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Volumn 290, Issue 28, 2015, Pages 17173-17180

Septin form and function at the cell cortex

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CELL PROLIFERATION; CELLS; CYTOLOGY; MAMMALS; MEMBRANES; NEURODEGENERATIVE DISEASES; PROTEINS;

EID: 84940055307     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R114.634444     Document Type: Article
Times cited : (110)

References (99)
  • 1
    • 77955858279 scopus 로고    scopus 로고
    • Control of cortical rigidity by the cytoskeleton: Emerging roles for septins
    • Gilden, J., and Krummel, M. F. (2010) Control of cortical rigidity by the cytoskeleton: emerging roles for septins. Cytoskeleton 67, 477-486
    • (2010) Cytoskeleton , vol.67 , pp. 477-486
    • Gilden, J.1    Krummel, M.F.2
  • 2
    • 84857457272 scopus 로고    scopus 로고
    • Septins: The fourth component of the cytoskeleton
    • Mostowy, S., and Cossart, P. (2012) Septins: the fourth component of the cytoskeleton. Nat. Rev. Mol. Cell Biol. 13, 183-194
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 183-194
    • Mostowy, S.1    Cossart, P.2
  • 3
    • 84855950538 scopus 로고    scopus 로고
    • Spatial guidance of cell asymmetry: Septin GTPases show the way
    • Spiliotis, E. T., and Gladfelter, A. S. (2012) Spatial guidance of cell asymmetry: septin GTPases show the way. Traffic 13, 195-203
    • (2012) Traffic , vol.13 , pp. 195-203
    • Spiliotis, E.T.1    Gladfelter, A.S.2
  • 4
    • 82755189600 scopus 로고    scopus 로고
    • Mammalian septins: Dynamic heteromers with roles in cellular morphogenesis and compartmentalization
    • Hall, P. A., and Russell, S. E. (2012) Mammalian septins: dynamic heteromers with roles in cellular morphogenesis and compartmentalization. J. Pathol. 226, 287-299
    • (2012) J. Pathol. , vol.226 , pp. 287-299
    • Hall, P.A.1    Russell, S.E.2
  • 6
    • 35548961325 scopus 로고    scopus 로고
    • Mammalian SEPT2 is required for scaffolding nonmuscle myosin II and its kinases
    • Joo, E., Surka, M. C., and Trimble, W. S. (2007) Mammalian SEPT2 is required for scaffolding nonmuscle myosin II and its kinases. Dev. Cell 13, 677-690
    • (2007) Dev. Cell , vol.13 , pp. 677-690
    • Joo, E.1    Surka, M.C.2    Trimble, W.S.3
  • 7
    • 84926482998 scopus 로고    scopus 로고
    • MyosinII heavy chain and formin mediate the targeting of myosin essential light chain to the division site before and during cytokinesis
    • Feng, Z., Okada, S., Cai, G., Zhou, B., and Bi, E. (2015) MyosinII heavy chain and formin mediate the targeting of myosin essential light chain to the division site before and during cytokinesis. Mol. Biol. Cell 26, 1211-1224
    • (2015) Mol. Biol. Cell , vol.26 , pp. 1211-1224
    • Feng, Z.1    Okada, S.2    Cai, G.3    Zhou, B.4    Bi, E.5
  • 9
    • 64549158361 scopus 로고    scopus 로고
    • Septins and the lateral compartmentalization of eukaryotic membranes
    • Caudron, F., and Barral, Y. (2009) Septins and the lateral compartmentalization of eukaryotic membranes. Dev. Cell 16, 493-506
    • (2009) Dev. Cell , vol.16 , pp. 493-506
    • Caudron, F.1    Barral, Y.2
  • 11
    • 77953590866 scopus 로고    scopus 로고
    • Regulation of microtubule organization and functions by septin GTPases
    • Spiliotis, E. T. (2010) Regulation of microtubule organization and functions by septin GTPases. Cytoskeleton 67, 339-345
    • (2010) Cytoskeleton , vol.67 , pp. 339-345
    • Spiliotis, E.T.1
  • 12
    • 0015193588 scopus 로고
    • Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis
    • Hartwell, L. H. (1971) Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis. Exp. Cell Res. 69, 265-276
    • (1971) Exp. Cell Res. , vol.69 , pp. 265-276
    • Hartwell, L.H.1
  • 13
    • 84893730542 scopus 로고    scopus 로고
