Mammalian septins in health and disease

References

• Byers B, Goetsch L. A highly ordered ring of membrane-associated filaments in budding yeast. J Cell Biol. 1976;69:717–721.
   PubMed Web of Science ®Google Scholar
• Hartwell LH. Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis. Exp Cell Res. 1971;69:265–276.
   PubMed Web of Science ®Google Scholar
• Longtine MS, DeMarini DJ, Valencik ML, et al. The septins: roles in cytokinesis and other processes. Curr Opin Cell Biol. 1996;8:106–119.
   PubMed Web of Science ®Google Scholar
• Nishihama R, Onishi M, Pringle JR. New insights into the phylogenetic distribution and evolutionary origins of the septins. Biol Chem. 2011;392:681–687.
   Web of Science ®Google Scholar
• McMurray MA, Bertin A, Garcia G 3rd, Lam L, Nogales E, Thorner J. Septin filament formation is essential in budding yeast. Dev Cell 20. 2011;20:540–549.
   Google Scholar
• Cooper JA, Kiehart DP. Septins may form a ubiquitous family of cytoskeletal filaments. J Cell Biol. 1996;134:1345–1348.
   PubMed Web of Science ®Google Scholar
• Mostowy S, Bonazzi M, Hamon MA, et al. Entrapment of intracytosolic bacteria by septin cage-like structures. Cell Host Microbe. 2010;8:433–444.
   PubMed Web of Science ®Google Scholar
• Kinoshita M, Field CM, Coughlin ML, Straight AF, Mitchison TJ. Self- and actin-templated assembly of mammalian septins. Dev Cell. 2002;3:791–802.
   PubMed Web of Science ®Google Scholar
• Vrabioiu AM, Mitchison TJ. Structural insights into yeast septin organization from polarized fluorescence microscopy. Nature. 2006;443:466–469.
   PubMed Web of Science ®Google Scholar
• Rodal AA, Kozubowski L, Goode BL, Drubin DG, Hartwig JH. Actin and septin ultrastructures at the budding yeast cell cortex. Mol Biol Cell. 2005;16:372–384.
   PubMed Web of Science ®Google Scholar
• Versele M, Gullbrand B, Shulewitz MJ, et al. Protein-protein interactions governing septin heteropentamer assembly and septin filament organization in Saccharomyces cerevisiae. Mol Biol Cell. 2004;15:4568–4583.
   PubMed Web of Science ®Google Scholar
• Cao L, Ding X, Yu W, Yang X, Shen S, Yu L. Phylogenetic and evolutionary analysis of the septin protein family in metazoan. FEBS Lett. 2007;581:5526–5532.
   PubMed Web of Science ®Google Scholar
• Kinoshita M. Assembly of mammalian septins. J Biochem. 2003;134:491–496.
   PubMed Web of Science ®Google Scholar
• Weirich CS, Erzberger JP, Barral Y. The septin family of GTPases: architecture and dynamics. Nat Rev Mol Cell Biol. 2008;9:478–489.
   PubMed Web of Science ®Google Scholar
• Pan F, Malmberg RL, Momany M. Analysis of septins across kingdoms reveals orthology and new motifs. BMC Evol Biol. 2007;7:103.
   PubMed Web of Science ®Google Scholar
• Casamayor A, Snyder M. Molecular dissection of a yeast septin: distinct domains are required for septin interaction, localization, and function. Mol Cell Biol. 2003;23;2762–2777.
   Web of Science ®Google Scholar
• Meseroll RA, Howard L, Gladfelter AS. Septin ring size scaling and dynamics require the coiled-coil region of Shs1p. Mol Biol Cell. 2012;23:3391–3406.
   Web of Science ®Google Scholar
• Bertin A, McMurray MA, Grob P, et al. Saccharomyces cerevisiae septins: supramolecular organization of heterooligomers and the mechanism of filament assembly. Proc Natl Acad Sci U S A. 2008;105; 8274–8279.
   Google Scholar
• Low C, Macara IG. Structural analysis of septin 2, 6, and 7 complexes. J Biol Chem. 2006;281:30697–30706.
   PubMed Web of Science ®Google Scholar
• Dolat L, Hu Q, Spiliotis ET. Septin functions in organ system physiology and pathology. Biol Chem. 2014;395:123–141.
