7 expression is required for rapid cortical contraction during dynamic shape changes (Gilden et al., 2012; Tooley et al., 2009).”
Microtubules support a disk-like septin arrangement at the plasma membrane of mammalian cells
Sellin, M. E., Holmfeldt, P., Stenmark, S., & Gullberg, M. H. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-09-0754 · Cited by 63 · see citing works
Transfection of choanoflagellates illuminates their cell biology and the ancestry of animal septins
Booth, D. S., Szmidt, H. L., & King, N. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-08-0514 · Cited by 61 · see citing works
Mammalian septins: dynamic heteromers with roles in cellular morphogenesis and compartmentalization
Hall, P. A., & Russell, S. H. (2011) · The Journal of Pathology · doi:10.1002/path.3024 · Cited by 58 · see citing works
Estey, M. P., Kim, M. S., & Trimble, W. S. (2011) · Current Biology · doi:10.1016/j.cub.2011.03.067 · Cited by 58 · see citing works
Self-citationHuman septins organize as octamer-based filaments and mediate actin-membrane anchoring in cells
Martins, C. S., Taveneau, C., Castro-Linares, G., Baibakov, M., Buzhinsky, N., Eroles, M., Milanović, V., Omi, S., Pédelacq, J. D., Iv, F., et al. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202203016 · Cited by 54 · see citing works
“…1995; Finger et al., 2003; Gilden et al., 2012; Ihara et al., 2005; Kim et al., 2010; Kissel et al., 2005; Kuo et al., 2012; Mostowy et al., 2010; Mostowy et al., 2011; Nguyen et al., 2000; Shindo and Wallingford, 2014; Steels et al., 2007; Tada et al., 2007; Tooley et al., 2009; Xie et al., 2007).”
Mastrogiovanni, M., Juzans, M., Alcover, A., & Bartolo, V. D. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.591348 · Cited by 59 · see citing works
Finnigan, G. C., Booth, E. A., Duvalyan, A., Liao, E. N., & Thorner, J. W. (2015) · Genetics · doi:10.1534/genetics.115.176503 · Cited by 55 · see citing works
“Similarly, septin function has been implicated in the amoeboid motility of T cells by promoting membrane retraction (Tooley et al. 2009; Gilden et al. 2012).”
Masters of asymmetry – lessons and perspectives from 50 years of septins
Spiliotis, E. T., & McMurray, M. A. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-11-0648 · Cited by 56 · see citing works
“, uropodia, filopodia, cilia) that underlie the morphogenesis of distinct cell types and tissues and arise from local membrane asymmetries, microdomains of distinct protein enrichment (Caudron and Barral, 2009; Tooley et al., 2009; Hu et al., 2010, 2012; Dolat et al., 2014a).”
Non-recurrent SEPT9 duplications cause hereditary neuralgic amyotrophy
Collie, A. M. B., Landsverk, M., Ruzzo, E. K., et al. (2009) · Journal of Medical Genetics · doi:10.1136/jmg.2009.072348 · Cited by 54 · see citing works
“SEPT9 is a member of the large family of septin proteins that interact with the cytoskeleton, including microtubules and actin, functioning in cellular processes such as cytokinesis, motility and cell polarity.(14) SEPT9 produces multiple mRNA transcripts through alternative 59 splicing.”
Ptpn21 Controls Hematopoietic Stem Cell Homeostasis and Biomechanics
Ni, F., Yu, W., Wang, X., Fay, M. E., Young, K. M., Qiu, Y., Lam, W. A., Sulchek, T., Cheng, T., Scadden, D. T., et al. (2019) · Cell stem cell · doi:10.1016/j.stem.2019.02.009 · Cited by 55 · see citing works
“Septin1 caught our attention also because Septins have been newly recognized as important components of the cytoskeleton, and they play a critical role in actin filament organization, regulating the mechanical properties of the cell (Gilden et al., 2012; Mavrakis et al., 2014; Mostowy and Cossart, 2012; Tooley et al.,…”
Septin C-Terminal Domain Interactions: Implications for Filament Stability and Assembly
Marques, I. A., Valadares, N. F., García, W., et al. (2011) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-011-9307-0 · Cited by 51 · see citing works
Pan, S., Zhan, Y., Chen, X., Wu, B., & Liu, B. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01101 · Cited by 50 · see citing works
“Septins are cytoskeletal proteins that provide compression and rigidity and support efficient motion of motile T cells (36).”
