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Volumn , Issue , 2008, Pages 147-168

Septins in the Metazoan Model Systems Drosophila Melanogaster and Caenorhabditis Elegans

Author keywords

C. elegans; Cellularization; Cytokinesis; Drosophilia; Filament formation; Fly; GTP binding; Nervous system; Neural development; Septin complexes; Worm

Indexed keywords


EID: 65849405223     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470779705.ch6     Document Type: Chapter
Times cited : (6)

References (55)
  • 1
    • 0034494631 scopus 로고    scopus 로고
    • Evidence for functional differentiation among Drosophila septins in cytokinesis and cellularization
    • Adam, J.C., Pringle, J.R. and Peifer, M. (2000) Evidence for functional differentiation among Drosophila septins in cytokinesis and cellularization. Molecular Biology of the Cell, 11, 3123-35.
    • (2000) Molecular Biology of the Cell , vol.11 , pp. 3123-3135
    • Adam, J.C.1    Pringle, J.R.2    Peifer, M.3
  • 2
    • 12844270469 scopus 로고    scopus 로고
    • The role of septins in the morphogenesis of Schizosaccha-romyces pombe and Drosophila melanogaster
    • Ph.D. Dissertation, The University of North Carolina, Chapel Hill.
    • Al-Awar, O.S. (1996) The role of septins in the morphogenesis of Schizosaccha-romyces pombe and Drosophila melanogaster, Ph.D. Dissertation, The University of North Carolina, Chapel Hill.
    • (1996)
    • Al-Awar, O.S.1
  • 3
    • 0345236609 scopus 로고    scopus 로고
    • Mid2p stabilizes septin rings during cytokinesis in fission yeast
    • Berlin, A., Paoletti, A. and Chang, F. (2003) Mid2p stabilizes septin rings during cytokinesis in fission yeast. Journal of Cell Biology, 160, 1083-92.
    • (2003) Journal of Cell Biology , vol.160 , pp. 1083-1092
    • Berlin, A.1    Paoletti, A.2    Chang, F.3
  • 4
    • 0026026818 scopus 로고
    • The GTPase superfamily: conserved structure and molecular mechanism
    • Bourne, H.R., Sanders, D.A. and McCormick, F. (1991) The GTPase superfamily: conserved structure and molecular mechanism. Nature, 349, 117-27.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 5
    • 0017153996 scopus 로고
    • A highly ordered ring of membrane-associated filaments in budding yeast
    • Byers, B. and Goetsch, L. (1976) A highly ordered ring of membrane-associated filaments in budding yeast. Journal of Cell Biology, 69, 717-21.
    • (1976) Journal of Cell Biology , vol.69 , pp. 717-721
    • Byers, B.1    Goetsch, L.2
  • 6
    • 0032373709 scopus 로고    scopus 로고
    • Cellularization in Drosophila melanogaster is disrupted by the inhibition of Rho activity and the activation of Cdc42 function
    • Crawford, J.M., Harden, N., Leung, T. et al. (1998) Cellularization in Drosophila melanogaster is disrupted by the inhibition of Rho activity and the activation of Cdc42 function. Developmental Biology, 204, 151-64.
    • (1998) Developmental Biology , vol.204 , pp. 151-164
    • Crawford, J.M.1    Harden, N.2    Leung, T.3
  • 7
    • 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, 393-96.
    • (2004) Science , vol.305 , pp. 393-396
    • Dobbelaere, J.1    Barral, Y.2
  • 8
    • 4544374422 scopus 로고    scopus 로고
    • Terminal cytokinesis events uncovered after an RNAi screen
    • Echard, A., Hickson, G.R.X., Foley, E. and O'Farrell, P.H. (2004) Terminal cytokinesis events uncovered after an RNAi screen. Current Biology, 14, 1685-93.
    • (2004) Current Biology , vol.14 , pp. 1685-1693
    • Echard, A.1    Hickson, G.R.X.2    Foley, E.3    O'Farrell, P.H.4
  • 10
    • 34347239315 scopus 로고    scopus 로고
    • The MARVEL domain protein, Singles Bar, is required for progression past the pre-fusion complex stage of myoblast fusion
    • Estrada, B., Maeland, A.D., Gisselbrecht, S.S. et al. (2007) The MARVEL domain protein, Singles Bar, is required for progression past the pre-fusion complex stage of myoblast fusion. Developmental Biology, 307, 328-39.