   PubMed Web of Science ®Google Scholar
• Huang YW, Surka MC, Reynaud D, Pace-Asciak C, Trimble WS. GTP binding and hydrolysis kinetics of human septin 2. FEBS J. 2006;273:3248–3260.
   PubMed Web of Science ®Google Scholar
• Farkasovsky M, Herter P, Voss B, Wittinghofer A. Nucleotide binding and filament assembly of recombinant yeast septin complexes. Biol Chem. 2005;386:643–656.
   PubMed Web of Science ®Google Scholar
• Zent E, Wittinghofer A. Human septin isoforms and the GDP-GTP cycle. Biol Chem. 2014;395:169–180.
   Web of Science ®Google Scholar
• Sirajuddin M, Farkasovsky M, Zent E, Wittinghofer A. GTP-induced conformational changes in septins and implications for function. Proc Natl Acad Sci U S A. 2009;106:16592–16597.
   Web of Science ®Google Scholar
• Vetter IR, Wittinghofer A. The guanine nucleotide-binding switch in three dimensions. Science. 2001;294:1299–1304.
   PubMed Web of Science ®Google Scholar
• Zhang J, Kong C, Xie H, McPherson PS, Grinstein S, Trimble WS. Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP. Curr Biol. 1999;9:1458–1467.
   PubMed Web of Science ®Google Scholar
• Kremer BE, Haystead T, Macara IG. Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4. Mol Biol Cell. 2005;16:4648–4659.
   Web of Science ®Google Scholar
• Kay BK, Williamson MP, Sudol M. The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 2000;14:231–241.
   PubMed Web of Science ®Google Scholar
• Pham T, DiCiccio JE, Trimble WS. Cytoskeleton: septins do the horizontal tango. Curr Biol. 2014;24:R324–R327.
   Web of Science ®Google Scholar
• John CM, Hite RK, Weirich CS, et al. The Caenorhabditis elegans septin complex is nonpolar. EMBO J. 2007;26:3296–3307.
   PubMed Web of Science ®Google Scholar
• Sirajuddin M, Farkasovsky M, Hauer F, et al. Structural insight into filament formation by mammalian septins. Nature. 2007;449:311–315.
   PubMed Web of Science ®Google Scholar
• de Almeida Marques I, Valadares NF, Garcia W, et al. Septin C-terminal domain interactions: implications for filament stability and assembly. Cell Biochem Biophys. 2012;62:317–328.
   Web of Science ®Google Scholar
• Joberty G, Perlungher RR, Sheffield PJ, et al. Borg proteins control septin organization and are negatively regulated by Cdc42. Nat Cell Biol. 2001;3:861–866.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Xie Y, Vessey JP, Konecna A, Dahm R, Macchi P, Kiebler MA. The GTP-binding protein Septin 7 is critical for dendrite branching and dendritic-spine morphology. Curr Biol. 2007;17:1746–1751.
   PubMed Web of Science ®Google Scholar
• Nagata K, Asano T, Nozawa Y, Inagaki M. Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11. J Biol Chem. 2004;279:55895–55904.
   PubMed Web of Science ®Google Scholar
• Sellin ME, Sandblad L, Stenmark S, Gullberg M. Deciphering the rules governing assembly order of mammalian septin complexes. Mol Biol Cell. 2011;22:3152–3164.
   PubMed Web of Science ®Google Scholar
• Surka MC, Tsang CW, Trimble WS. The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis. Mol Biol Cell. 2002;13:3532–3545.
   PubMed Web of Science ®Google Scholar
• 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;191:741–749.
   PubMed Web of Science ®Google Scholar
• 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;195:815–826.
   PubMed Web of Science ®Google Scholar
• Mostowy S, Cossart P. Septins: the fourth component of the cytoskeleton. Nat Rev Mol Cell Biol. 2012;13:183–194.
   PubMed Web of Science ®Google Scholar
• Bai X, Bowen JR, Knox TK, et al. Novel septin 9 repeat motifs altered in neuralgic amyotrophy bind and bundle microtubules. J Cell Biol. 2013;203:895–905.
   Web of Science ®Google Scholar
• Cooper TG. Cytoplasmic droplets: the good, the bad or just confusing? Hum Reprod. 2005;20:9–11.
   Web of Science ®Google Scholar
• Mavrakis M, Azou-Gros Y, Tsai FC, et al. Septins promote F-actin ring formation by crosslinking actin filaments into curved bundles. Nat Cell Biol. 2014;16:322–334.
