메뉴 건너뛰기




Volumn 124, Issue 24, 2011, Pages 4141-4146

Septins at a glance

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN 10; CELL CYCLE PROTEIN 11; CELL CYCLE PROTEIN 12; CELL CYCLE PROTEIN 3; GUANINE NUCLEOTIDE; GUANOSINE TRIPHOSPHATASE; MIXED LINEAGE LEUKEMIA PROTEIN; SCAFFOLD PROTEIN; SEPTIN; SEPTIN 1; SEPTIN 2; SEPTIN 3; SEPTIN 4; SEPTIN 6; SEPTIN 7; UNCLASSIFIED DRUG;

EID: 84856812823     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.087007     Document Type: Article
Times cited : (40)

References (106)
  • 1
    • 0033555685 scopus 로고    scopus 로고
    • Nim1-related kinases coordinate cell cycle progression with the organization of the peripheral cytoskeleton in yeast
    • Barral, Y., Parra, M., Bidlingmaier, S. and Snyder, M.(1999). Nim1-related kinases coordinate cell cycle progression with the organization of the peripheral cytoskeleton in yeast. Genes Dev. 13, 176-187.
    • (1999) Genes Dev , vol.13 , pp. 176-187
    • Barral, Y.1    Parra, M.2    Bidlingmaier, S.3    Snyder, M.4
  • 2
    • 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
  • 3
    • 0033363646 scopus 로고    scopus 로고
    • The septin CDCrel-1 binds syntaxin and inhibits exocytosis
    • Beites, C. L., Xie, H., Bowser, R. and Trimble, W. S.(1999). The septin CDCrel-1 binds syntaxin and inhibits exocytosis. Nat. Neurosci. 2, 434-439.
    • (1999) Nat. Neurosci. , vol.2 , pp. 434-439
    • Beites, C.L.1    Xie, H.2    Bowser, R.3    Trimble, W.S.4
  • 4
    • 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. J. Cell Biol. 160, 1083-1092.
    • (2003) J. Cell Biol. , vol.160 , pp. 1083-1092
    • Berlin, A.1    Paoletti, A.2    Chang, F.3
  • 8
    • 36049050123 scopus 로고    scopus 로고
    • Phylogenetic and evolutionary analysis of the septin protein family in metazoan
    • Cao, L., Ding, X., Yu, W., Yang, X., Shen, S. and Yu, L.(2007). Phylogenetic and evolutionary analysis of the septin protein family in metazoan. FEBS Lett. 581, 5526-5532.
    • (2007) FEBS Lett , vol.581 , pp. 5526-5532
    • Cao, L.1    Ding, X.2    Yu, W.3    Yang, X.4    Shen, S.5    Yu, L.6
  • 9
    • 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
  • 10
    • 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
  • 12
    • 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
  • 15
    • 51049124338 scopus 로고    scopus 로고
    • GTP binding is required for SEPT12 to form filaments and to interact with SEPT11
    • Ding, X., Yu, W., Liu, M., Shen, S., Chen, F., Cao, L., Wan, B. and Yu, L.(2008). GTP binding is required for SEPT12 to form filaments and to interact with SEPT11. Mol. Cells 25, 385-389.
    • (2008) Mol. Cells , vol.25 , pp. 385-389
    • Ding, X.1    Yu, W.2    Liu, M.3    Shen, S.4    Chen, F.5    Cao, L.6    Wan, B.7    Yu, L.8
  • 16
    • 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
  • 17
    • 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
  • 19
    • 21644435926 scopus 로고    scopus 로고
    • Characterization of anillin mutants reveals essential roles in septin localization and plasma membrane integrity
    • Field, C. M., Coughlin, M. L., Doberstein, S., Marty, T. and Sullivan, W.(2005). Characterization of anillin mutants reveals essential roles in septin localization and plasma membrane integrity. Development 132, 2849-2860.
    • (2005) Development , vol.132 , pp. 2849-2860
    • Field, C.M.1    Coughlin, M.L.2    Doberstein, S.3    Marty, T.4    Sullivan, W.5
  • 20
    • 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
  • 23
    • 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. G. and Lew, D.(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.G.4    Lew, D.5
  • 24
    • 2342561882 scopus 로고    scopus 로고
    • The mitochondrial ARTS protein promotes apoptosis through targeting XIAP
    • Gottfried, Y., Rotem, A., Lotan, R., Steller, H. and Larisch, S.(2004). The mitochondrial ARTS protein promotes apoptosis through targeting XIAP. EMBO J. 23, 1627-1635.