    • (2007) Developmental Biology , vol.307 , pp. 328-339
    • Estrada, B.1    Maeland, A.D.2    Gisselbrecht, S.S.3
  • 12
    • 0029154616 scopus 로고
    • Anillin, a contractile ring protein that cycles from the nucleus to the cell cortex
    • Field, C.M. and Alberts, B.M. (1995) Anillin, a contractile ring protein that cycles from the nucleus to the cell cortex. Journal of Cell Biology, 131, 165-78.
    • (1995) Journal of Cell Biology , vol.131 , pp. 165-178
    • Field, C.M.1    Alberts, B.M.2
  • 13
    • 0029982293 scopus 로고    scopus 로고
    • A purified Drosophila septin complex forms filaments and exhibits GTPase activity
    • Field, C.M., Al-Awar, O., Rosenblatt, J. et al. (1996) A purified Drosophila septin complex forms filaments and exhibits GTPase activity. Journal of Cell Biology, 133, 605-16.
    • (1996) Journal of Cell Biology , vol.133 , pp. 605-616
    • Field, C.M.1    Al-Awar, O.2    Rosenblatt, J.3
  • 14
    • 21644435926 scopus 로고    scopus 로고
    • Characterization of anillin mutants reveals essential roles in septin localization and plasma membrane integrity
    • Field, C.M., Coughlin, M., Doberstein, S. et al. (2005) Characterization of anillin mutants reveals essential roles in septin localization and plasma membrane integrity. Development, 132, 2849-60.
    • (2005) Development , vol.132 , pp. 2849-2860
    • Field, C.M.1    Coughlin, M.2    Doberstein, S.3
  • 15
    • 0042663892 scopus 로고    scopus 로고
    • A role for septins in cellular and axonal migration in C. elegans
    • Finger, F.P., Kopish, K.R. and White, J.G. (2003) A role for septins in cellular and axonal migration in C. elegans. Developmental Biology, 261, 220-34.
    • (2003) Developmental Biology , vol.261 , pp. 220-234
    • Finger, F.P.1    Kopish, K.R.2    White, J.G.3
  • 16
    • 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. et al. (1998) Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function. Journal of Cell Biology, 143, 737-49.
    • (1998) Journal of Cell Biology , vol.143 , pp. 737-749
    • Frazier, J.A.1    Wong, M.L.2    Longtine, M.S.3
  • 17
    • 0345600247 scopus 로고    scopus 로고
    • A protein interaction map of Drosophila melanogaster
    • Giot, L., Bader, J.S., Brouwer, C. et al. (2003) A protein interaction map of Drosophila melanogaster. Science, 302, 1727-36.
    • (2003) Science , vol.302 , pp. 1727-1736
    • Giot, L.1    Bader, J.S.2    Brouwer, C.3
  • 19
    • 84889479471 scopus 로고    scopus 로고
    • Genetic analysis of the Sep2 and Sep5 septins
    • Abstracts of the 41st Annual Drosophila Research Conference, a158 (Abstract), Pittsburgh, Pennsylvania.
    • Hales, K.G., Peifer, M. and Pringle, J.R. (2000) Genetic analysis of the Sep2 and Sep5 septins. Abstracts of the 41st Annual Drosophila Research Conference, a158 (Abstract), Pittsburgh, Pennsylvania.
    • (2000)
    • Hales, K.G.1    Peifer, M.2    Pringle, J.R.3
  • 21
    • 0030474931 scopus 로고    scopus 로고
    • Assembly of ring canals in the male germ line from structural components of the contractile ring
    • Hime, G.R., Brill, J.A. and Fuller, M.T. (1996) Assembly of ring canals in the male germ line from structural components of the contractile ring. Journal of Cell Science, 109, 2779-88.
    • (1996) Journal of Cell Science , vol.109 , pp. 2779-2788
    • Hime, G.R.1    Brill, J.A.2    Fuller, M.T.3
  • 22
    • 0032103420 scopus 로고    scopus 로고
    • Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments
    • Hsu, S.-C., Hazuka, C.D., Roth, R. et al. (1998) Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments. Neuron, 20, 1111-22.
    • (1998) Neuron , vol.20 , pp. 1111-1122
    • Hsu, S.-C.1    Hazuka, C.D.2    Roth, R.3
  • 23
    • 34547211102 scopus 로고    scopus 로고
    • The Caenorhabditis elegans septin complex is nonpolar
    • John, C.M., Hite, R.K., Weirich, C.S. et al. (2007) The Caenorhabditis elegans septin complex is nonpolar. EMBO Journal, 26, 3296-307.
