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Volumn 13, Issue 2, 2012, Pages 195-203

Spatial Guidance of Cell Asymmetry: Septin GTPases Show the Way

Author keywords

Cell polarity; Diffusion barriers; F actin; Fungal and animal morphogenesis; GTPases; Membrane domains; Microtubules; Scaffolds; Septins

Indexed keywords

ADENOSINE TRIPHOSPHATE; FUNGAL PROTEIN; GUANOSINE TRIPHOSPHATASE; MESSENGER RNA; MYOSIN ADENOSINE TRIPHOSPHATASE; SEPTIN; SONIC HEDGEHOG PROTEIN;

EID: 84855950538     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2011.01268.x     Document Type: Review
Times cited : (66)

References (106)
  • 1
    • 34547121710 scopus 로고    scopus 로고
    • Analysis of septins across kingdoms reveals orthology and new motifs
    • Pan F, Malmberg RL, Momany M. Analysis of septins across kingdoms reveals orthology and new motifs. BMC Evol Biol 2007; 7: 103.
    • (2007) BMC Evol Biol , vol.7 , pp. 103
    • Pan, F.1    Malmberg, R.L.2    Momany, M.3
  • 2
    • 80052719413 scopus 로고    scopus 로고
    • New insights into the phylogenetic distribution and evolutinary origins of the septins
    • Nishihama R, Onishi M, Pringle JR. New insights into the phylogenetic distribution and evolutinary origins of the septins. Biol Chem 2011; 392: 681-687.
    • (2011) Biol Chem , vol.392 , pp. 681-687
    • Nishihama, R.1    Onishi, M.2    Pringle, J.R.3
  • 3
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe DD, Wolf YI, Koonin EV, Aravind L. Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol 2002; 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
  • 4
    • 58549085982 scopus 로고    scopus 로고
    • Reuse, replace, recycle. Specificity in subunit inheritance and assembly of higher-order septin structures during mitotic and meiotic division in budding yeast
    • McMurray MA, Thorner J. Reuse, replace, recycle. Specificity in subunit inheritance and assembly of higher-order septin structures during mitotic and meiotic division in budding yeast. Cell Cycle 2009; 8: 195-203.
    • (2009) Cell Cycle , vol.8 , pp. 195-203
    • McMurray, M.A.1    Thorner, J.2
  • 5
    • 82755198278 scopus 로고    scopus 로고
    • The genomics and regulation of the human septin genes
    • In: Hall PA, Russell SEH, Pringle JR, editors. Chichester: John Wiley & Sons; pp. -.
    • Russell SEH. The genomics and regulation of the human septin genes. In: Hall PA, Russell SEH, Pringle JR, editors. The Septins. Chichester: John Wiley & Sons; 2008. pp. 171-185.
    • (2008) The Septins , pp. 171-185
    • Russell, S.E.H.1
  • 7
  • 8
    • 70349728578 scopus 로고    scopus 로고
    • GTP-induced conformational changes in septins and implications for function
    • Sirajuddin M, Farkasovsky M, Zent E, Wittinghofer A. GTP-induced conformational changes in septins and implications for function. Proc Natl Acad Sci USA 2009; 106: 16592-16597.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 16592-16597
    • Sirajuddin, M.1    Farkasovsky, M.2    Zent, E.3    Wittinghofer, A.4
  • 11
    • 80052245849 scopus 로고    scopus 로고
    • Deciphering the rules governing assembly order of mammalian septin complexes
    • 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.
    • (2011) Mol Biol Cell , vol.22 , pp. 3152-3164
    • Sellin, M.E.1    Sandblad, L.2    Stenmark, S.3    Gullberg, M.4
  • 16
    • 57649194799 scopus 로고    scopus 로고
    • Forchlorfenuron alters mammalian septin assembly, organization, and dynamics
    • Hu Q, Nelson WJ, Spiliotis ET. Forchlorfenuron alters mammalian septin assembly, organization, and dynamics. J Biol Chem 2008; 283: 29563-29571.
    • (2008) J Biol Chem , vol.283 , pp. 29563-29571
    • Hu, Q.1    Nelson, W.J.2    Spiliotis, E.T.3
  • 18
    • 0141541745 scopus 로고    scopus 로고
    • The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast
    • Caviston JP, Longtine M, Pringle JR, Bi E. The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast. Mol Biol Cell 2003; 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
  • 19
    • 0037345639 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of septin dynamics during the cell cycle
    • Dobbelaere J, Gentry MS, Hallberg RL, Barral Y. Phosphorylation-dependent regulation of septin dynamics during the cell cycle. Dev Cell 2003; 4: 345-357.
    • (2003) Dev Cell , vol.4 , pp. 345-357
    • Dobbelaere, J.1    Gentry, M.S.2    Hallberg, R.L.3    Barral, Y.4
  • 20
    • 33749165924 scopus 로고    scopus 로고