    • (2004) EMBO J , vol.23 , pp. 1627-1635
    • Gottfried, Y.1    Rotem, A.2    Lotan, R.3    Steller, H.4    Larisch, S.5
  • 28
    • 0141750432 scopus 로고    scopus 로고
    • Cytoskeletal activation of a checkpoint kinase
    • Hanrahan, J. and Snyder, M.(2003). Cytoskeletal activation of a checkpoint kinase. Mol. Cell 12, 663-673.
    • (2003) Mol. Cell , vol.12 , pp. 663-673
    • Hanrahan, J.1    Snyder, M.2
  • 29
    • 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
  • 30
    • 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., Foletti, D. L., Heuser, J. and Scheller, R. H.(1998). Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments. Neuron 20, 1111-1122.
    • (1998) Neuron , vol.20 , pp. 1111-1122
    • Hsu, S.C.1    Hazuka, C.D.2    Roth, R.3    Foletti, D.L.4    Heuser, J.5    Scheller, R.H.6
  • 31
    • 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
  • 34
    • 0038342507 scopus 로고    scopus 로고
    • Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies
    • Ihara, M., Tomimoto, H., Kitayama, H., Morioka, Y., Akiguchi, I., Shibasaki, H., Noda, M. and Kinoshita, M.(2003). Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies. J. Biol. Chem. 278, 24095-24102.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24095-24102
    • Ihara, M.1    Tomimoto, H.2    Kitayama, H.3    Morioka, Y.4    Akiguchi, I.5    Shibasaki, H.6    Noda, M.7    Kinoshita, M.8
  • 35
    • 20044369350 scopus 로고    scopus 로고
    • Cortical organization by the septin cytoskeleton is essential for structural and mechanical integrity of mammalian spermatozoa
    • Ihara, M., Kinoshita, A., Yamada, S., Tanaka, H., Tanigaki, A., Kitano, A., Goto, M., Okubo, K., Nishiyama, H. and Ogawa, O.(2005). Cortical organization by the septin cytoskeleton is essential for structural and mechanical integrity of mammalian spermatozoa. Dev. Cell 8, 343-352.
    • (2005) Dev. Cell , vol.8 , pp. 343-352
    • Ihara, M.1    Kinoshita, A.2    Yamada, S.3    Tanaka, H.4    Tanigaki, A.5    Kitano, A.6    Goto, M.7    Okubo, K.8    Nishiyama, H.9    Ogawa, O.10
  • 36
    • 0035980069 scopus 로고    scopus 로고
    • Characterization of the CDC10 product and the timing of events of the budding site of Saccharomyces cerevisiae
    • Jeong, J. W., Kim, D. H., Choi, S. Y. and Kim, H. B.(2001). Characterization of the CDC10 product and the timing of events of the budding site of Saccharomyces cerevisiae. Mol. Cells 12, 77-83.
    • (2001) Mol. Cells , vol.12 , pp. 77-83
    • Jeong, J.W.1    Kim, D.H.2    Choi, S.Y.3    Kim, H.B.4
  • 39
    • 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
  • 40
    • 84862908732 scopus 로고    scopus 로고
    • SEPT9 occupies the terminal positions in septin octamers and mediates polymerization-dependent functions in abscission
    • (in press)
    • Kim, M. S., Froese, C. D., Estey, M. P. and Trimble, W.(2011a). SEPT9 occupies the terminal positions in septin octamers and mediates polymerization-dependent functions in abscission. J. Cell Biol. (in press).
    • (2011) J. Cell Biol.
    • Kim, M.S.1    Froese, C.D.2    Estey, M.P.3    Trimble, W.4
  • 42
    • 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., Ide, C., Kinoshita, A., Haraguchi, T., Hiraoka, Y. and Noda, M.(1997). Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures. Genes Dev. 11, 1535-1547.
