Synonyms
SEPT1: Septin 1; DIFF6; LARP; PNUTL3; SEP1
SEPT2: Septin 2; DIFF6; NEDD-5; NEDD5; Pnutl3; hNedd5; KIAA0158
SEPT3: Septin 3; SEP3; bK250D10.3
SEPT4: Septin 4; H5; ARTS; MART; SEP4; CE5B3; PNUTL2; hucep-7; BRADEION; hCDCREL-2
SEPT5: Septin 5; H5; CDCREL; PNUTL1; CDCREL1; CDCREL-1; HCDCREL-1
SEPT6: Septin 6; KIAA0128; MGC16619; MGC20339; SEP2
SEPT7: Septin 7; CDC3; CDC10; SEPT7A
SEPT8: Septin 8; KIAA0202; SEP2
SEPT9: Septin 9; MSF; MSF1; NAPB; SINT1; PNUTL4; SeptD1; AF17q25; KIAA0991; Ov/Br septin
SEPT10: Septin 10; FLJ11619; sept1-like
SEPT11: Septin 11; FLJ10849
SEPT12: Septin 12; FLJ25410; SPGF10
SEPT14: Septin 14; FLJ44060
Historical Background
Septins were initially identified in the budding yeast, Saccharomyces cerevisiae, as genes essential for cytoplasmic division (Hartwell 1971; Hartwell et al. 1970). While the isolation and characterization of yeast mutants with defects in cell-cycle control yielded a Nobel Prize for Leland Hartwell, septin mutants which displayed a...
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References
Abbey M, Hakim C, Anand R, Lafera J, Schambach A, Kispert A, et al. GTPase domain driven dimerization of SEPT7 is dispensable for the critical role of septins in fibroblast cytokinesis. Sci Report. 2016;6:20007. https://doi.org/10.1038/srep20007. http://www.nature.com/articles/srep20007#supplementary-information.
Ageta-Ishihara N, Miyata T, Ohshima C, Watanabe M, Sato Y, Hamamura Y, et al. Septins promote dendrite and axon development by negatively regulating microtubule stability via HDAC6-mediated deacetylation. Nat Commun. 2013;4:2532. https://doi.org/10.1038/ncomms3532.
Angelis D, Spiliotis ET. Septin mutations in human cancers. Front Cell Dev Biol. 2016;4:122. https://doi.org/10.3389/fcell.2016.00122.
Brand F, Schumacher S, Kant S, Menon MB, Simon R, Turgeon B, et al. The extracellular signal-regulated kinase 3 (mitogen-activated protein kinase 6 [MAPK6])-MAPK-activated protein kinase 5 signaling complex regulates septin function and dendrite morphology. Mol Cell Biol. 2012;32:2467–78. https://doi.org/10.1128/MCB.06633-11. [pii] MCB.06633-11.
Bridges AA, Jentzsch MS, Oakes PW, Occhipinti P, Gladfelter AS. Micron-scale plasma membrane curvature is recognized by the septin cytoskeleton. J Cell Biol. 2016;213:23–32. https://doi.org/10.1083/jcb.201512029.
Brown SD, Moore MW. The international mouse phenotyping consortium: past and future perspectives on mouse phenotyping. Mamm Genome. 2012;23:632–40. https://doi.org/10.1007/s00335-012-9427-x.
Byers B, Goetsch L. A highly ordered ring of membrane-associated filaments in budding yeast. J Cell Biol. 1976;69:717–21.
Calvo F, Ranftl R, Hooper S, Farrugia AJ, Moeendarbary E, Bruckbauer A, et al. Cdc42EP3/BORG2 and septin network enables mechano-transduction and the emergence of cancer-associated fibroblasts. Cell Rep. 2015;13:2699–714. https://doi.org/10.1016/j.celrep.2015.11.052.
Cerveira N, Bizarro S, Teixeira MR. MLL-SEPTIN gene fusions in hematological malignancies. Biol Chem. 2011;392:713–24. https://doi.org/10.1515/BC.2011.072.
Chahwan R, Gravel S, Matsusaka T, Jackson SP. Dma/RNF8 proteins are evolutionarily conserved E3 ubiquitin ligases that target septins. Cell Cycle. 2013;12:1000–8. https://doi.org/10.4161/cc.23947.