Listeria monocytogenesMembrane Trafficking and Lifestyle: The Exception or the Rule?
Pizarro‐Cerdá, J., & Cossart, P. (2009) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.042308.113331 · Cited by 50 · see citing works
Yoon, S., Kim, Y. K., Han, E. D., et al. (2012) · Lab on a Chip · doi:10.1039/c2lc40084g · Cited by 48 · see citing works
Finnigan, G. C., Takagi, J., Cho, C., & Thorner, J. W. (2015) · Genetics · doi:10.1534/genetics.115.176495 · Cited by 47 · see citing works
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 45 · see citing works
Beise, N., & Trimble, W. S. (2011) · Journal of Cell Science · doi:10.1242/jcs.087007 · Cited by 45 · see citing works
“Interestingly, decreases in septin-mediated membrane bracing does not block motility, but cells become poorly persistent and uncoordinated (Tooley et al., 2009).”
Self-citationRegulation of mechanotransduction: Emerging roles for septins
Lam, M. S. Y., & Calvo, F. (2018) · Cytoskeleton · doi:10.1002/cm.21485 · Cited by 43 · see citing works
“…a similar degree as when F-actin is reduced (Mostowy et al., 2011); septins stabilize the cell cortex of T lymphocytes (Gilden, Peck, Chen, & Krummel, 2012); and cells without septins experience dramatic membrane blebbing due to a soft and unstable cortex (Gilden et al., 2012; Tooley et al., 2008).”
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 · see citing works
“G4 cell line and observed that septin depletion had no effect on the proliferation of these cells (Tooley et al., 2009).”
Obeidy, P., Ju, L. A., Oehlers, S. H., et al. (2019) · Immunology and Cell Biology · doi:10.1111/imcb.12304 · Cited by 41 · see citing works
“This increased the transmigration and chemotaxis capacity and reduced the migration speed.(8) In our study, we report that reduction in Arp3 levels in primary cytotoxic T cells triggers formation of bleb protrusions.”
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 40 · see citing works
Self-citationUncovering the Roles of Septins in Cilia
Palander, O., El-Zeiry, M., & Trimble, W. S. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00036 · Cited by 40 · see citing works
“…binding of septins to membranes has been shown to promote membrane tubulation in vitro (Tanaka-Takiguchi et al., 2009), promote the retraction of blebs from the cell membrane (Gilden et al., 2012) and stabilize the plasma membrane to allow directed cell migration in T cells (Tooley et al., 2009).”
Self-citationNovel Functions of the Septin Cytoskeleton
Ivanov, A. I., Le, H. T., Naydenov, N. G., & Rieder, F. (2020) · American Journal Of Pathology · doi:10.1016/j.ajpath.2020.09.007 · Cited by 40 · see citing works
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 · see citing works
Hernández-Rodríguez, Y., Masuo, S., Johnson, D., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092819 · Cited by 39 · see citing works
Dynamics of dendritic cell–T cell interactions: a role in T cell outcome
Hugues, S. (2010) · Seminars in Immunopathology · doi:10.1007/s00281-010-0211-2 · Cited by 39 · see citing works
“Other data suggest that septins tune actomyosin forces act during motility and regulate T cell trafficking in confined tissues [56].”
Cdc42 regulates Cdc42EP3 function in cancer-associated fibroblasts
Farrugia, A. J., & Calvo, F. (2016) · Small GTPases · doi:10.1080/21541248.2016.1194952 · Cited by 39 · see citing works
Wasik, A. A., Dumont, V., Tienari, J., et al. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2016.12.010 · Cited by 38 · see citing works
Role of septins in microbial infection
Ngo, H. V., & Mostowy, S. (2019) · Journal of Cell Science · doi:10.1242/jcs.226266 · Cited by 37 · see citing works
Lymphocyte egress signal sphingosine-1-phosphate promotes ERM-guided, bleb-based migration
Robertson, T. F., Chengappa, P., Gómez, D., et al. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202007182 · Cited by 37 · see citing works
“One candidate group of proteins is the septins, which also constrain blebbing and regulate migratory behavior (Gilden et al., 2012; Tooley et al., 2009).”