    • (1997) Genes Dev , vol.11 , pp. 1535-1547
    • Kinoshita, M.1    Kumar, S.2    Mizoguchi, A.3    Ide, C.4    Kinoshita, A.5    Haraguchi, T.6    Hiraoka, Y.7    Noda, M.8
  • 45
    • 2342526538 scopus 로고    scopus 로고
    • FLJ10849, a septin family gene, fuses MLL in a novel leukemia cell line CNLBC1 derived from chronic neutrophilic leukemia in transformation with t(4;11)(q21;q23)
    • Kojima, K., Sakai, I., Hasegawa, A., Niiya, H., Azuma, T., Matsuo, Y., Fujii, N., Tanimoto, M. and Fujita, S.(2004). FLJ10849, a septin family gene, fuses MLL in a novel leukemia cell line CNLBC1 derived from chronic neutrophilic leukemia in transformation with t(4;11)(q21;q23). Leukemia 18, 998-1005.
    • (2004) Leukemia , vol.18 , pp. 998-1005
    • Kojima, K.1    Sakai, I.2    Hasegawa, A.3    Niiya, H.4    Azuma, T.5    Matsuo, Y.6    Fujii, N.7    Tanimoto, M.8    Fujita, S.9
  • 46
    • 34548289288 scopus 로고    scopus 로고
    • Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7
    • Kremer, B. E., Adang, L. A. and Macara, I. G.(2007). Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7. Cell 130, 837-850.
    • (2007) Cell , vol.130 , pp. 837-850
    • Kremer, B.E.1    Adang, L.A.2    Macara, I.G.3
  • 48
    • 0036645506 scopus 로고    scopus 로고
    • Microtubule capture by the cleavage apparatus is required for proper spindle positioning in yeast
    • Kusch, J., Meyer, A., Snyder, M. P. and Barral, Y.(2002). Microtubule capture by the cleavage apparatus is required for proper spindle positioning in yeast. Genes Dev. 16, 1627-1639.
    • (2002) Genes Dev , vol.16 , pp. 1627-1639
    • Kusch, J.1    Meyer, A.2    Snyder, M.P.3    Barral, Y.4
  • 50
    • 13944265973 scopus 로고    scopus 로고
    • The ARTS connection: role of ARTS in apoptosis and cancer
    • Larisch, S.(2004). The ARTS connection: role of ARTS in apoptosis and cancer. Cell Cycle 3, 1021-1023.
    • (2004) Cell Cycle , vol.3 , pp. 1021-1023
    • Larisch, S.1
  • 52
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe, D. D., Wolf, Y. I., Koonin, E. V. and Aravind, L.(2002). Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 317, 41-72.
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 57
    • 33750082712 scopus 로고    scopus 로고
    • Structural analysis of septin 2, 6, and 7 complexes
    • Low, C. and Macara, I. G.(2006). Structural analysis of septin 2, 6, and 7 complexes. J. Biol. Chem. 281, 30697-30706.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30697-30706
    • Low, C.1    Macara, I.G.2
  • 58
    • 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
  • 60
    • 0037195256 scopus 로고    scopus 로고
    • GTP binding induces filament assembly of a recombinant septin
    • Mendoza, M., Hyman, A. A. and Glotzer, M.(2002). GTP binding induces filament assembly of a recombinant septin. Curr. Biol. 12, 1858-1863.
    • (2002) Curr. Biol. , vol.12 , pp. 1858-1863
    • Mendoza, M.1    Hyman, A.A.2    Glotzer, M.3
  • 62
    • 49449093766 scopus 로고    scopus 로고
    • Role of nucleotide binding in septin-septin interactions and septin localization in Saccharomyces cerevisiae
    • Nagaraj, S., Rajendran, A., Jackson, C. E. and Longtine, M. S.(2008). Role of nucleotide binding in septin-septin interactions and septin localization in Saccharomyces cerevisiae. Mol. Cell. Biol. 28, 5120-5137.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 5120-5137
    • Nagaraj, S.1    Rajendran, A.2    Jackson, C.E.3    Longtine, M.S.4
  • 63
    • 12444250092 scopus 로고    scopus 로고
    • Cytoskeletal modification of Rho guanine nucleotide exchange factor activity: identification of a Rho guanine nucleotide exchange factor as a binding partner for Sept9b, a mammalian septin
    • Nagata, K.-I. and Inagaki, M.(2004). Cytoskeletal modification of Rho guanine nucleotide exchange factor activity: identification of a Rho guanine nucleotide exchange factor as a binding partner for Sept9b, a mammalian septin. Oncogene 24, 65-76.