Choi P, Snyder H, Petrucelli L, Theisler C, Chong M, Zhang Y, et al. SEPT5_v2 is a parkin-binding protein. Brain Res Mol Brain Res. 2003;117:179–89.
Deb BK, Hasan G. Regulation of store-operated Ca2+ entry by septins. Front Cell Dev Biol. 2016;4:142. https://doi.org/10.3389/fcell.2016.00142.
Deb BK, Pathak T, Hasan G. Store-independent modulation of Ca(2+) entry through Orai by Septin 7. Nat Commun. 2016;7. https://doi.org/10.1038/ncomms11751.
Dent J, Kato K, Peng XR, Martinez C, Cattaneo M, Poujol C, et al. A prototypic platelet septin and its participation in secretion. Proc Natl Acad Sci USA. 2002;99:3064–9. https://doi.org/10.1073/pnas.05271519999/5/3064.
Diesenberg K, Beerbaum M, Fink U, Schmieder P, Krauss M. SEPT9 negatively regulates ubiquitin-dependent downregulation of EGFR. J Cell Sci. 2015;128:397–407. https://doi.org/10.1242/jcs.162206.
Estey MP, Di Ciano-Oliveira C, Froese CD, Bejide MT, Trimble WS. Distinct roles of septins in cytokinesis: SEPT9 mediates midbody abscission. J Cell Biol. 2010;191:741–9. https://doi.org/10.1083/jcb.201006031.
Estey MP, Di Ciano-Oliveira C, Froese CD, Fung KY, Steels JD, Litchfield DW, et al. Mitotic regulation of SEPT9 protein by cyclin-dependent kinase 1 (Cdk1) and Pin1 protein is important for the completion of cytokinesis. J Biol Chem. 2013;288:30075–86. https://doi.org/10.1074/jbc.M113.474932.
Ewers H, Tada T, Petersen JD, Racz B, Sheng M, Choquet D. A septin-dependent diffusion barrier at dendritic spine necks. PLoS One. 2014;9:e113916. https://doi.org/10.1371/journal.pone.0113916.
Founounou N, Loyer N, Le Borgne R. Septins regulate the contractility of the actomyosin ring to enable adherens junction remodeling during cytokinesis of epithelial cells. Developmental cell. 2013;24:242–55. https://doi.org/10.1016/j.devcel.2013.01.008.
Frazier JA, Wong ML, Longtine MS, Pringle JR, Mann M, Mitchison TJ, et al. Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function. J Cell Biol. 1998;143:737–49.
Fuchtbauer A, Lassen LB, Jensen AB, Howard J, Quiroga Ade S, Warming S, et al. Septin9 is involved in septin filament formation and cellular stability. Biol Chem. 2011;392:769–77. https://doi.org/10.1515/BC.2011.088.
Fujishima K, Kiyonari H, Kurisu J, Hirano T, Kengaku M. Targeted disruption of Sept3, a heteromeric assembly partner of Sept5 and Sept7 in axons, has no effect on developing CNS neurons. J Neurochem. 2007;102:77–92. https://doi.org/10.1111/j.1471-4159.2007.04478.x.
Gilden JK, Peck S, Chen YC, Krummel MF. The septin cytoskeleton facilitates membrane retraction during motility and blebbing. J Cell Biol. 2012;196:103–14. https://doi.org/10.1083/jcb.201105127.
Guillot C, Lecuit T. Adhesion disengagement uncouples intrinsic and extrinsic forces to drive cytokinesis in epithelial tissues. Dev Cell. 2013;24:227–41. https://doi.org/10.1016/j.devcel.2013.01.010.
Hartwell LH. Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis. Exp Cell Res. 1971;69:265–76.
Hartwell LH, Culotti J, Reid B. Genetic control of the cell-division cycle in yeast. I. Detection of mutants. Proc Natl Acad Sci USA. 1970;66:352–9.
Hernandez-Rodriguez Y, Momany M. Posttranslational modifications and assembly of septin heteropolymers and higher-order structures. Curr Opin Microbiol. 2012;15:660–8. https://doi.org/10.1016/j.mib.2012.09.007.