    • Septin functions in organ system physiology and pathology
    • Dolat, L., Hu, Q., and Spiliotis, E. T. (2014) Septin functions in organ system physiology and pathology. Biol. Chem. 395, 123-141
    • (2014) Biol. Chem. , vol.395 , pp. 123-141
    • Dolat, L.1    Hu, Q.2    Spiliotis, E.T.3
  • 16
    • 84884130685 scopus 로고    scopus 로고
    • Colorectal cancer screening with blood-based biomarkers: Cost-effectiveness of methylated septin 9 DNA versus current strategies
    • Ladabaum, U., Allen, J., Wandell, M., and Ramsey, S. (2013) Colorectal cancer screening with blood-based biomarkers: cost-effectiveness of methylated septin 9 DNA versus current strategies. Cancer Epidemiol. Biomarkers Prev. 22, 1567-1576
    • (2013) Cancer Epidemiol. Biomarkers Prev. , vol.22 , pp. 1567-1576
    • Ladabaum, U.1    Allen, J.2    Wandell, M.3    Ramsey, S.4
  • 19
    • 35348834213 scopus 로고    scopus 로고
    • Role of Septin cytoskeleton in spine morphogenesis and dendrite development in neurons
    • Tada, T., Simonetta, A., Batterton, M., Kinoshita, M., Edbauer, D., and Sheng, M. (2007) Role of Septin cytoskeleton in spine morphogenesis and dendrite development in neurons. Curr. Biol. 17, 1752-1758
    • (2007) Curr. Biol. , vol.17 , pp. 1752-1758
    • Tada, T.1    Simonetta, A.2    Batterton, M.3    Kinoshita, M.4    Edbauer, D.5    Sheng, M.6
  • 20
    • 35348907374 scopus 로고    scopus 로고
    • The GTP-binding protein Septin 7 is critical for dendrite branching and dendritic-spine morphology
    • Xie, Y., Vessey, J. P., Konecna, A., Dahm, R., Macchi, P., and Kiebler, M. A. (2007) The GTP-binding protein Septin 7 is critical for dendrite branching and dendritic-spine morphology. Curr. Biol. 17, 1746-1751
    • (2007) Curr. Biol. , vol.17 , pp. 1746-1751
    • Xie, Y.1    Vessey, J.P.2    Konecna, A.3    Dahm, R.4    Macchi, P.5    Kiebler, M.A.6
  • 21
    • 84901418931 scopus 로고    scopus 로고
    • Fungal pathogens are platforms for discovering novel and conserved septin properties
    • Bridges, A. A., and Gladfelter, A. S. (2014) Fungal pathogens are platforms for discovering novel and conserved septin properties. Curr. Opin. Microbiol. 20, 42-48
    • (2014) Curr. Opin. Microbiol. , vol.20 , pp. 42-48
    • Bridges, A.A.1    Gladfelter, A.S.2
  • 23
  • 24
    • 84867159864 scopus 로고    scopus 로고
    • A Candida albicans temperature-sensitive cdc12-6 mutant identifies roles for septins in selection of sites of germ tube formation and hyphal morphogenesis
    • Li, L., Zhang, C., and Konopka, J. B. (2012) A Candida albicans temperature-sensitive cdc12-6 mutant identifies roles for septins in selection of sites of germ tube formation and hyphal morphogenesis. Eukaryot. Cell 11, 1210-1218
    • (2012) Eukaryot. Cell , vol.11 , pp. 1210-1218
    • Li, L.1    Zhang, C.2    Konopka, J.B.3
  • 25
    • 80052719413 scopus 로고    scopus 로고
    • New insights into the phylogenetic distribution and evolutionary origins of the septins
    • Nishihama, R., Onishi, M., and Pringle, J. R. (2011) New insights into the phylogenetic distribution and evolutionary origins of the septins. Biol. Chem. 392, 681-687
    • (2011) Biol. Chem. , vol.392 , pp. 681-687
    • Nishihama, R.1    Onishi, M.2    Pringle, J.R.3
  • 27
    • 70350499161 scopus 로고    scopus 로고
    • The evolution, complex structures and function of septin proteins
    • Cao, L., Yu, W., Wu, Y., and Yu, L. (2009) The evolution, complex structures and function of septin proteins. Cell. Mol. Life Sci. 66, 3309-3323
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 3309-3323
    • Cao, L.1    Yu, W.2    Wu, Y.3    Yu, L.4
  • 30
    • 84869848114 scopus 로고    scopus 로고
    • Septin filament organization in Saccharomyces cerevisiae
    • Bertin, A., and Nogales, E. (2012) Septin filament organization in Saccharomyces cerevisiae. Commun. Integr. Biol. 5, 503-505