    • (2004) Oncogene , vol.24 , pp. 65-76
    • Nagata, K.-I.1    Inagaki, M.2
  • 65
    • 0024206251 scopus 로고
    • Kinetic analysis of the hydrolysis of GTP by p21N-Ras: The basal GTPase mechanism
    • Neal, S. E., Eccleston, J. F., Hall, A. and Webb, M. R.(1988) Kinetic analysis of the hydrolysis of GTP by p21N-Ras: The basal GTPase mechanism. J. Biol. Chem. 263, 18718-18722.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18718-18722
    • Neal, S.E.1    Eccleston, J.F.2    Hall, A.3    Webb, M.R.4
  • 66
    • 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, 371-379.
    • (1994) Cell , vol.77 , pp. 371-379
    • Neufeld, T.P.1    Rubin, G.M.2
  • 67
    • 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
  • 68
    • 0031684860 scopus 로고    scopus 로고
    • Purification and assay of a septin complex from Drosophila embryos
    • Oegema, K., Desai, A., Wong, M. L., Mitchison, T. J. and Field, C. M.(1998). Purification and assay of a septin complex from Drosophila embryos. Methods Enzymol. 298, 279-295.
    • (1998) Methods Enzymol , vol.298 , pp. 279-295
    • Oegema, K.1    Desai, A.2    Wong, M.L.3    Mitchison, T.J.4    Field, C.M.5
  • 69
    • 0033065099 scopus 로고    scopus 로고
    • 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)
    • Osaka, M., Rowley, J. D. and Zeleznik-Le, N. J.(1999). 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. USA 96, 6428-6433.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6428-6433
    • Osaka, M.1    Rowley, J.D.2    Zeleznik-Le, N.J.3
  • 70
    • 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 Evol. Biol. 7, 103.
    • (2007) BMC Evol. Biol. , vol.7 , pp. 103
    • Pan, F.1    Malmberg, R.L.2    Momany, M.3
  • 71
    • 77953951585 scopus 로고    scopus 로고
    • Conquering the complex world of human septins: implications for health and disease
    • Peterson, E. A. and Petty, E. M.(2010). Conquering the complex world of human septins: implications for health and disease. Clin. Gen. 77, 511-524.
    • (2010) Clin. Gen. , vol.77 , pp. 511-524
    • Peterson, E.A.1    Petty, E.M.2
  • 74
    • 26944448622 scopus 로고    scopus 로고
    • Do septins have a role in cancer?
    • Russell, S. E. H. and Hall, P. A.(2005). Do septins have a role in cancer? Br. J. Cancer 93, 499-503.
    • (2005) Br. J. Cancer , vol.93 , pp. 499-503
    • Russell, S.E.H.1    Hall, P.A.2
  • 75
    • 77953128969 scopus 로고    scopus 로고
    • Cytokinesis and cancer
    • Sagona, A. P. and Stenmark, H.(2010). Cytokinesis and cancer. FEBS Lett. 584, 2652-2661.
    • (2010) FEBS Lett , vol.584 , pp. 2652-2661
    • Sagona, A.P.1    Stenmark, H.2
  • 77
    • 2642575982 scopus 로고    scopus 로고
    • A barrier to lateral diffusion in the cleavage furrow of dividing mammalian cells
    • Schmidt, K. and Nichols, B. J.(2004). A barrier to lateral diffusion in the cleavage furrow of dividing mammalian cells. Curr. Biol. 14, 1002-1006.
    • (2004) Curr. Biol. , vol.14 , pp. 1002-1006
    • Schmidt, K.1    Nichols, B.J.2
  • 78
    • 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
  • 79
    • 49649106438 scopus 로고    scopus 로고
    • A mechanism for asymmetric segregation of age during yeast budding
    • Shcheprova, Z., Baldi, S., Frei, S. B., Gonnet, G. and Barral, Y.(2008). A mechanism for asymmetric segregation of age during yeast budding. Nature 454, 728-734.