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 38 · see citing works
Physical view on migration modes
Mierke, C. T. (2015) · Cell Adhesion & Migration · doi:10.1080/19336918.2015.1066958 · Cited by 34 · see citing works
“…REVIEW aspects of the actomyosin networks or the mechanical impact of other cytoskeletal elements such as actin-crosslinkers, or intermediate filaments such as vimentin are still less well investigated and elusive (Brown et al. 2001; Laevsky and Knecht, 2003; Tooley et al. 2008; Xu et al., 2008).”
Østevold, K., Meléndez, A. V., Lehmann, F., Schmidt, G., Aktories, K., & Schwan, C. (2017) · Oncotarget · doi:10.18632/oncotarget.20805 · Cited by 34 · see citing works
“While several studies showed that septins are involved in cell migration [55, 57, 58], their precise roles are not entirely clear.”
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 33 · see citing works
“…as scaffolds for the localization of cell cycle proteins, facilitate cytokinesis, and contribute to cell migration [Bi et al., 1998; Barral et al., 1999; Barral et al., 2000; Longtine et al., 2000; Takizawa et al., 2000; Longtine and Bi, 2003; Dobbelaere and Barral, 2004; Tooley et al., 2009].”
The last-born daughter cell contributes to division orientation of Drosophila larval neuroblasts
Loyer, N., & Januschke, J. (2018) · Nature Communications · doi:10.1038/s41467-018-06276-0 · Cited by 32 · see citing works
The actin‐driven spatiotemporal organization of T‐cell signaling at the system scale
Roybal, K. T., Sinai, P., Verkade, P., Murphy, R. F., & Wülfing, C. (2013) · Immunological Reviews · doi:10.1111/imr.12103 · Cited by 30 · see citing works
“in T-cell migration (16, 17) and during asymmetric cell division (18, 19), as well as in virtually every other cell type (20–22).”
Cdc42-Borg4-Septin7 axis regulates HSC polarity and function
Kandi, R., Senger, K., Grigoryan, A., Soller, K., Sakk, V., Schuster, T., Eiwen, K., Menon, M. B., Gaestel, M., Zheng, Y., et al. (2021) · EMBO Reports · doi:10.15252/embr.202152931 · Cited by 31 · see citing works
A Clockwork Bleb: cytoskeleton, calcium, and cytoplasmic fluidity
Ikenouchi, J., & Aoki, K. (2021) · FEBS Journal · doi:10.1111/febs.16220 · Cited by 29 · see citing works
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 · see citing works
Self-citationWang, Y., Jeong, Y., Jhiang, S. M., Yu, L., & Menq, C.-H. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098762 · Cited by 27 · see citing works
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 27 · see citing works
Insights into the Mechanism for Dictating Polarity in Migrating T-Cells
Niggli, V. (2014) · International review of cytology · doi:10.1016/b978-0-12-800178-3.00007-5 · Cited by 25 · see citing works
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 26 · see citing works
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 26 · see citing works
“78 Septins assemble along the cell cortex, providing a scaffolding structure.”
Septin-regulated actin dynamics promoteSalmonellainvasion of host cells
Boddy, K. C., Gao, A. D., Truong, D., Kim, M. S., Froese, C. D., Trimble, W. S., & Brumell, J. H. (2018) · Cellular Microbiology · doi:10.1111/cmi.12866 · Cited by 25 · see citing works
“used as a tool to disrupt the septin cytoskeleton, since it is essential for stability of other septins (Tooley et al., 2009).”
Self-citationSeptins are critical regulators of osteoclastic bone resorption
Møller, A. M. J., Füchtbauer, E., Brüel, A., Andersen, T. L., Borggaard, X. G., Pavlos, N. J., Thomsen, J. S., Pedersen, F. S., Delaissé, J., & Søe, K. (2018) · Scientific Reports · doi:10.1038/s41598-018-31159-1 · Cited by 24 · see citing works
Merlini, L., Bolognesi, A., Juanes, M. A., Vandermoere, F., Courtellemont, T., Pascolutti, R., Sevéno, M., Barral, Y., & Piatti, S. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-06-0366 · Cited by 23 · see citing works
“In migrating cell types such as T-lymphocytes, septins form an annular corset at the cell cortex to rigidify the cell periphery, protect it against mechanical stress, and promote the persistence of migration (Tooley et al., 2009).”