    • (2012) Commun. Integr. Biol. , vol.5 , pp. 503-505
    • Bertin, A.1    Nogales, E.2
  • 31
    • 0033576647 scopus 로고    scopus 로고
    • Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP
    • Zhang, J., Kong, C., Xie, H., McPherson, P. S., Grinstein, S., and Trimble, W. S. (1999) Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP. Curr. Biol. 9, 1458-1467
    • (1999) Curr. Biol. , vol.9 , pp. 1458-1467
    • Zhang, J.1    Kong, C.2    Xie, H.3    McPherson, P.S.4    Grinstein, S.5    Trimble, W.S.6
  • 32
    • 0037383708 scopus 로고    scopus 로고
    • Molecular dissection of a yeast septin: Distinct domains are required for septin interaction, localization, and function
    • Casamayor, A., and Snyder, M. (2003) Molecular dissection of a yeast septin: distinct domains are required for septin interaction, localization, and function. Mol. Cell. Biol. 23, 2762-2777
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2762-2777
    • Casamayor, A.1    Snyder, M.2
  • 33
    • 78649333504 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5- bisphosphate promotes budding yeast septin filament assembly and organization
    • Bertin, A., McMurray, M. A., Thai, L., Garcia, G., 3rd, Votin, V., Grob, P., Allyn, T., Thorner, J., and Nogales, E. (2010) Phosphatidylinositol-4,5- bisphosphate promotes budding yeast septin filament assembly and organization. J. Mol. Biol. 404, 711-731
    • (2010) J. Mol. Biol. , vol.404 , pp. 711-731
    • Bertin, A.1    McMurray, M.A.2    Thai, L.3    Garcia, G.4    Votin, V.5    Grob, P.6    Allyn, T.7    Thorner, J.8    Nogales, E.9
  • 34
    • 84873140093 scopus 로고    scopus 로고
    • Septin phosphorylation and coiled-coil domains function in cell and septin ring morphology in the filamentous fungus Ashbya gossypii
    • Meseroll, R. A., Occhipinti, P., and Gladfelter, A. S. (2013) Septin phosphorylation and coiled-coil domains function in cell and septin ring morphology in the filamentous fungus Ashbya gossypii. Eukaryot. Cell 12, 182-193
    • (2013) Eukaryot. Cell , vol.12 , pp. 182-193
    • Meseroll, R.A.1    Occhipinti, P.2    Gladfelter, A.S.3
  • 36
    • 14444286600 scopus 로고    scopus 로고
    • Polymerization of purified yeast septins: Evidence that organized filament arrays may not be required for septin function
    • Frazier, J. A., Wong, M. L., Longtine, M. S., Pringle, J. R., Mann, M., Mitchison, T. J., and Field, C. (1998) Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function. J. Cell Biol. 143, 737-749
    • (1998) J. Cell Biol. , vol.143 , pp. 737-749
    • Frazier, J.A.1    Wong, M.L.2    Longtine, M.S.3    Pringle, J.R.4    Mann, M.5    Mitchison, T.J.6    Field, C.7
  • 41
    • 84923321595 scopus 로고    scopus 로고
    • Architecture and dynamic remodelling of the septin cytoskeleton during the cell cycle
    • Ong, K., Wloka, C., Okada, S., Svitkina, T., and Bi, E. (2014) Architecture and dynamic remodelling of the septin cytoskeleton during the cell cycle. Nat. Commun. 5, 5698
    • (2014) Nat. Commun. , vol.5 , pp. 5698
    • Ong, K.1    Wloka, C.2    Okada, S.3    Svitkina, T.4    Bi, E.5
  • 45
    • 77954841928 scopus 로고    scopus 로고
    • A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution
    • Hu, Q., Milenkovic, L., Jin, H., Scott, M. P., Nachury, M. V., Spiliotis, E. T., and Nelson, W. J. (2010) A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution. Science 329, 436-439
    • (2010) Science , vol.329 , pp. 436-439
    • Hu, Q.1    Milenkovic, L.2    Jin, H.3    Scott, M.P.4    Nachury, M.V.5    Spiliotis, E.T.6    Nelson, W.J.7
  • 46
    • 79960597240 scopus 로고    scopus 로고
    • Septin 6 regulates the cytoarchitecture of neurons through localization at dendritic branch points and bases of protrusions