    • (2008) Nature , vol.454 , pp. 728-734
    • Shcheprova, Z.1    Baldi, S.2    Frei, S.B.3    Gonnet, G.4    Barral, Y.5
  • 80
    • 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
  • 81
    • 77950907753 scopus 로고    scopus 로고
    • Septin 14 is involved in cortical neuronal migration via interaction with Septin 4
    • Shinoda, T., Ito, H., Sudo, K., Iwamoto, I., Morishita, R. and Nagata, K.(2010). Septin 14 is involved in cortical neuronal migration via interaction with Septin 4. Mol. Biol. Cell 21, 1324-1334.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1324-1334
    • Shinoda, T.1    Ito, H.2    Sudo, K.3    Iwamoto, I.4    Morishita, R.5    Nagata, K.6
  • 83
    • 70349728578 scopus 로고    scopus 로고
    • GTP-induced conformational changes in septins and implications for function
    • Sirajuddin, M., Farkasovsky, M., Zent, E. and Wittinghofer, A.(2009). GTP-induced conformational changes in septins and implications for function. Proc. Natl. Acad. Sci. USA 106, 16592-16597.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 16592-16597
    • Sirajuddin, M.1    Farkasovsky, M.2    Zent, E.3    Wittinghofer, A.4
  • 85
    • 38749147682 scopus 로고    scopus 로고
    • Epithelial polarity requires septin coupling of vesicle transport to polyglutamylated microtubules
    • Spiliotis, E. T., Hunt, S. J., Hu, Q., Kinoshita, M. and Nelson, W. J.(2008). Epithelial polarity requires septin coupling of vesicle transport to polyglutamylated microtubules. J. Cell Biol. 180, 295-303.
    • (2008) J. Cell Biol. , vol.180 , pp. 295-303
    • Spiliotis, E.T.1    Hunt, S.J.2    Hu, Q.3    Kinoshita, M.4    Nelson, W.J.5
  • 87
    • 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.(2002). The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis. Mol. Biol. Cell 13, 3532-3545.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3532-3545
    • Surka, M.C.1    Tsang, C.W.2    Trimble, W.3
  • 88
    • 58149314553 scopus 로고    scopus 로고
    • The checkpoint kinase Hsl1p is activated by Elm1p-dependent phosphorylation
    • Szkotnicki, L., Crutchley, J. M., Zyla, T. R., Bardes, E. S. G. and Lew, D. J.(2008). The checkpoint kinase Hsl1p is activated by Elm1p-dependent phosphorylation. Mol. Biol. Cell 19, 4675-4686.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4675-4686
    • Szkotnicki, L.1    Crutchley, J.M.2    Zyla, T.R.3    Bardes, E.S.G.4    Lew, D.J.5
  • 89
    • 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
  • 90
    • 58349115398 scopus 로고    scopus 로고
    • Septin-mediated uniform bracing of phospholipid membranes
    • Tanaka-Takiguchi, Y., Kinoshita, M. and Takiguchi, K.(2009). Septin-mediated 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
  • 91
    • 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. J. Cell Biol. 160, 1093-1103.
    • (2003) J. Cell Biol. , vol.160 , pp. 1093-1103
    • Tasto, J.J.1    Morrell, J.L.2    Gould, K.L.3
  • 93
    • 0037455053 scopus 로고    scopus 로고
    • The septin protein Nedd5 associates with both the exocyst complex and microtubules and disruption of its GTPase activity promotes aberrant neurite sprouting in PC12 cells
    • Vega, I. E. and Hsu, S. C.(2003). The septin protein Nedd5 associates with both the exocyst complex and microtubules and disruption of its GTPase activity promotes aberrant neurite sprouting in PC12 cells. Neuroreport 14, 31-37.
    • (2003) Neuroreport , vol.14 , pp. 31-37
    • Vega, I.E.1    Hsu, S.C.2
  • 94
    • 1442334322 scopus 로고    scopus 로고
    • Septin collar formation in budding yeast requires GTP binding and direct phosphorylation by the PAK
    • 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) Cla4. J. Cell Biol. , vol.164 , pp. 701-715
    • Versele, M.1    Thorner, J.2
  • 95
    • 23744499989 scopus 로고    scopus 로고
    • Some assembly required: yeast septins provide the instruction manual
    • Versele, M. and Thorner, J.(2005). Some assembly required: yeast septins provide the instruction manual. Trends Cell Biol. 15, 414-424.