    • Structural insights into yeast septin organization from polarized fluorescence microscopy
    • Vrabioiu AM, Mitchison TJ. Structural insights into yeast septin organization from polarized fluorescence microscopy. Nature 2006; 443: 466-469.
    • (2006) Nature , vol.443 , pp. 466-469
    • Vrabioiu, A.M.1    Mitchison, T.J.2
  • 23
    • 1442337555 scopus 로고    scopus 로고
    • The majority of the Saccharomyces cerevisiae septin complexes do not exchange guanine nucleotides
    • 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.
    • (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
  • 24
    • 0037474299 scopus 로고    scopus 로고
    • Borg/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments
    • Sheffield PJ, Oliver CJ, Kremer BE, Sheng S, Shao Z, Macara IG. Borg/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments. J Biol Chem 2003; 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
  • 25
    • 0037195256 scopus 로고    scopus 로고
    • GTP binding induces filament assembly of a recombinant septin
    • Mendoza M, Hyman AA, Glotzer M. GTP binding induces filament assembly of a recombinant septin. Curr Biol 2002; 12: 1858-1863.
    • (2002) Curr Biol , vol.12 , pp. 1858-1863
    • Mendoza, M.1    Hyman, A.A.2    Glotzer, M.3
  • 26
    • 26844470092 scopus 로고    scopus 로고
    • Nucleotide binding and filament assembly of recombinant yeast septin complexes
    • Farkasovsky M, Herter P, Voss B, Wittinghofer A. Nucleotide binding and filament assembly of recombinant yeast septin complexes. Biol Chem 2005; 386: 643-656.
    • (2005) Biol Chem , vol.386 , pp. 643-656
    • Farkasovsky, M.1    Herter, P.2    Voss, B.3    Wittinghofer, A.4
  • 27
    • 0015193588 scopus 로고
    • Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis
    • 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.
    • (1971) Exp Cell Res , vol.69 , pp. 265-276
    • Hartwell, L.H.1
  • 28
    • 0017153996 scopus 로고
    • A highly ordered ring of membrane-associated filaments in budding yeast
    • Byers B, Goetsch L. A highly ordered ring of membrane-associated filaments in budding yeast. J Cell Biol 1976; 69: 717-721.
    • (1976) J Cell Biol , vol.69 , pp. 717-721
    • Byers, B.1    Goetsch, L.2
  • 29
    • 14444286600 scopus 로고    scopus 로고
    • Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function
    • Frazier JA, Wong ML, Longtine MS, Pringle JR, Mann M, Mitchison TJ, Field C. Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function. J Cell Biol 1998; 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
  • 30
    • 0002224147 scopus 로고
    • Loss of the filamentous ring in cytokinesis-defective mutants of budding yeast
    • Byers B, Goetsch L. Loss of the filamentous ring in cytokinesis-defective mutants of budding yeast. J Cell Biol 1976; 70: 35a.
    • (1976) J Cell Biol , vol.70
    • Byers, B.1    Goetsch, L.2
  • 31
    • 77953570400 scopus 로고    scopus 로고
    • Origins and development of the septin field
    • In: Hall PA, Russell SEH, Pringle JR, editors. Chichester: John Wiley & Sons; -.
    • Pringle JR. Origins and development of the septin field. In: Hall PA, Russell SEH, Pringle JR, editors. The Septins. Chichester: John Wiley & Sons; 2008, pp. 7-34.
    • (2008) The Septins , pp. 7-34
    • Pringle, J.R.1
  • 32
    • 65249171464 scopus 로고    scopus 로고
    • Regulation of distinct septin rings in a single cell by Elm1p and Gin4p kinases
    • DeMay BS, Meseroll RA, Occhipinti P, Gladfelter AS. Regulation of distinct septin rings in a single cell by Elm1p and Gin4p kinases. Mol Biol Cell 2009; 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
  • 33
    • 0034944723 scopus 로고    scopus 로고
    • The germ tubes of Candida albicans hyphae and pseudohyphae show different patterns of septin ring localization
    • Sudbery PE. The germ tubes of Candida albicans hyphae and pseudohyphae show different patterns of septin ring localization. Mol Microbiol 2001; 41: 19-31.
    • (2001) Mol Microbiol , vol.41 , pp. 19-31
    • Sudbery, P.E.1
  • 34
    • 0036679377 scopus 로고    scopus 로고
    • Septin function in Candida albicans morphogenesis
    • Warenda AJ, Konopka JB. Septin function in Candida albicans morphogenesis. Mol Biol Cell 2002; 13: 2732-2746.
    • (2002) Mol Biol Cell , vol.13 , pp. 2732-2746
    • Warenda, A.J.1    Konopka, J.B.2
  • 35
    • 75149119287 scopus 로고    scopus 로고