    • Cho, S. J., Lee, H., Dutta, S., Song, J., Walikonis, R., and Moon, I. S. (2011) Septin 6 regulates the cytoarchitecture of neurons through localization at dendritic branch points and bases of protrusions. Mol. Cells 32, 89-98
    • (2011) Mol. Cells , vol.32 , pp. 89-98
    • Cho, S.J.1    Lee, H.2    Dutta, S.3    Song, J.4    Walikonis, R.5    Moon, I.S.6
  • 47
    • 78649656769 scopus 로고    scopus 로고
    • Guides to the final frontier of the cytoskeleton: Septins in filamentous fungi
    • Gladfelter, A. S. (2010) Guides to the final frontier of the cytoskeleton: septins in filamentous fungi. Curr. Opin. Microbiol. 13, 720-726
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 720-726
    • Gladfelter, A.S.1
  • 48
    • 65249171464 scopus 로고    scopus 로고
    • Regulation of distinct septin rings in a single cell by Elm1p and Gin4p kinases
    • DeMay, B. S., Meseroll, R. A., Occhipinti, P., and Gladfelter, A. S. (2009) Regulation of distinct septin rings in a single cell by Elm1p and Gin4p kinases. Mol. Biol. Cell 20, 2311-2326
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2311-2326
    • DeMay, B.S.1    Meseroll, R.A.2    Occhipinti, P.3    Gladfelter, A.S.4
  • 49
    • 30844461245 scopus 로고    scopus 로고
    • Diversity of septin scaffolds
    • Kinoshita, M. (2006) Diversity of septin scaffolds. Curr. Opin. Cell Biol. 18, 54-60
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 54-60
    • Kinoshita, M.1
  • 50
    • 71049147069 scopus 로고    scopus 로고
    • Septins: Molecular partitioning and the generation of cellular asymmetry
    • McMurray, M. A., and Thorner, J. (2009) Septins: molecular partitioning and the generation of cellular asymmetry. Cell Div. 4, 18
    • (2009) Cell Div , vol.4 , pp. 18
    • McMurray, M.A.1    Thorner, J.2
  • 51
    • 23044500737 scopus 로고    scopus 로고
    • Role of the septin ring in the asymmetric localization of proteins at the mother-bud neck in Saccharomyces cerevisiae
    • Kozubowski, L., Larson, J. R., and Tatchell, K. (2005) Role of the septin ring in the asymmetric localization of proteins at the mother-bud neck in Saccharomyces cerevisiae. Mol. Biol. Cell 16, 3455-3466
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3455-3466
    • Kozubowski, L.1    Larson, J.R.2    Tatchell, K.3
  • 52
    • 84875442981 scopus 로고    scopus 로고
    • Feedback control of Swe1p degradation in the yeast morphogenesis checkpoint
    • King, K., Kang, H., Jin, M., and Lew, D. J. (2013) Feedback control of Swe1p degradation in the yeast morphogenesis checkpoint. Mol. Biol. Cell 24, 914-922
    • (2013) Mol. Biol. Cell , vol.24 , pp. 914-922
    • King, K.1    Kang, H.2    Jin, M.3    Lew, D.J.4
  • 53
    • 84901020800 scopus 로고    scopus 로고
    • Anillin-dependent organization of septin filaments promotes intercellular bridge elongation and Chmp4B targeting to the abscission site
    • Renshaw, M. J., Liu, J., Lavoie, B. D., and Wilde, A. (2014) Anillin-dependent organization of septin filaments promotes intercellular bridge elongation and Chmp4B targeting to the abscission site. Open Biol. 4, 130190
    • (2014) Open Biol , vol.4 , pp. 130190
    • Renshaw, M.J.1    Liu, J.2    Lavoie, B.D.3    Wilde, A.4
  • 54
    • 79955513613 scopus 로고    scopus 로고
    • The chromosomal passenger complex and centralspindlin independently contribute to contractile ring assembly
    • Lewellyn, L., Carvalho, A., Desai, A., Maddox, A. S., and Oegema, K. (2011) The chromosomal passenger complex and centralspindlin independently contribute to contractile ring assembly. J. Cell Biol. 193, 155-169
    • (2011) J. Cell Biol , vol.193 , pp. 155-169
    • Lewellyn, L.1    Carvalho, A.2    Desai, A.3    Maddox, A.S.4    Oegema, K.5
  • 55
    • 34247618242 scopus 로고    scopus 로고
    • Anillin and the septins promote asymmetric ingression of the cytokinetic furrow