    • (2005) Trends Cell Biol , vol.15 , pp. 414-424
    • Versele, M.1    Thorner, J.2
  • 96
    • 4644251602 scopus 로고    scopus 로고
    • Protein-protein interactions governing septin heteropentamer assembly and septin filament organization in Saccharomyces cerevisiae
    • Versele, M., Gullbrand, B., Shulewitz, M. J., Cid, V. J., Bahmanyar, S., Chen, R. E., Barth, P., Alber, T. and Thorner, J.(2004). Protein-protein interactions governing septin heteropentamer assembly and septin filament organization in Saccharomyces cerevisiae. Mol. Biol. Cell 15, 4568-4583.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4568-4583
    • Versele, M.1    Gullbrand, B.2    Shulewitz, M.J.3    Cid, V.J.4    Bahmanyar, S.5    Chen, R.E.6    Barth, P.7    Alber, T.8    Thorner, J.9
  • 97
    • 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
  • 98
    • 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. and Mitchison, T. J.(2003). The majority of the Saccharomyces cerevisiae septin complexes do not exchange guanine nucleotides. J. Biol. Chem. 279, 3111-3118.
    • (2003) J. Biol. Chem. , vol.279 , pp. 3111-3118
    • Vrabioiu, A.M.1    Gerber, S.A.2    Gygi, S.P.3    Field, C.4    Mitchison, T.J.5
  • 99
    • 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
  • 100
    • 78951474636 scopus 로고    scopus 로고
    • Cooperation between the septins and the actomyosin ring and role of a cell-integrity pathway during cell division in fission yeast
    • Wu, J. Q., Ye, Y., Wang, N., Pollard, T. D. and Pringle, J. R.(2010). Cooperation between the septins and the actomyosin ring and role of a cell-integrity pathway during cell division in fission yeast. Genetics 186, 897-915.
    • (2010) Genetics , vol.186 , pp. 897-915
    • Wu, J.Q.1    Ye, Y.2    Wang, N.3    Pollard, T.D.4    Pringle, J.R.5
  • 101
    • 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
  • 102
    • 77954463587 scopus 로고    scopus 로고
    • Septins regulate developmental switching from microdomain to nanodomain coupling of Ca2+ influx to neurotransmitter release at a central synapse
    • Yang, Y. M., Fedchyshyn, M. J., Grande, G., Aitoubah, J., Tsang, C. W., Xie, H., Ackerley, C. A., Trimble, W. S. and Wang, L. Y.(2010). Septins regulate developmental switching from microdomain to nanodomain coupling of Ca2+ influx to neurotransmitter release at a central synapse. Neuron 67, 100-115.
    • (2010) Neuron , vol.67 , pp. 100-115
    • Yang, Y.M.1    Fedchyshyn, M.J.2    Grande, G.3    Aitoubah, J.4    Tsang, C.W.5    Xie, H.6    Ackerley, C.A.7    Trimble, W.S.8    Wang, L.Y.9
  • 104
    • 66349091880 scopus 로고    scopus 로고
    • Contribution of phosphatidylserine to membrane surface charge and protein targeting during phagosome maturation
    • Yeung, T., Heit, B., Dubuisson, J. F., Fairn, G. D., Chiu, B., Inman, R., Kapus, A., Swanson, M. and Grinstein, S.(2009). Contribution of phosphatidylserine to membrane surface charge and protein targeting during phagosome maturation. J. Cell Biol. 185, 917-928.
    • (2009) J. Cell Biol. , vol.185 , pp. 917-928
    • Yeung, T.1    Heit, B.2    Dubuisson, J.F.3    Fairn, G.D.4    Chiu, B.5    Inman, R.6    Kapus, A.7    Swanson, M.8    Grinstein, S.9
  • 105
    • 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
  • 106
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • Zhang, Y., Gao, J., Chung, K. K., Huang, H., Dawson, V. L. and Dawson, T. M.(2000). Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc. Natl. Acad. Sci. USA 97, 13354-13359.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.