    • (2007) EMBO Journal , vol.26 , pp. 3296-3307
    • John, C.M.1    Hite, R.K.2    Weirich, C.S.3
  • 24
    • 0036898823 scopus 로고    scopus 로고
    • Self-and actin-templated assembly of mammalian septins
    • Kinoshita, M., Field, C.M., Coughlin, M.L. et al. (2002) Self-and actin-templated assembly of mammalian septins. Developmental Cell, 3, 791-802.
    • (2002) Developmental Cell , vol.3 , pp. 791-802
    • Kinoshita, M.1    Field, C.M.2    Coughlin, M.L.3
  • 25
    • 0030943556 scopus 로고    scopus 로고
    • Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures
    • Kinoshita, M., Kumar, S., Mizoguchi, A. et al. (1997) Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures. Genes and Development, 11, 1535-47.
    • (1997) Genes and Development , vol.11 , pp. 1535-1547
    • Kinoshita, M.1    Kumar, S.2    Mizoguchi, A.3
  • 26
    • 0037338867 scopus 로고    scopus 로고
    • The spindle-associated transmembrane protein Axs identifies a membranous structure ensheathing the meiotic spindle
    • Kramer, J. and Hawley, R.S. (2003) The spindle-associated transmembrane protein Axs identifies a membranous structure ensheathing the meiotic spindle. Nature Cell Biology, 5, 261-63.
    • (2003) Nature Cell Biology , vol.5 , pp. 261-263
    • Kramer, J.1    Hawley, R.S.2
  • 27
    • 26244468767 scopus 로고    scopus 로고
    • Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4
    • Kremer, B.E., Haystead, T. and Macara, I.G. (2005) Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4. Molecular Biology of the Cell, 16, 4648-59.
    • (2005) Molecular Biology of the Cell , vol.16 , pp. 4648-4659
    • Kremer, B.E.1    Haystead, T.2    Macara, I.G.3
  • 29
    • 21644444741 scopus 로고    scopus 로고
    • Distinct roles for two C. elegans anillins in the gonad and early embryo
    • Maddox, A.S., Habermann, B., Desai, A. and Oegema, K. (2005) Distinct roles for two C. elegans anillins in the gonad and early embryo. Development, 132, 2837-48.
    • (2005) Development , vol.132 , pp. 2837-2848
    • Maddox, A.S.1    Habermann, B.2    Desai, A.3    Oegema, K.4
  • 30
    • 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. Developmental Cell, 12, 827-35.
    • (2007) Developmental Cell , vol.12 , pp. 827-835
    • Maddox, A.S.1    Lewellyn, L.2    Desai, A.3    Oegema, K.4
  • 32
    • 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? Current Biology, 12, R788-90.
    • (2002) Current Biology , vol.12
    • Mitchison, T.J.1    Field, C.M.2
  • 33
    • 36248991758 scopus 로고    scopus 로고
    • Overexpression of Septin 4, the Drosophila homologue of human CDCrel-1, is toxic for dopaminergic neurons
    • Munoz-Soriano, V. and Paricio, N. (2007) Overexpression of Septin 4, the Drosophila homologue of human CDCrel-1, is toxic for dopaminergic neurons. The European Journal of Neuroscience, 26, 3150-58.
    • (2007) The European Journal of Neuroscience , vol.26 , pp. 3150-3158
    • Munoz-Soriano, V.1    Paricio, N.2
  • 34
    • 0028175009 scopus 로고
    • The Drosophila peanut gene is required for cytokinesis and encodes a protein similar to yeast putative bud neck filament proteins
    • Neufeld, T.P. and Rubin, G.M. (1994) The Drosophila peanut gene is required for cytokinesis and encodes a protein similar to yeast putative bud neck filament proteins. Cell, 77, 371-79.
    • (1994) Cell , vol.77 , pp. 371-379
    • Neufeld, T.P.1    Rubin, G.M.2
  • 35
    • 0033677841 scopus 로고    scopus 로고
    • The C. elegans septin genes, unc-59 and unc-61, are required for normal postembryonic cytokineses and morphogenesis but have no essential function in embryogenesis
    • Nguyen, T.Q., Sawa, H., Okano, H. and White, J.G. (2000) The C. elegans septin genes, unc-59 and unc-61, are required for normal postembryonic cytokineses and morphogenesis but have no essential function in embryogenesis. Journal of Cell Science, 113, 3825-37.