    • Maddox, A. S., Lewellyn, L., Desai, A., and Oegema, K. (2007) Anillin and the septins promote asymmetric ingression of the cytokinetic furrow. Dev. Cell 12, 827-835
    • (2007) Dev. Cell , vol.12 , pp. 827-835
    • Maddox, A.S.1    Lewellyn, L.2    Desai, A.3    Oegema, K.4
  • 56
    • 84862908732 scopus 로고    scopus 로고
    • SEPT9 occupies the terminal positions in septin octamers and mediates polymerization-dependent functions in abscission
    • Kim, M. S., Froese, C. D., Estey, M. P., and Trimble, W. S. (2011) SEPT9 occupies the terminal positions in septin octamers and mediates polymerization-dependent functions in abscission. J. Cell Biol. 195, 815-826
    • (2011) J. Cell Biol. , vol.195 , pp. 815-826
    • Kim, M.S.1    Froese, C.D.2    Estey, M.P.3    Trimble, W.S.4
  • 58
    • 84857035575 scopus 로고    scopus 로고
    • Anillin acts as a bifunctional linker coordinating midbody ring biogenesis during cytokinesis
    • Kechad, A., Jananji, S., Ruella, Y., and Hickson, G. R. (2012) Anillin acts as a bifunctional linker coordinating midbody ring biogenesis during cytokinesis. Curr. Biol. 22, 197-203
    • (2012) Curr. Biol. , vol.22 , pp. 197-203
    • Kechad, A.1    Jananji, S.2    Ruella, Y.3    Hickson, G.R.4
  • 59
    • 84890148738 scopus 로고    scopus 로고
    • Opposing actions of septins and Sticky on Anillin promote the transition from contractile to midbody ring
    • El Amine, N., Kechad, A., Jananji, S., and Hickson, G. R. (2013) Opposing actions of septins and Sticky on Anillin promote the transition from contractile to midbody ring. J. Cell Biol. 203, 487-504
    • (2013) J. Cell Biol. , vol.203 , pp. 487-504
    • El Amine, N.1    Kechad, A.2    Jananji, S.3    Hickson, G.R.4
  • 62
    • 79959755284 scopus 로고    scopus 로고
    • A role for septins in the interaction between the Listeria monocytogenes invasion protein InlB and the Met receptor
    • Mostowy, S., Janel, S., Forestier, C., Roduit, C., Kasas, S., Pizarro-Cerdá, J., Cossart, P., and Lafont, F. (2011) A role for septins in the interaction between the Listeria monocytogenes invasion protein InlB and the Met receptor. Biophys. J. 100, 1949-1959
    • (2011) Biophys. J. , vol.100 , pp. 1949-1959
    • Mostowy, S.1    Janel, S.2    Forestier, C.3    Roduit, C.4    Kasas, S.5    Pizarro-Cerdá, J.6    Cossart, P.7    Lafont, F.8
  • 63
    • 84863011435 scopus 로고    scopus 로고
    • The septin cytoskeleton facilitates membrane retraction during motility and blebbing
    • Gilden, J. K., Peck, S., Chen, Y. C., and Krummel, M. F. (2012) The septin cytoskeleton facilitates membrane retraction during motility and blebbing. J. Cell Biol. 196, 103-114
    • (2012) J. Cell Biol. , vol.196 , pp. 103-114
    • Gilden, J.K.1    Peck, S.2    Chen, Y.C.3    Krummel, M.F.4
  • 64
    • 80052776185 scopus 로고    scopus 로고
    • The mother-bud neck as a signaling platform for the coordination between spindle position and cytokinesis in budding yeast
    • Merlini, L., and Piatti, S. (2011) The mother-bud neck as a signaling platform for the coordination between spindle position and cytokinesis in budding yeast. Biol. Chem. 392, 805-812
    • (2011) Biol. Chem. , vol.392 , pp. 805-812
    • Merlini, L.1    Piatti, S.2
  • 65
    • 82655181327 scopus 로고    scopus 로고
    • Microtubules support a disk-like septin arrangement at the plasma membrane of mammalian cells
    • Sellin, M. E., Holmfeldt, P., Stenmark, S., and Gullberg, M. (2011) Microtubules support a disk-like septin arrangement at the plasma membrane of mammalian cells. Mol. Biol. Cell 22, 4588-4601
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4588-4601
    • Sellin, M.E.1    Holmfeldt, P.2    Stenmark, S.3    Gullberg, M.4
  • 67
    • 79961115058 scopus 로고    scopus 로고
    • Septin GTPases spatially guide microtubule organization and plus end dynamics in polarizing epithelia