   PubMed Web of Science ®Google Scholar
• Johnson ES, Gupta AA. An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell. 2001;106:735–744.
   PubMed Web of Science ®Google Scholar
• Joo E, Surka MC, Trimble WS. Mammalian SEPT2 is required for scaffolding nonmuscle myosin II and its kinases. Dev Cell. 2007;13:677–690.
   Web of Science ®Google Scholar
• Spiliotis ET, Hunt SJ, Hu Q, Kinoshita M, Nelson WJ. Epithelial polarity requires septin coupling of vesicle transport to polyglutamylated microtubules. J Cell Biol. 2008;180:295–303.
   Web of Science ®Google Scholar
• Beites CL, Xie H, Bowser R, Trimble WS. The septin CDCrel-1 binds syntaxin and inhibits exocytosis. Nat Neurosci. 1999;2:434–439.
   PubMed Web of Science ®Google Scholar
• Barral Y, Parra M, Bidlingmaier S, Snyder M. Nim1-related kinases coordinate cell cycle progression with the organization of the peripheral cytoskeleton in yeast. Genes Dev. 1999;13:176–187.
   PubMed Web of Science ®Google Scholar
• Hanrahan J, Snyder M. Cytoskeletal activation of a checkpoint kinase. Mol Cell. 2003;12:663–673.
   PubMed Web of Science ®Google Scholar
• Longtine MS, Theesfeld CL, McMillan JN, Weaver E, Pringle JR, Lew DJ. Septin-dependent assembly of a cell cycle-regulatory module in Saccharomyces cerevisiae. Mol Cell Biol. 2000;20:4049–4061.
   Google Scholar
• Vrabioiu AM, Gerber SA, Gygi SP, Field CM, Mitchison TJ. The majority of the Saccharomyces cerevisiae septin complexes do not exchange guanine nucleotides. J Biol Chem. 2004;279:3111–3118.
   PubMed Web of Science ®Google Scholar
• Kinoshita M. Diversity of septin scaffolds. Curr Opin Cell Biol. 2006;18:54–60.
   PubMed Web of Science ®Google Scholar
• Kusch J, Meyer A, Snyder MP, Barral Y. Microtubule capture by the cleavage apparatus is required for proper spindle positioning in yeast. Genes Dev. 2002;16:1627–1639.
   PubMed Web of Science ®Google Scholar
• Barral Y, Mermall V, Mooseker MS, Snyder M. Compartmentalization of the cell cortex by septins is required for maintenance of cell polarity in yeast. Mol Cell. 2000;5:841–851.
   PubMed Web of Science ®Google Scholar
• Takizawa PA, DeRisi JL, Wilhelm JE, Vale RD. Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier. Science. 2000;290:341–344.
   PubMed Web of Science ®Google Scholar
• Dobbelaere J, Barral Y. Spatial coordination of cytokinetic events by compartmentalization of the cell cortex. Science. 2004;305:393–396.
   PubMed Web of Science ®Google Scholar
• Saarikangas J, Barral Y. The emerging functions of septins in metazoans. EMBO Rep. 2011;12:1118–1126.
   PubMed Web of Science ®Google Scholar
• Schmidt K, Nichols BJ. A barrier to lateral diffusion in the cleavage furrow of dividing mammalian cells. Curr Biol. 2004;14:1002–1006.
   PubMed Web of Science ®Google Scholar
• Satir P, Pedersen LB, Christensen ST. The primary cilium at a glance. J Cell Sci. 2010;123:499–503.
   PubMed Web of Science ®Google Scholar
• Hu Q, Milenkovic L, Jin H, et al. A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution. Science. 2010;329:436–439.
   PubMed Web of Science ®Google Scholar
• Ihara M, Kinoshita A, Yamada S, et al. Cortical organization by the septin cytoskeleton is essential for structural and mechanical integrity of mammalian spermatozoa. Dev Cell. 2005;8:343–352.
   PubMed Web of Science ®Google Scholar
• 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;8:353–364.
   PubMed Web of Science ®Google Scholar
• Steels JD, Estey MP, Froese CD, Reynaud D, Pace-Asciak C, Trimble WS. Sept12 is a component of the mammalian sperm tail annulus. Cell Motil Cytoskeleton. 2007;64:794–807.