Zhong, J., Ding, R., Jiang, H., Li, L., Wan, J., Feng, X., Chen, M., Peng, L., Li, X., Lin, J., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1081889 · Cited by 22 · see citing works
Park, T. J., Kim, S. K., & Wallingford, J. B. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.11.078 · Cited by 22 · see citing works
“Wdpcp is an effector of PCP signaling, which is generally considered to act via Rho and Rho Kinase to organize the actin cytoskeleton [15; 27; 28; 29].”
InfluentialThe mechanobiology of NK cells- ‘Forcing NK to Sense’ target cells
Wong, D. C. P., & Ding, J. L. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188860 · Cited by 20 · see citing works
Vial, A., Taveneau, C., Costa, L., Chauvin, B., Nasrallah, H., Godefroy, C., Dosset, P., Isambert, H., Ngo, K. X., Mangenot, S., et al. (2021) · Nanoscale · doi:10.1039/d1nr01978c · Cited by 20 · see citing works
Zhovmer, A. S., Manning, A., Smith, C., Nguyen, A., Prince, O., Sáez, P. J., Ma, X., Tsygankov, D., Cartagena‐Rivera, A. X., Singh, N. A., et al. (2024) · Science Advances · doi:10.1126/sciadv.adi1788 · Cited by 18 · see citing works
“Previous reports show that septins participate in the formation of contractile actomyosin rings during cytokinesis, indicating a possible link between septins and amoeboid migration ( 13 , 17 ).”
InfluentialZeraik, A. E., Galkin, V. E., Rinaldi, G., Garratt, R. C., Smout, M. J., Loukas, A. C., Mann, V. H., de Araújo, A. P. U., Demarco, R. C., & Brindley, P. J. (2014) · International Journal for Parasitology · doi:10.1016/j.ijpara.2014.03.010 · Cited by 19 · see citing works
“It has been postulated that septin filaments function as a molecular corset, providing rigidity at the cell cortex to support efficient motion of T cells and that septin might tune actomyosin forces during motility (Tooley et al., 2008).”
Formin like 1 expression is increased on CD4+ T lymphocytes in spontaneous autoimmune uveitis
Degroote, R. L., Uhl, P., Amann, B., Krackhardt, A. M., Ueffing, M., Hauck, S. M., & Deeg, C. A. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2016.12.015 · Cited by 19 · see citing works
Septin9 is involved in T-cell development and CD8+ T-cell homeostasis
Lassen, L. B., Füchtbauer, A. C., Schmitz, A., Sørensen, A. B., Pedersen, F. S., & Füchtbauer, E. (2013) · Cell and Tissue Research · doi:10.1007/s00441-013-1618-6 · Cited by 19 · see citing works
- Authors
- Tooley, A. J., Gilden, J., Jacobelli, J., Beemiller, P., Trimble, W. S., Kinoshita, M., & Krummel, M. F.
- Affiliations
- University of California, San Francisco (US)
- University of Toronto (CA)
- Kyoto University (JP)
- Corresponding author
- Krummel, Matthew F.
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2008-11-30
- Volume
- 11
- Issue
- 1
- Pages
- 17-26
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC3777658
- OpenAlex
- W2054984177
- Semantic Scholar
- 6ed6b435479e9e2c1b789d6891832a8c3c07559f
- Cited by
- 189
- References
- 38
- Citations by year
- 2026: 11 · 2025: 1 · 2024: 5 · 2023: 11 · 2022: 11 · 2021: 12 · 2020: 8 · 2019: 7 · 2018: 13 · 2017: 10 · 2016: 14 · 2015: 14 · 2014: 16 · 2013: 9 · 2012: 10
- FWCI
- 5.25
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Science Foundation
- Leukemia and Lymphoma Society
- National Institute of Allergy and Infectious Diseases (R21AI062899, R01AI052116)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- septins, T cell migration, cell motility, cell cortex, actomyosin force, membrane blebbing, uropod, lymphocyte migration, pore migration
- MeSH terms
- Actins, Animals, Cell Membrane, Cell Movement, Cells, Cultured, Chemotaxis, Leukocyte, Cytoskeletal Proteins, Cytoskeleton, Mice, Transgenic, Myosins, Stress, Mechanical, T-Lymphocytes, Down-Regulation, GTP Phosphohydrolases, Cell Surface Extensions, RNA Interference, Cell Shape, 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