    • Bowen, J. R., Hwang, D., Bai, X., Roy, D., and Spiliotis, E. T. (2011) Septin GTPases spatially guide microtubule organization and plus end dynamics in polarizing epithelia. J. Cell Biol. 194, 187-197
    • (2011) J. Cell Biol. , vol.194 , pp. 187-197
    • Bowen, J.R.1    Hwang, D.2    Bai, X.3    Roy, D.4    Spiliotis, E.T.5
  • 68
    • 26244468767 scopus 로고    scopus 로고
    • Mammalian septins regulate microtubule stability through interaction with the microtubulebinding protein MAP4
    • Kremer, B. E., Haystead, T., and Macara, I. G. (2005) Mammalian septins regulate microtubule stability through interaction with the microtubulebinding protein MAP4. Mol. Biol. Cell 16, 4648-4659
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4648-4659
    • Kremer, B.E.1    Haystead, T.2    Macara, I.G.3
  • 70
    • 84961289039 scopus 로고    scopus 로고
    • Barriers to the free diffusion of proteins and lipids in the plasma membrane
    • Trimble, W. S., and Grinstein, S. (2015) Barriers to the free diffusion of proteins and lipids in the plasma membrane. J. Cell Biol. 208, 259-271
    • (2015) J. Cell Biol. , vol.208 , pp. 259-271
    • Trimble, W.S.1    Grinstein, S.2
  • 72
    • 0034644626 scopus 로고    scopus 로고
    • Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier
    • Takizawa, P. A., DeRisi, J. L., Wilhelm, J. E., and Vale, R. D. (2000) Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier. Science 290, 341-344
    • (2000) Science , vol.290 , pp. 341-344
    • Takizawa, P.A.1    DeRisi, J.L.2    Wilhelm, J.E.3    Vale, R.D.4
  • 73
    • 0033636552 scopus 로고    scopus 로고
    • Compartmentalization of the cell cortex by septins is required for maintenance of cell polarity in yeast
    • Barral, Y., Mermall, V., Mooseker, M. S., and Snyder, M. (2000) Compartmentalization of the cell cortex by septins is required for maintenance of cell polarity in yeast. Mol. Cell 5, 841-851
    • (2000) Mol. Cell , vol.5 , pp. 841-851
    • Barral, Y.1    Mermall, V.2    Mooseker, M.S.3    Snyder, M.4
  • 74
    • 22344453326 scopus 로고    scopus 로고
    • Septin-dependent compartmentalization of the endoplasmic reticulum during yeast polarized growth
    • Luedeke, C., Frei, S. B., Sbalzarini, I., Schwarz, H., Spang, A., and Barral, Y. (2005) Septin-dependent compartmentalization of the endoplasmic reticulum during yeast polarized growth. J. Cell Biol. 169, 897-908
    • (2005) J. Cell Biol. , vol.169 , pp. 897-908
    • Luedeke, C.1    Frei, S.B.2    Sbalzarini, I.3    Schwarz, H.4    Spang, A.5    Barral, Y.6
  • 76
    • 3142729153 scopus 로고    scopus 로고
    • Spatial coordination of cytokinetic events by compartmentalization of the cell cortex
    • Dobbelaere, J., and Barral, Y. (2004) Spatial coordination of cytokinetic events by compartmentalization of the cell cortex. Science 305, 393-396
    • (2004) Science , vol.305 , pp. 393-396
    • Dobbelaere, J.1    Barral, Y.2
  • 77
    • 80052698947 scopus 로고    scopus 로고
    • Evidence that a septin diffusion barrier is dispensable for cytokinesis in budding yeast
    • Wloka, C., Nishihama, R., Onishi, M., Oh, Y., Hanna, J., Pringle, J. R., Krauss, M., and Bi, E. (2011) Evidence that a septin diffusion barrier is dispensable for cytokinesis in budding yeast. Biol. Chem. 392, 813-829
    • (2011) Biol. Chem. , vol.392 , pp. 813-829
    • Wloka, C.1    Nishihama, R.2    Onishi, M.3    Oh, Y.4    Hanna, J.5    Pringle, J.R.6    Krauss, M.7    Bi, E.8
  • 78
    • 80052964158 scopus 로고    scopus 로고
    • Submembranous septins as relatively stable components of actin-based membrane skeleton
    • Hagiwara, A., Tanaka, Y., Hikawa, R., Morone, N., Kusumi, A., Kimura, H., and Kinoshita, M. (2011) Submembranous septins as relatively stable components of actin-based membrane skeleton. Cytoskeleton 68, 512-525