   PubMed Web of Science ®Google Scholar
• 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;17:1752–1758.
   PubMed Web of Science ®Google Scholar
• Buser AM, Erne B, Werner HB, Nave KA, Schaeren-Wiemers N. The septin cytoskeleton in myelinating glia. Mol Cell Neurosci. 2009;40:156–166.
   PubMed Web of Science ®Google Scholar
• Patzig J, Jahn O, Tenzer S, et al. Quantitative and integrative proteome analysis of peripheral nerve myelin identifies novel myelin proteins and candidate neuropathy loci. J Neurosci. 2011;31:16369–16386.
   PubMed Web of Science ®Google Scholar
• Kim SK, Shindo A, Park TJ, et al. Planar cell polarity acts through septins to control collective cell movement and ciliogenesis. Science. 2010;329:1337–1340.
   PubMed Web of Science ®Google Scholar
• McCaffrey LM, Macara IG. Widely conserved signaling pathways in the establishment of cell polarity. Cold Spring Harb Perspect Biol. 2009;1:a001370.
   Web of Science ®Google Scholar
• Pringle JR, Bi E, Harkins HA, et al. Establishment of cell polarity in yeast. Cold Spring Harb Symp Quant Biol. 1995;60:729–744.
   PubMedGoogle Scholar
• Drubin DG, Nelson WJ. Origins of cell polarity. Cell. 1996;84:335–344.
   PubMed Web of Science ®Google Scholar
• Bowen JR, Hwang D, Bai X, Roy D, Spiliotis ET. Septin GTPases spatially guide microtubule organization and plus end dynamics in polarizing epithelia. J Cell Biol. 2011;194:187–197.
   Web of Science ®Google Scholar
• Spiliotis ET, Kinoshita M, Nelson WJ. A mitotic septin scaffold required for mammalian chromosome congression and segregation. Science. 2005;307:1781–1785.
   PubMed Web of Science ®Google Scholar
• Nagata K, Kawajiri A, Matsui S, et al. Filament formation of MSF-A, a mammalian septin, in human mammary epithelial cells depends on interactions with microtubules. J Biol Chem. 2003;278:18538–18543.
   PubMed Web of Science ®Google Scholar
• Spiliotis ET. Regulation of microtubule organization and functions by septin GTPases. Cytoskeleton. 2010;67:339–345.
   Web of Science ®Google Scholar
• Huang YW, Yan M, Collins RF, Diciccio JE, Grinstein S, Trimble WS. Mammalian septins are required for phagosome formation. Mol Biol Cell. 2008;19:1717–1726.
   Web of Science ®Google Scholar
• Mostowy S, Nam Tham T, Danckaert A, et al. Septins regulate bacterial entry into host cells. PloS One. 2009;4:e4196.
   Web of Science ®Google Scholar
• Tooley AJ, Gilden J, Jacobelli J, et al. Amoeboid T lymphocytes require the septin cytoskeleton for cortical integrity and persistent motility. Nat Cell Biol. 2009;11:17–26.
   Web of Science ®Google Scholar
• Lassen LB, Füchtbauer A, Schmitz A, Sørensen AB, Pedersen FS, Füchtbauer EM. Septin9 is involved in T-cell development and CD8+ T-cell homeostasis. Cell Tissue Res. 2013;352:695–705.
   Web of Science ®Google Scholar
• Kinoshita A, Kinoshita M, Akiyama H, et al. Identification of septins in neurofibrillary tangles in Alzheimer’s disease. Am J Pathol. 1998;153:1551–1560.
   PubMed Web of Science ®Google Scholar
• Ihara M, Tomimoto H, Kitayama H, et al. Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson’s disease and other synucleinopathies. J Biol Chem. 2003;278:24095–24102.
   PubMed Web of Science ®Google Scholar
• Shehadeh L, Mitsi G, Adi N, Bishopric N, Papapetropoulos S. Expression of Lewy body protein septin 4 in postmortem brain of Parkinson’s disease and control subjects. Mov Disord. 2009;24:204–210.
   Web of Science ®Google Scholar
• Pennington K, Beasley CL, Dicker P, et al. Prominent synaptic and metabolic abnormalities revealed by proteomic analysis of the dorsolateral prefrontal cortex in schizophrenia and bipolar disorder. Mol Psychiatry. 2008;13:1102–1117.