Hu Q, Milenkovic L, Jin H, Scott MP, Nachury MV, Spiliotis ET, et al. A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution. Science. 2010;329:436–9. https://doi.org/10.1126/science.1191054.
Huang YW, Yan M, Collins RF, Diciccio JE, Grinstein S, Trimble WS. Mammalian septins are required for phagosome formation. Mol Biol Cell. 2008;19:1717–26. https://doi.org/10.1091/mbc.E07-07-0641.
Ihara M, Kinoshita A, Yamada S, Tanaka H, Tanigaki A, Kitano A, et al. Cortical organization by the septin cytoskeleton is essential for structural and mechanical integrity of mammalian spermatozoa. Dev Cell. 2005;8:343–52. https://doi.org/10.1016/j.devcel.2004.12.005.
Iwaisako K, Hatano E, Taura K, Nakajima A, Tada M, Seo S, et al. Loss of Sept4 exacerbates liver fibrosis through the dysregulation of hepatic stellate cells. J Hepatol. 2008;49:768–78. https://doi.org/10.1016/j.jhep.2008.05.026.
Joberty G, Perlungher RR, Sheffield PJ, Kinoshita M, Noda M, Haystead T, et al. Borg proteins control septin organization and are negatively regulated by Cdc42. Nat Cell Biol. 2001;3:861–6. https://doi.org/10.1038/ncb1001-861ncb1001-861.
Kim SK, Shindo A, Park TJ, Oh EC, Ghosh S, Gray RS, et al. Planar cell polarity acts through septins to control collective cell movement and ciliogenesis. Science. 2010;329:1337–40. https://doi.org/10.1126/science.1191184.
Kim MS, Froese CD, Estey MP, Trimble WS. SEPT9 occupies the terminal positions in septin octamers and mediates polymerization-dependent functions in abscission. J Cell Biol. 2011;195:815–26. https://doi.org/10.1083/jcb.201106131. [pii] jcb.201106131.
Kinoshita M. The septins. Genome Biol. 2003;4:236. https://doi.org/10.1186/gb-2003-4-11-236.
Kinoshita M. Insight into septin functions from mouse models. The septins. Chichester: Wiley; 2008. p. 319–36.
Kinoshita M, Kumar S, Mizoguchi A, Ide C, Kinoshita A, Haraguchi T, et al. Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures. Genes Dev. 1997;11:1535–47.
Kissel H, Georgescu MM, Larisch S, Manova K, Hunnicutt GR, Steller H. The Sept4 septin locus is required for sperm terminal differentiation in mice. Dev Cell. 2005;8:353–64. https://doi.org/10.1016/j.devcel.2005.01.021.
Lin YH, Lin YM, Wang YY, Yu IS, Lin YW, Wang YH, et al. The expression level of septin12 is critical for spermiogenesis. Am J Pathol. 2009;174:1857–68. https://doi.org/10.2353/ajpath.2009.080955.
Liu M, Shen S, Chen F, Yu W, Yu L. Linking the septin expression with carcinogenesis. Mol Biol Rep. 2010;37:3601–8. https://doi.org/10.1007/s11033-010-0009-2.
Maddox AS, Lewellyn L, Desai A, Oegema K. Anillin and the septins promote asymmetric ingression of the cytokinetic furrow. Dev Cell. 2007;12:827–35. https://doi.org/10.1016/j.devcel.2007.02.018.
Mavrakis M, Azou-Gros Y, Tsai FC, Alvarado J, Bertin A, Iv F, et al. Septins promote F-actin ring formation by crosslinking actin filaments into curved bundles. Nat Cell Biol. 2014;16:322–34. https://doi.org/10.1038/ncb2921.
McMurray MA, Bertin A, Garcia 3rd G, Lam L, Nogales E, Thorner J. Septin filament formation is essential in budding yeast. Dev Cell. 2011;20:540–9. https://doi.org/10.1016/j.devcel.2011.02.004.
Menon MB, Gaestel M. Sep(t)arate or not – how some cells take septin-independent routes through cytokinesis. J Cell Sci. 2015;128:1877–86. https://doi.org/10.1242/jcs.164830.