    • (2011) Cytoskeleton , vol.68 , pp. 512-525
    • Hagiwara, A.1    Tanaka, Y.2    Hikawa, R.3    Morone, N.4    Kusumi, A.5    Kimura, H.6    Kinoshita, M.7
  • 79
    • 0037474299 scopus 로고    scopus 로고
    • Borg/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments
    • Sheffield, P. J., Oliver, C. J., Kremer, B. E., Sheng, S., Shao, Z., and Macara, I. G. (2003) Borg/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments. J. Biol. Chem. 278, 3483-3488
    • (2003) J. Biol. Chem. , vol.278 , pp. 3483-3488
    • Sheffield, P.J.1    Oliver, C.J.2    Kremer, B.E.3    Sheng, S.4    Shao, Z.5    Macara, I.G.6
  • 80
    • 26844470092 scopus 로고    scopus 로고
    • Nucleotide binding and filament assembly of recombinant yeast septin complexes
    • Farkasovsky, M., Herter, P., Voss, B., and Wittinghofer, A. (2005) Nucleotide binding and filament assembly of recombinant yeast septin complexes. Biol. Chem. 386, 643-656
    • (2005) Biol. Chem. , vol.386 , pp. 643-656
    • Farkasovsky, M.1    Herter, P.2    Voss, B.3    Wittinghofer, A.4
  • 81
    • 63049129910 scopus 로고    scopus 로고
    • Drosophila Orc6 facilitates GTPase activity and filament formation of the septin complex
    • Huijbregts, R. P., Svitin, A., Stinnett, M. W., Renfrow, M. B., and Chesnokov, I. (2009) Drosophila Orc6 facilitates GTPase activity and filament formation of the septin complex. Mol. Biol. Cell 20, 270-281
    • (2009) Mol. Biol. Cell , vol.20 , pp. 270-281
    • Huijbregts, R.P.1    Svitin, A.2    Stinnett, M.W.3    Renfrow, M.B.4    Chesnokov, I.5
  • 82
    • 84901339707 scopus 로고    scopus 로고
    • Higher-order septin assembly is driven by GTP-promoted conformational changes: Evidence from unbiased mutational analysis in Saccharomyces cerevisiae
    • Weems, A. D., Johnson, C. R., Argueso, J. L., and McMurray, M. A. (2014) Higher-order septin assembly is driven by GTP-promoted conformational changes: evidence from unbiased mutational analysis in Saccharomyces cerevisiae. Genetics 196, 711-27
    • (2014) Genetics , vol.196 , pp. 711-727
    • Weems, A.D.1    Johnson, C.R.2    Argueso, J.L.3    McMurray, M.A.4
  • 83
    • 0037137437 scopus 로고    scopus 로고
    • Cytoskeleton: What does GTP do for septins?
    • Mitchison, T. J., and Field, C. M. (2002) Cytoskeleton: what does GTP do for septins? Curr. Biol. 12, R788-790
    • (2002) Curr. Biol. , vol.12 , pp. R788-R790
    • Mitchison, T.J.1    Field, C.M.2
  • 84
    • 1442337555 scopus 로고    scopus 로고
    • The majority of the Saccharomyces cerevisiae septin complexes do not exchange guanine nucleotides
    • Vrabioiu, A. M., Gerber, S. A., Gygi, S. P., Field, C. M., and Mitchison, T. J. (2004) The majority of the Saccharomyces cerevisiae septin complexes do not exchange guanine nucleotides. J. Biol. Chem. 279, 3111-3118
    • (2004) J. Biol. Chem. , vol.279 , pp. 3111-3118
    • Vrabioiu, A.M.1    Gerber, S.A.2    Gygi, S.P.3    Field, C.M.4    Mitchison, T.J.5
  • 85
    • 49649105136 scopus 로고    scopus 로고
    • Septin stability and recycling during dynamic structural transitions in cell division and development
    • McMurray, M. A., and Thorner, J. (2008) Septin stability and recycling during dynamic structural transitions in cell division and development. Curr. Biol. 18, 1203-1208
    • (2008) Curr. Biol. , vol.18 , pp. 1203-1208
    • McMurray, M.A.1    Thorner, J.2
  • 86
    • 1442334322 scopus 로고    scopus 로고
    • Septin collar formation in budding yeast requires GTP binding and direct phosphorylation by the PAK, Cla4
    • Versele, M., and Thorner, J. (2004) Septin collar formation in budding yeast requires GTP binding and direct phosphorylation by the PAK, Cla4. J. Cell Biol. 164, 701-715
    • (2004) J. Cell Biol. , vol.164 , pp. 701-715
    • Versele, M.1    Thorner, J.2
  • 87