   PubMed Web of Science ®Google Scholar
• Engidawork E, Gulesserian T, Fountoulakis M, Lubec G. Aberrant protein expression in cerebral cortex of fetus with Down syndrome. Neuroscience. 2003;122:145–154.
   PubMed Web of Science ®Google Scholar
• Walikonis RS, Jensen ON, Mann M, Provance DW Jr, Mercer JA, Kennedy MB. Identification of proteins in the postsynaptic density fraction by mass spectrometry. J Neurosci. 2000;20:4069–4080.
   PubMed Web of Science ®Google Scholar
• Kalikin LM, Sims HL, Petty EM. Genomic and expression analyses of alternatively spliced transcripts of the MLL septin-like fusion gene (MSF) that map to a 17q25 region of loss in breast and ovarian tumors. Genomics. 2000;63:165–172.
   PubMed Web of Science ®Google Scholar
• McIlhatton MA, Burrows JF, Donaghy PG, Chanduloy S, Johnston PG, Russell SE. Genomic organization, complex splicing pattern and expression of a human septin gene on chromosome 17q25.3. Oncogene. 2001;20:5930–5939.
   PubMed Web of Science ®Google Scholar
• Kuhlenbäumer G, Hannibal MC, Nelis E, et al. Mutations in SEPT9 cause hereditary neuralgic amyotrophy. Nat Genet. 2005;37:1044–1046.
   PubMed Web of Science ®Google Scholar
• Hannibal MC, Ruzzo EK, Miller LR, et al. SEPT9 gene sequencing analysis reveals recurrent mutations in hereditary neuralgic amyotrophy. Neurology. 2009;72:1755–1759.
   Web of Science ®Google Scholar
• Collie AM, Landsverk ML, Ruzzo E, et al. Non-recurrent SEPT9 duplications cause hereditary neuralgic amyotrophy. J Med Genet. 2010;47:601–607.
   Web of Science ®Google Scholar
• Landsverk ML, Ruzzo EK, Mefford HC, et al. Duplication within the SEPT9 gene associated with a founder effect in North American families with hereditary neuralgic amyotrophy. Hum Mol Genet. 2009;18:1200–1208.
   Web of Science ®Google Scholar
• Sudo K, Ito H, Iwamoto I, Morishita R, Asano T, Nagata K. SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are associated with altered interactions with SEPT4/SEPT11 and resistance to Rho/Rhotekin-signaling. Hum Mutat. 2007;28:1005–1013.
   Web of Science ®Google Scholar
• Kuo YC, Lin YH, Chen HI, et al. SEPT12 mutations cause male infertility with defective sperm annulus. Hum Mutat. 2012;33:710–719.
   Web of Science ®Google Scholar
• Megonigal MD, Rappaport EF, Jones DH, et al. t(11;22)(q23;q11.2) In acute myeloid leukemia of infant twins fuses MLL with hCDCrel, a cell division cycle gene in the genomic region of deletion in DiGeorge and velocardiofacial syndromes. Proc Natl Acad Sci U S A. 1998;95:6413–6418.
   PubMed Web of Science ®Google Scholar
• Osaka M, Rowley JD, Zeleznik-Le NJ. 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). Proc Natl Acad Sci U S A. 1999;96:6428–6433.
   PubMed Web of Science ®Google Scholar
• Rabbitts TH. Chromosomal translocations in human cancer. Nature. 1994;372:143–149.
   PubMed Web of Science ®Google Scholar
• Thirman MJ, Gill HJ, Burnett RC, et al. Rearrangement of the MLL gene in acute lymphoblastic and acute myeloid leukemias with 11q23 chromosomal translocations. N Engl J Med. 1993;329:909–914.
   PubMed Web of Science ®Google Scholar
• Borkhardt A, Teigler-Schlegel A, Fuchs U, et al. An ins(X;11) (q24;q23) fuses the MLL and the Septin 6/KIAA0128 gene in an infant with AML-M2. Genes Chromosomes Cancer. 2001;32:82–88.
   PubMed Web of Science ®Google Scholar
• Yamamoto K, Shibata F, Yamaguchi M, Miura O. Fusion of MLL and MSF in adult de novo acute myelomonocytic leukemia (M4) with t(11;17)(q23;q25). Int J Hematol. 2002;75:503–507.