    • Septins enforce morphogenetic events during sexual reproduction and contribute to virulence of Cryptococcus neoformans
    • Kozubowski L, Heitman J. Septins enforce morphogenetic events during sexual reproduction and contribute to virulence of Cryptococcus neoformans. Mol Microbiol 2010; 75: 658-675.
    • (2010) Mol Microbiol , vol.75 , pp. 658-675
    • Kozubowski, L.1    Heitman, J.2
  • 36
    • 77958586645 scopus 로고    scopus 로고
    • Septins from the phytopathogenic fungus Ustilago maydis are required for proper morphogenesis but dispensable for virulence
    • Alvarez-Tabares I, Perez-Martin J. Septins from the phytopathogenic fungus Ustilago maydis are required for proper morphogenesis but dispensable for virulence. PLoS One 2010; 5: e12933.
    • (2010) PLoS One , vol.5
    • Alvarez-Tabares, I.1    Perez-Martin, J.2
  • 37
    • 0036156036 scopus 로고    scopus 로고
    • Aspergillus nidulans septin AspB plays pre- and postmitotic roles in septum, branch, and conidiophore development
    • Westfall PJ, Momany M. Aspergillus nidulans septin AspB plays pre- and postmitotic roles in septum, branch, and conidiophore development. Mol Biol Cell 2002; 13: 110-118.
    • (2002) Mol Biol Cell , vol.13 , pp. 110-118
    • Westfall, P.J.1    Momany, M.2
  • 38
    • 79952352917 scopus 로고    scopus 로고
    • Exo-endocytic trafficking and the septin-based diffusion barrier are required for the maintenance of Cdc42p polarization during budding yeast asymmetric growth
    • Orlando K, Sun X, Zhang J, Lu T, Yokomizo L, Wang P, Guo W. Exo-endocytic trafficking and the septin-based diffusion barrier are required for the maintenance of Cdc42p polarization during budding yeast asymmetric growth. Mol Biol Cell 2011; 22: 624-633.
    • (2011) Mol Biol Cell , vol.22 , pp. 624-633
    • Orlando, K.1    Sun, X.2    Zhang, J.3    Lu, T.4    Yokomizo, L.5    Wang, P.6    Guo, W.7
  • 39
    • 0037148528 scopus 로고    scopus 로고
    • Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p
    • Gladfelter AS, Bose I, Zyla TR, Bardes ES, Lew DJ. Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p. J Cell Biol 2002; 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
  • 41
    • 71049147069 scopus 로고    scopus 로고
    • Septins: molecular partitioning and the generation of cellular asymmetry
    • McMurray MA, Thorner J. Septins: molecular partitioning and the generation of cellular asymmetry. Cell Div 2009; 4: 18.
    • (2009) Cell Div , vol.4 , pp. 18
    • McMurray, M.A.1    Thorner, J.2
  • 42
    • 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 JR, Tatchell K. Role of the septin ring in the asymmetric localization of proteins at the mother-bud neck in Saccharomyces cerevisiae. Mol Biol Cell 2005; 16: 3455-3466.
    • (2005) Mol Biol Cell , vol.16 , pp. 3455-3466
    • Kozubowski, L.1    Larson, J.R.2    Tatchell, K.3
  • 43
    • 64549158361 scopus 로고    scopus 로고
    • Septins and the lateral compartmentalization of eukaryotic membranes
    • Caudron F, Barral Y. Septins and the lateral compartmentalization of eukaryotic membranes. Dev Cell 2009; 16: 493-506.
    • (2009) Dev Cell , vol.16 , pp. 493-506
    • Caudron, F.1    Barral, Y.2
  • 44
    • 0026019902 scopus 로고
    • Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: localization of the CDC3 gene product and the timing of events at the budding site
    • Kim HB, Haarer BK, Pringle JR. Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: localization of the CDC3 gene product and the timing of events at the budding site. J Cell Biol 1991; 112: 535-544.
    • (1991) J Cell Biol , vol.112 , pp. 535-544
    • Kim, H.B.1    Haarer, B.K.2    Pringle, J.R.3
  • 45
    • 33749477214 scopus 로고    scopus 로고
    • AgSwe1p regulates mitosis in response to morphogenesis and nutrients in multinucleated Ashbya gossypii cells
    • Helfer H, Gladfelter AS. AgSwe1p regulates mitosis in response to morphogenesis and nutrients in multinucleated Ashbya gossypii cells. Mol Biol Cell 2006; 17: 4494-4512.
    • (2006) Mol Biol Cell , vol.17 , pp. 4494-4512
    • Helfer, H.1    Gladfelter, A.S.2
  • 46
    • 75649098993 scopus 로고    scopus 로고
    • Septins AspA and AspC are important for normal development and limit the emergence of new growth foci in the multicellular fungus Aspergillus nidulans
    • Lindsey R, Cowden S, Hernandez-Rodriguez Y, Momany M. Septins AspA and AspC are important for normal development and limit the emergence of new growth foci in the multicellular fungus Aspergillus nidulans. Eukaryot Cell 2010; 9: 155-163.