    • 84893472708 scopus 로고    scopus 로고
    • Endosomal transport of septin mRNA and protein indicates local translation on endosomes and is required for correct septin filamentation
    • Baumann, S., König, J., Koepke, J., and Feldbrügge, M. (2014) Endosomal transport of septin mRNA and protein indicates local translation on endosomes and is required for correct septin filamentation. EMBO Rep. 15, 94-102
    • (2014) EMBO Rep , vol.15 , pp. 94-102
    • Baumann, S.1    König, J.2    Koepke, J.3    Feldbrügge, M.4
  • 88
    • 80052245849 scopus 로고    scopus 로고
    • Deciphering the rules governing assembly order of mammalian septin complexes
    • Sellin, M. E., Sandblad, L., Stenmark, S., and Gullberg, M. (2011) Deciphering the rules governing assembly order of mammalian septin complexes. Mol. Biol. Cell 22, 3152-3164
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3152-3164
    • Sellin, M.E.1    Sandblad, L.2    Stenmark, S.3    Gullberg, M.4
  • 89
    • 58349115398 scopus 로고    scopus 로고
    • Septinmediated uniform bracing of phospholipid membranes
    • Tanaka-Takiguchi, Y., Kinoshita, M., and Takiguchi, K. (2009) Septinmediated uniform bracing of phospholipid membranes. Curr. Biol. 19, 140-145
    • (2009) Curr. Biol. , vol.19 , pp. 140-145
    • Tanaka-Takiguchi, Y.1    Kinoshita, M.2    Takiguchi, K.3
  • 92
    • 0141541745 scopus 로고    scopus 로고
    • The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast
    • Caviston, J. P., Longtine, M., Pringle, J. R., and Bi, E. (2003) The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast. Mol. Biol. Cell 14, 4051-4066
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4051-4066
    • Caviston, J.P.1    Longtine, M.2    Pringle, J.R.3    Bi, E.4
  • 93
    • 0037148528 scopus 로고    scopus 로고
    • Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p
    • Gladfelter, A. S., Bose, I., Zyla, T. R., Bardes, E. S., and Lew, D. J. (2002) Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p. J. Cell Biol. 156, 315-326
    • (2002) J. Cell Biol. , vol.156 , pp. 315-326
    • Gladfelter, A.S.1    Bose, I.2    Zyla, T.R.3    Bardes, E.S.4    Lew, D.J.5
  • 95
    • 84880946030 scopus 로고    scopus 로고
    • Daughter cell identity emerges from the interplay of Cdc42, septins, and exocytosis
    • Okada, S., Leda, M., Hanna, J., Savage, N. S., Bi, E., and Goryachev, A. B. (2013) Daughter cell identity emerges from the interplay of Cdc42, septins, and exocytosis. Dev. Cell 26, 148-161
    • (2013) Dev. Cell , vol.26 , pp. 148-161
    • Okada, S.1    Leda, M.2    Hanna, J.3    Savage, N.S.4    Bi, E.5    Goryachev, A.B.6
  • 96
    • 0017153996 scopus 로고
    • A highly ordered ring of membraneassociated filaments in budding yeast
    • Byers, B., and Goetsch, L. (1976) A highly ordered ring of membraneassociated filaments in budding yeast. J. Cell Biol. 69, 717-721
    • (1976) J. Cell Biol. , vol.69 , pp. 717-721
    • Byers, B.1    Goetsch, L.2
  • 98
    • 33749165924 scopus 로고    scopus 로고
    • Structural insights into yeast septin organization from polarized fluorescence microscopy
    • Vrabioiu, A. M., and Mitchison, T. J. (2006) Structural insights into yeast septin organization from polarized fluorescence microscopy. Nature 443, 466-469
    • (2006) Nature , vol.443 , pp. 466-469
    • Vrabioiu, A.M.1    Mitchison, T.J.2
  • 99
    • 84872277354 scopus 로고    scopus 로고
    • Posttranslational modifications and assembly of septin heteropolymers and higher-order structures
    • Hernández-Rodríguez, Y., and Momany, M. (2012) Posttranslational modifications and assembly of septin heteropolymers and higher-order structures. Curr. Opin. Microbiol. 15, 660-668
    • (2012) Curr. Opin. Microbiol. , vol.15 , pp. 660-668
    • Hernández-Rodríguez, Y.1    Momany, M.2


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