Menon MB, Sawada A, Chaturvedi A, Mishra P, Schuster-Gossler K, Galla M, et al. Genetic deletion of SEPT7 reveals a cell type-specific role of septins in microtubule destabilization for the completion of cytokinesis. PLoS Genet. 2014;10:e1004558. https://doi.org/10.1371/journal.pgen.1004558.
Mostowy S, Cossart P. Septins: the fourth component of the cytoskeleton. Nat Rev Mol Cell Biol. 2012;13:183–94. https://doi.org/10.1038/nrm3284. [pii] nrm3284.
Mostowy S, Bonazzi M, Hamon MA, Tham TN, Mallet A, Lelek M, et al. Entrapment of intracytosolic bacteria by septin cage-like structures. Cell Host Microbe. 2010;8:433–44. https://doi.org/10.1016/j.chom.2010.10.009. [pii] S1931-3128(10)00346-X.
Mujal AM, Gilden JK, Gerard A, Kinoshita M, Krummel MF. A septin requirement differentiates autonomous and contact-facilitated T cell proliferation. Nat Immunol. 2015. https://doi.org/10.1038/ni.3330.
Nagata K, Kawajiri A, Matsui S, Takagishi M, Shiromizu T, Saitoh N, et al. Filament formation of MSF-A, a mammalian septin, in human mammary epithelial cells depends on interactions with microtubules. J Biol Chem. 2003;278:18538–43. https://doi.org/10.1074/jbc.M205246200.
Neufeld TP, Rubin GM. The Drosophila peanut gene is required for cytokinesis and encodes a protein similar to yeast putative bud neck filament proteins. Cell. 1994;77:371–9.
Ono R, Ihara M, Nakajima H, Ozaki K, Kataoka-Fujiwara Y, Taki T, et al. Disruption of Sept6, a fusion partner gene of MLL, does not affect ontogeny, leukemogenesis induced by MLL-SEPT6, or phenotype induced by the loss of Sept4. Mol Cell Biol. 2005;25:10965–78. https://doi.org/10.1128/MCB.25.24.10965-10978.2005.
Pagliuso A, Tham TN, Stevens JK, Lagache T, Persson R, Salles A, et al. A role for septin 2 in Drp1-mediated mitochondrial fission. EMBO Rep. 2016;17:858–73. https://doi.org/10.15252/embr.201541612.
Patzig J, Erwig MS, Tenzer S, Kusch K, Dibaj P, Mobius W, et al. Septin/anillin filaments scaffold central nervous system myelin to accelerate nerve conduction. Elife. 2016;5. https://doi.org/10.7554/eLife.17119.
Peng XR, Jia Z, Zhang Y, Ware J, Trimble WS. The septin CDCrel-1 is dispensable for normal development and neurotransmitter release. Mol Cell Biol. 2002;22:378–87.
Perez AM, Finnigan GC, Roelants FM, Thorner J. Septin-associated protein kinases in the yeast Saccharomyces cerevisiae. Front Cell Dev Biol. 2016;4:119. https://doi.org/10.3389/fcell.2016.00119.
Periquet M, Corti O, Jacquier S, Brice A. Proteomic analysis of parkin knockout mice: alterations in energy metabolism, protein handling and synaptic function. J Neurochem. 2005;95:1259–76. https://doi.org/10.1111/j.1471-4159.2005.03442.x.
Pous C, Klipfel L, Baillet A. Cancer-related functions and subcellular localizations of septins. Front Cell Dev Biol. 2016;4:126. https://doi.org/10.3389/fcell.2016.00126.
Pringle JR. Origins and development of the septin field. In: The septins. Chicester: Wiley; 2008. p. 5–34.
Qi M, Yu W, Liu S, Jia H, Tang L, Shen M, et al. Septin1, a new interaction partner for human serine/threonine kinase aurora-B. Biochem Biophys Res Commun. 2005;336:994–1000. https://doi.org/10.1016/j.bbrc.2005.06.212.
Röseler S, Bläser S, Bartsch I, Rempp H, Bauer H, Lieber M, et al. SEPT11, a novel platelet septin partners with the platelet septin SEPT5. Blood. 2005;106:3945.