   PubMed Web of Science ®Google Scholar
• Kreuziger LM, Porcher JC, Ketterling RP, Steensma DP. An MLL-SEPT9 fusion and t(11;17)(q23;q25) associated with de novo myelodysplastic syndrome. Leuk Res. 2007;31:1145–1148.
   PubMed Web of Science ®Google Scholar
• Kurosu T, Tsuji K, Ohki M, et al. A variant-type MLL/SEPT9 fusion transcript in adult de novo acute monocytic leukemia (M5b) with t(11;17)(q23;q25). Int J Hematol. 2008;88:192–196.
   PubMed Web of Science ®Google Scholar
• Stevens SJ, Meers LE, Albrechts JC, et al. A translocation in acute lymphoblastic leukemia that cytogenetically mimics the recurrent MLL-AFF1 translocation and fuses SEPT11 to MLL. Cancer Genet Cytogenet. 2010;201:48–51.
   Google Scholar
• Cerveira N, Santos J, Teixeira MR. Structural and expression changes of septins in myeloid neoplasia. Crit Rev Oncog. 2009;15:91–115.
   Google Scholar
• Connolly D, Yang Z, Castaldi M, et al. Septin 9 isoform expression, localization and epigenetic changes during human and mouse breast cancer progression. Breast Cancer Res. 2011;13:R76.
   PubMed Web of Science ®Google Scholar
• Cerveira N, Bizarro S, Teixeira MR. MLL-SEPTIN gene fusions in hematological malignancies. Biol Chem. 2011;392:713–724.
   PubMed Web of Science ®Google Scholar
• Ostrom QT, Bauchet L, Davis FG, et al. The epidemiology of glioma in adults: a “state of the science” review. Neuro Oncol. 2014;16:896–913.
   PubMed Web of Science ®Google Scholar
• Sakai K, Kurimoto M, Tsugu A, Hubbard SL, Trimble WS, Rutka JT. Expression of Nedd5, a mammalian septin, in human brain tumors. J Neurooncol. 2002;57:169–177.
   PubMed Web of Science ®Google Scholar
• Khalil AA. Biomarker discovery: a proteomic approach for brain cancer profiling. Cancer Sci. 2007;98:201–213.
   PubMed Web of Science ®Google Scholar
• Kim DS, Hubbard SL, Peraud A, Salhia B, Sakai K, Rutka JT. Analysis of mammalian septin expression in human malignant brain tumors. Neoplasia. 2004;6:168–178.
   PubMed Web of Science ®Google Scholar
• Jia ZF, Huang Q, Kang CS, et al. Overexpression of septin 7 suppresses glioma cell growth. J Neurooncol. 2010;98:329–340.
   Web of Science ®Google Scholar
• Siegel R, Naishadham D, Jemal A. Cancer statistics, 2012. CA Cancer J Clin. 2012;62:10–29.
   PubMed Web of Science ®Google Scholar
• Montagna C, Lyu MS, Hunter K, et al. The septin 9 (MSF) gene is amplified and overexpressed in mouse mammary gland adenocarcinomas and human breast cancer cell lines. Cancer Res. 2003;63:2179–2187.
   PubMed Web of Science ®Google Scholar
• Russell SE, McIlhatton MA, Burrows JF, et al. Isolation and mapping of a human septin gene to a region on chromosome 17q, commonly deleted in sporadic epithelial ovarian tumors. Cancer Res. 2000;60:4729–4734.
   PubMed Web of Science ®Google Scholar
• Sørensen AB, Warming S, Füchtbauer EM, Pedersen FS. Alternative splicing, expression, and gene structure of the septin-like putative proto-oncogene Sint1. Gene. 2002;285:79–89.
   PubMed Web of Science ®Google Scholar
• Gonzalez ME, Peterson EA, Privette LM, Loffreda-Wren JL, Kalikin LM, Petty EM. High SEPT9_v1 expression in human breast cancer cells is associated with oncogenic phenotypes. Cancer Res. 2007;67:8554–8564.
   PubMed Web of Science ®Google Scholar
• Connolly D, Hoang HG, Adler E, et al. Septin 9 amplification and isoform-specific expression in peritumoral and tumor breast tissue. Biol Chem. 2014;395:157–167.
   PubMed Web of Science ®Google Scholar
• Amir S, Golan M, Mabjeesh NJ. Targeted knockdown of SEPT9_v1 inhibits tumor growth and angiogenesis of human prostate cancer cells concomitant with disruption of hypoxia-inducible factor-1 pathway. Mol Cancer Res. 2010;8:643–652.