    • (2000) Journal of Cell Science , vol.113 , pp. 3825-3837
    • Nguyen, T.Q.1    Sawa, H.2    Okano, H.3    White, J.G.4
  • 36
    • 0034618062 scopus 로고    scopus 로고
    • Functional analysis of a human homologue of the Drosophila actin binding protein anillin suggests a role in cytokinesis
    • Oegema, K., Savoian, M.S., Mitchison, T.J. and Field, C.M. (2000) Functional analysis of a human homologue of the Drosophila actin binding protein anillin suggests a role in cytokinesis. Journal of Cell Biology, 150, 539-51.
    • (2000) Journal of Cell Biology , vol.150 , pp. 539-551
    • Oegema, K.1    Savoian, M.S.2    Mitchison, T.J.3    Field, C.M.4
  • 37
    • 34547121710 scopus 로고    scopus 로고
    • Analysis of septins across kingdoms reveals orthology and new motifs
    • Pan, F., Malmberg, R.L. and Momany, M. (2007) Analysis of septins across kingdoms reveals orthology and new motifs. BMC Evolutionary Biology, 7, 103.
    • (2007) BMC Evolutionary Biology , vol.7 , pp. 103
    • Pan, F.1    Malmberg, R.L.2    Momany, M.3
  • 38
    • 11144311144 scopus 로고    scopus 로고
    • Actin and septin ultrastructures at the budding yeast cell cortex
    • Rodal, A.A., Kozubowski, L., Goode, B.L. et al. (2005) Actin and septin ultrastructures at the budding yeast cell cortex. Molecular Biology of the Cell, 16, 372-84.
    • (2005) Molecular Biology of the Cell , vol.16 , pp. 372-384
    • Rodal, A.A.1    Kozubowski, L.2    Goode, B.L.3
  • 39
    • 0035853825 scopus 로고    scopus 로고
    • Polymerizatin of FtsZ, a bacterial homolog of tubulin: is assembly cooperative?
    • Romberg, L., Simon, M. and Erickson, H.P. (2001) Polymerizatin of FtsZ, a bacterial homolog of tubulin: is assembly cooperative? Journal of Biological Chemistry, 276, 11743-53.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 11743-11753
    • Romberg, L.1    Simon, M.2    Erickson, H.P.3
  • 40
    • 0742270614 scopus 로고    scopus 로고
    • Reassessing the role and dynamics of nonmuscle myosin II during furrow formation in early Drosophila embryos
    • Royou, A., Field, C., Sisson, J.C. et al. (2004) Reassessing the role and dynamics of nonmuscle myosin II during furrow formation in early Drosophila embryos. Molecular Biology of the Cell, 15, 838-50.
    • (2004) Molecular Biology of the Cell , vol.15 , pp. 838-850
    • Royou, A.1    Field, C.2    Sisson, J.C.3
  • 42
    • 0027481755 scopus 로고
    • Mutations affecting growth cone guidance in Drosophila: genes necessary for guidance toward or away from the midline
    • Seeger, M., Tear, G., Ferres-Marco, D. and Goodman, C.S. (1993) Mutations affecting growth cone guidance in Drosophila: genes necessary for guidance toward or away from the midline. Neuron, 10, 409-26.
    • (1993) Neuron , vol.10 , pp. 409-426
    • Seeger, M.1    Tear, G.2    Ferres-Marco, D.3    Goodman, C.S.4
  • 43
    • 0037087517 scopus 로고    scopus 로고
    • Identification of septin-interacting proteins and characterization of the Smt3/SUMO-conjugation system in Drosophila
    • Shih, H.-P., Hales, K.G., Pringle, J.R. and Peifer, M. (2002) Identification of septin-interacting proteins and characterization of the Smt3/SUMO-conjugation system in Drosophila. Journal of Cell Science, 115, 1259-71.
    • (2002) Journal of Cell Science , vol.115 , pp. 1259-1271
    • Shih, H.-P.1    Hales, K.G.2    Pringle, J.R.3    Peifer, M.4
  • 44
    • 0034645066 scopus 로고    scopus 로고
    • Lava Lamp, a novel peripheral Golgi protein, is required for Drosophila melanogaster cellularization
    • Sisson, J.C., Field, C., Ventura, R. et al. (2000) Lava Lamp, a novel peripheral Golgi protein, is required for Drosophila melanogaster cellularization. Journal of Cell Biology, 151, 905-17.
    • (2000) Journal of Cell Biology , vol.151 , pp. 905-917
    • Sisson, J.C.1    Field, C.2    Ventura, R.3
  • 45
    • 0036329002 scopus 로고    scopus 로고
    • Molecular dissection of cytokinesis by RNA interference in Drosophila cultured cells
    • Somma, M.P., Fasulo, B., Cenci, G. et al. (2002) Molecular dissection of cytokinesis by RNA interference in Drosophila cultured cells. Molecular Biology of the Cell, 13, 2448-60.