Roseler S, Sandrock K, Bartsch I, Busse A, Omran H, Loges NT, et al. Lethal phenotype of mice carrying a Sept11 null mutation. Biol Chem. 2011;392:779–81. https://doi.org/10.1515/BC.2011.093.
Sanders SL, Field CM. Cell division. Septins in common? Curr Biol. 1994;4:907–10.
Sandrock K, Bartsch I, Blaser S, Busse A, Busse E, Zieger B. Characterization of human septin interactions. Biol Chem. 2011;392:751–61. https://doi.org/10.1515/BC.2011.081.
Scholz R, Imami K, Scott NE, Trimble WS, Foster LJ, Finlay BB. Novel host proteins and signaling pathways in enteropathogenic E. coli pathogenesis identified by global phosphoproteome analysis. Mol Cell Proteomics. 2015;14:1927–45. https://doi.org/10.1074/mcp.M114.046847.
Sellin ME, Sandblad L, Stenmark S, Gullberg M. Deciphering the rules governing assembly order of mammalian septin complexes. Mol Biol Cell. 2011;22:3152–64. https://doi.org/10.1091/mbc.E11-03-0253.
Sharma S, Quintana A, Findlay GM, Mettlen M, Baust B, Jain M, et al. An siRNA screen for NFAT activation identifies septins as coordinators of store-operated Ca entry. Nature. 2013:499(7457):238-242. https://doi.org/10.1038/nature12229., [pii] nature12229.
She YM, Huang YW, Zhang L, Trimble WS. Septin 2 phosphorylation: theoretical and mass spectrometric evidence for the existence of a single phosphorylation site in vivo. Rapid Commun Mass Spectrom. 2004;18:1123–30. https://doi.org/10.1002/rcm.1453.
Shindo A, Wallingford JB. PCP and septins compartmentalize cortical actomyosin to direct collective cell movement. Science. 2014;343:649–52. https://doi.org/10.1126/science.1243126.
Shiryaev A, Kostenko S, Dumitriu G, Moens U. Septin 8 is an interaction partner and in vitro substrate of MK5. World J Biol Chem. 2012;3:98–109. https://doi.org/10.4331/wjbc.v3.i5.98.
Sirajuddin M, Farkasovsky M, Hauer F, Kuhlmann D, Macara IG, Weyand M, et al. Structural insight into filament formation by mammalian septins. Nature. 2007;449:311–5. https://doi.org/10.1038/nature06052.
Sirajuddin M, Farkasovsky M, Zent E, Wittinghofer A. GTP-induced conformational changes in septins and implications for function. Proc Natl Acad Sci USA. 2009;106:16592–7. https://doi.org/10.1073/pnas.0902858106. [pii] 0902858106.
Sirianni A, Krokowski S, Lobato-Marquez D, Buranyi S, Pfanzelter J, Galea D, et al. Mitochondria mediate septin cage assembly to promote autophagy of Shigella. EMBO Rep. 2016;17:1029–43. https://doi.org/10.15252/embr.201541832.
Song K, Russo G, Krauss M. Septins as modulators of endo-lysosomal membrane traffic. Front Cell Dev Biol. 2016;4:124. https://doi.org/10.3389/fcell.2016.00124.
Spiliotis ET, Kinoshita M, Nelson WJ. A mitotic septin scaffold required for Mammalian chromosome congression and segregation. Science. 2005;307:1781–5. https://doi.org/10.1126/science.1106823.
Surka MC, Tsang CW, Trimble WS. The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis. Mol Biol Cell. 2002;13:3532–45. https://doi.org/10.1091/mbc.E02-01-0042.
Suzuki G, Harper KM, Hiramoto T, Sawamura T, Lee M, Kang G, et al. Sept5 deficiency exerts pleiotropic influence on affective behaviors and cognitive functions in mice. Hum Mol Genet. 2009;18:1652–60. https://doi.org/10.1093/hmg/ddp086.