   PubMed Web of Science ®Google Scholar
• Chacko AD, McDade SS, Chanduloy S, et al. Expression of the SEPT9_i4 isoform confers resistance to microtubule-interacting drugs. Cell Oncol (Dordr). 2012;35:85–93.
   Web of Science ®Google Scholar
• Gonzalez ME, Makarova O, Peterson EA, Privette LM, Petty EM. Up-regulation of SEPT9_v1 stabilizes c-Jun-N-terminal kinase and contributes to its pro-proliferative activity in mammary epithelial cells. Cell Signal. 2009;21:477–487.
   Web of Science ®Google Scholar
• Chacko AD, Hyland PL, McDade SS, Hamilton PW, Russell SH, Hall PA. SEPT9_v4 expression induces morphological change, increased motility and disturbed polarity. J Pathol. 2005;206:458–465.
   Web of Science ®Google Scholar
• Burrows JF, Chanduloy S, McIlhatton MA, et al. Altered expression of the septin gene, SEPT9, in ovarian neoplasia. J Pathol. 2003;201:581–588.
   PubMed Web of Science ®Google Scholar
• Scott M, McCluggage WG, Hillan KJ, Hall PA, Russell SE. Altered patterns of transcription of the septin gene, SEPT9, in ovarian tumorigenesis. Int J Cancer. 2006;118:1325–1329.
   PubMed Web of Science ®Google Scholar
• Foundation for the National Institutes of Health. Key initiatives: Biomarkers Consortium. 2014. Available from: http://www.fnih.org/work/key-initiatives/biomarkers-consortium. Accessed January 17, 2015.
   Google Scholar
• Final Recommendation Statement: Colorectal Cancer: Screening. US Preventive Services Task Force. October 2014. Available from http://www.uspreventiveservicestaskforce.org/Page/Document/RecommendationStatementFinal/colorectal-cancer-screening. Accessed January 30, 2015.
   Google Scholar
• Wild N, Andres H, Rollinger W, et al. A combination of serum markers for the early detection of colorectal cancer. Clin Cancer Res. 2010;16:6111–6121.
   PubMed Web of Science ®Google Scholar
• Lofton-Day C, Model F, Devos T, et al. DNA methylation biomarkers for blood-based colorectal cancer screening. Clin Chem. 2008;54:414–423.
   PubMed Web of Science ®Google Scholar
• Grützmann R, Molnar B, Pilarsky C, et al. Sensitive detection of colorectal cancer in peripheral blood by septin 9 DNA methylation assay. PloS One. 2008;3:e3759.
   PubMed Web of Science ®Google Scholar
• Powrózek T, Krawczyk P, Kucharczyk T, Milanowski J. Septin 9 promoter region methylation in free circulating DNA – potential role in noninvasive diagnosis of lung cancer: preliminary report. Med Oncol. 2014;31:917.
   PubMed Web of Science ®Google Scholar
• Cerami E, Gao J, Dogrusoz U, et al. The cBio cancer genomics portal: an open platform for exploring multidimensional cancer genomics data. Cancer Discov. 2012;2:401–404.
   PubMed Web of Science ®Google Scholar
• National Cancer Institute. The Cancer Genome Atlas. Available from: http://cancergenome.nih.gov. Accessed January 17, 2015.
   Google Scholar
• Robertson C, Church SW, Nagar HA, Price J, Hall PA, Russell SE. Properties of SEPT9 isoforms and the requirement for GTP binding. J Pathol. 2004;203:519–527.
   PubMed Web of Science ®Google Scholar
• Scott M, Hyland PL, McGregor G, Hillan KJ, Russell SE, Hall PA. Multimodality expression profiling shows SEPT9 to be overexpressed in a wide range of human tumours. Oncogene. 2005;24:4688–4700.
   PubMed Web of Science ®Google Scholar
• Wright SD, Ramos RA, Patel M, Miller DS. Septin: a factor in plasma that opsonizes lipopolysaccharide-bearing particles for recognition by CD14 on phagocytes. J Exp Med. 1992;176:719–727.
   PubMed Web of Science ®Google Scholar
• Oh Y, Bi E. Septin structure and function in yeast and beyond. Trends Cell Biol. 2011;21:141–148.
   PubMed Web of Science ®Google Scholar