    • (2002) Molecular Biology of the Cell , vol.13 , pp. 2448-2460
    • Somma, M.P.1    Fasulo, B.2    Cenci, G.3
  • 46
    • 38749147682 scopus 로고    scopus 로고
    • Epithelial polarity requires septin coupling of vesicle transport to polyglutamylated microtubules
    • Spiliotis, E.T., Hunt, S.J., Hu, Q. et al. (2008) Epithelial polarity requires septin coupling of vesicle transport to polyglutamylated microtubules. Journal of Cell Biology, 180, 295-303.
    • (2008) Journal of Cell Biology , vol.180 , pp. 295-303
    • Spiliotis, E.T.1    Hunt, S.J.2    Hu, Q.3
  • 47
    • 15244346231 scopus 로고    scopus 로고
    • A mitotic septin scaffold required for mammalian chromosome congression and segregation
    • Spiliotis, E.T., Kinoshita, M. and Nelson, W.J. (2005) A mitotic septin scaffold required for mammalian chromosome congression and segregation. Science, 307, 1781-85.
    • (2005) Science , vol.307 , pp. 1781-1785
    • Spiliotis, E.T.1    Kinoshita, M.2    Nelson, W.J.3
  • 48
    • 11144333618 scopus 로고    scopus 로고
    • Anillin binds nonmuscle myosin II and regulates the contractile ring
    • Straight, A.F., Field, C.M. and Mitchison, T.J. (2005) Anillin binds nonmuscle myosin II and regulates the contractile ring. Molecular Biology of the Cell, 16, 193-201.
    • (2005) Molecular Biology of the Cell , vol.16 , pp. 193-201
    • Straight, A.F.1    Field, C.M.2    Mitchison, T.J.3
  • 49
    • 1442274704 scopus 로고    scopus 로고
    • Pathways for membrane trafficking during cytokinesis
    • Strickland, L.I. and Burgess, D.R. (2004) Pathways for membrane trafficking during cytokinesis. Trends in Cell Biology, 14, 115-18.
    • (2004) Trends in Cell Biology , vol.14 , pp. 115-118
    • Strickland, L.I.1    Burgess, D.R.2
  • 50
    • 0036798406 scopus 로고    scopus 로고
    • The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis
    • Surka, M.C., Tsang, C.W. and Trimble, W.S. (2002) The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis. Molecular Biology of the Cell, 13, 3532-45.
    • (2002) Molecular Biology of the Cell , vol.13 , pp. 3532-3545
    • Surka, M.C.1    Tsang, C.W.2    Trimble, W.S.3
  • 51
    • 0345057349 scopus 로고    scopus 로고
    • An anillin homologue, Mid2p, acts during fission yeast cytokinesis to organize the septin ring and promote cell separation
    • Tasto, J.J., Morrell, J.L. and Gould, K.L. (2003) An anillin homologue, Mid2p, acts during fission yeast cytokinesis to organize the septin ring and promote cell separation. Journal of Cell Biology, 160, 1093-103.
    • (2003) Journal of Cell Biology , vol.160 , pp. 1093-1103
    • Tasto, J.J.1    Morrell, J.L.2    Gould, K.L.3
  • 52
    • 1442337555 scopus 로고    scopus 로고
    • The majority of the Saccha-romyces cerevisiae septin complexes do not exchange guanine nucleotides
    • Vrabioiu, A.M., Gerber, S.A., Gygi, S.P. et al. (2004) The majority of the Saccha-romyces cerevisiae septin complexes do not exchange guanine nucleotides. Journal of Biological Chemistry, 279, 3111-18.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 3111-3118
    • Vrabioiu, A.M.1    Gerber, S.A.2    Gygi, S.P.3
  • 53
    • 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, 466-69.
    • (2006) Nature , vol.443 , pp. 466-469
    • Vrabioiu, A.M.1    Mitchison, T.J.2
  • 55
    • 0020485766 scopus 로고
    • Neurone differentiation in cell lineage mutants of Caenorhabditis elegans
    • White, J.G., Horvitz, H.R. and Sulston, J.E. (1982) Neurone differentiation in cell lineage mutants of Caenorhabditis elegans. Nature, 297, 584-87.
    • (1982) Nature , vol.297 , pp. 584-587
    • White, J.G.1    Horvitz, H.R.2    Sulston, J.E.3


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