Tada T, Simonetta A, Batterton M, Kinoshita M, Edbauer D, Sheng M. Role of Septin cytoskeleton in spine morphogenesis and dendrite development in neurons. Curr Biol. 2007;17:1752–8. https://doi.org/10.1016/j.cub.2007.09.039.
Taniguchi M, Taoka M, Itakura M, Asada A, Saito T, Kinoshita M, et al. Phosphorylation of adult type Sept5 (CDCrel-1) by cyclin-dependent kinase 5 inhibits interaction with syntaxin-1. J Biol Chem. 2007;282:7869–76. https://doi.org/10.1074/jbc.M609457200.
Tooley AJ, Gilden J, Jacobelli J, Beemiller P, Trimble WS, Kinoshita M, et al. Amoeboid T lymphocytes require the septin cytoskeleton for cortical integrity and persistent motility. Nat Cell Biol. 2009;11:17–26. https://doi.org/10.1038/ncb1808. [pii] ncb1808.
Torraca V, Mostowy S. Septins and bacterial infection. Front Cell Dev Biol. 2016;4:127. https://doi.org/10.3389/fcell.2016.00127.
Vagin O, Tokhtaeva E, Garay PE, Souda P, Bassilian S, Whitelegge JP, et al. Recruitment of septin cytoskeletal proteins by botulinum toxin A protease determines its remarkable stability. J Cell Sci. 2014;127:3294–308. https://doi.org/10.1242/jcs.146324.
Versele M, Thorner J. Some assembly required: yeast septins provide the instruction manual. Trends Cell Biol. 2005;15:414–24. https://doi.org/10.1016/j.tcb.2005.06.007.
Versele M, Gullbrand B, Shulewitz MJ, Cid VJ, Bahmanyar S, Chen RE, et al. Protein-protein interactions governing septin heteropentamer assembly and septin filament organization in Saccharomyces cerevisiae. Mol Biol Cell. 2004;15:4568–83. https://doi.org/10.1091/mbc.E04-04-0330.
Warren JD, Xiong W, Bunker AM, Vaughn CP, Furtado LV, Roberts WL, et al. Septin 9 methylated DNA is a sensitive and specific blood test for colorectal cancer. BMC Med. 2011;9:133. https://doi.org/10.1186/1741-7015-9-133.
Weems AD, Johnson CR, Argueso JL, McMurray MA. Higher-order septin assembly is driven by GTP-promoted conformational changes: evidence from unbiased mutational analysis in Saccharomyces cerevisiae. Genetics. 2014;196:711–27. https://doi.org/10.1534/genetics.114.161182.
Weirich CS, Erzberger JP, Barral Y. The septin family of GTPases: architecture and dynamics. Nat Rev Mol Cell Biol. 2008;9:478–89. https://doi.org/10.1038/nrm2407.
Xue J, Wang X, Malladi CS, Kinoshita M, Milburn PJ, Lengyel I, et al. Phosphorylation of a new brain-specific septin, G-septin, by cGMP-dependent protein kinase. J Biol Chem. 2000;275:10047–56.
Xue J, Milburn PJ, Hanna BT, Graham ME, Rostas JA, Robinson PJ. Phosphorylation of septin 3 on Ser-91 by cGMP-dependent protein kinase-I in nerve terminals. Biochem J. 2004;381:753–60. https://doi.org/10.1042/BJ20040455.
Yoruker EE, Holdenrieder S, Gezer U. Blood-based biomarkers for diagnosis, prognosis and treatment of colorectal cancer. Clin Chim Acta. 2016;455:26–32. https://doi.org/10.1016/j.cca.2016.01.016.
Yu W, Ding X, Chen F, Liu M, Shen S, Gu X, et al. The phosphorylation of SEPT2 on Ser218 by casein kinase 2 is important to hepatoma carcinoma cell proliferation. Mol Cell Biochem. 2009;325:61–7. https://doi.org/10.1007/s11010-008-0020-2.
Zhu JL, Lin SL, Li M, Ouyang YC, Hou Y, Schatten H, et al. Septin2 is modified by SUMOylation and required for chromosome congression in mouse oocytes. Cell Cycle. 2010;9:1607–16. https://doi.org/10.4161/cc.9.8.11463.
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Menon, M.B. (2018). Septin. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101986
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