    • (2010) Eukaryot Cell , vol.9 , pp. 155-163
    • Lindsey, R.1    Cowden, S.2    Hernandez-Rodriguez, Y.3    Momany, M.4
  • 48
    • 0042663892 scopus 로고    scopus 로고
    • A role for septins in cellular and axonal migration in C. elegans
    • Finger FP, Kopish KR, White JG. A role for septins in cellular and axonal migration in C. elegans. Dev Biol 2003; 261: 220-234.
    • (2003) Dev Biol , vol.261 , pp. 220-234
    • Finger, F.P.1    Kopish, K.R.2    White, J.G.3
  • 49
    • 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, Nagata K. Septin 14 is involved in cortical neuronal migration via interaction with Septin 4. Mol Biol Cell 2010; 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
  • 51
    • 21344441151 scopus 로고    scopus 로고
    • SEPT9-v4 expression induces morphological change, increased motility and disturbed polarity
    • 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.
    • (2005) J Pathol , vol.206 , pp. 458-465
    • Chacko, A.D.1    Hyland, P.L.2    McDade, S.S.3    Hamilton, P.W.4    Russell, S.H.5    Hall, P.A.6
  • 52
    • 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, Sheng M. Role of Septin cytoskeleton in spine morphogenesis and dendrite development in neurons. Curr Biol 2007; 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
  • 53
    • 35348907374 scopus 로고    scopus 로고
    • The GTP-binding protein Septin 7 is critical for dendrite branching and dendritic-spine morphology
    • 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.
    • (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
  • 54
    • 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 IE, Hsu SC. 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 2003; 14: 31-37.
    • (2003) Neuroreport , vol.14 , pp. 31-37
    • Vega, I.E.1    Hsu, S.C.2
  • 55
    • 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 MP, Nachury MV, Spiliotis ET, Nelson WJ. A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution. Science 2010; 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
  • 56
    • 38749147682 scopus 로고    scopus 로고
    • Epithelial polarity requires septin coupling of vesicle transport to polyglutamylated microtubules
    • 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.
    • (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
  • 59
    • 33947398366 scopus 로고    scopus 로고
    • Central roles of small GTPases in the development of cell polarity in yeast and beyond
    • Park HO, Bi E. Central roles of small GTPases in the development of cell polarity in yeast and beyond. Microbiol Mol Biol Rev 2007; 71: 48-96.
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 48-96
    • Park, H.O.1    Bi, E.2
  • 60
    • 0035575575 scopus 로고    scopus 로고
    • Shrinking patches and slippery rafts: scales of domains in the plasma membrane
    • Edidin M. Shrinking patches and slippery rafts: scales of domains in the plasma membrane. Trends Cell Biol 2001; 11: 492-496.
    • (2001) Trends Cell Biol , vol.11 , pp. 492-496
    • Edidin, M.1
  • 61
    • 7444232710 scopus 로고    scopus 로고
    • Role of the membrane skeleton in creation of microdomains
    • Ritchie K, Kusumi A. Role of the membrane skeleton in creation of microdomains. Subcell Biochem 2004; 37: 233-245.
    • (2004) Subcell Biochem , vol.37 , pp. 233-245
    • Ritchie, K.1    Kusumi, A.2
  • 63
    • 0037383708 scopus 로고    scopus 로고
    • Molecular dissection of a yeast septin: distinct domains are required for septin interaction, localization, and function
    • 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.
    • (2003) Mol Cell Biol , vol.23 , pp. 2762-2777
    • Casamayor, A.1    Snyder, M.2
  • 64
    • 0033576647 scopus 로고    scopus 로고
    • Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP
    • 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.
    • (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
  • 69
    • 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 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.
    • (2000) Mol Cell , vol.5 , pp. 841-851
    • Barral, Y.1    Mermall, V.2    Mooseker, M.S.3    Snyder, M.4
  • 70
    • 0034644626 scopus 로고    scopus 로고
    • Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier
    • 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.
    • (2000) Science , vol.290 , pp. 341-344
    • Takizawa, P.A.1    DeRisi, J.L.2    Wilhelm, J.E.3    Vale, R.D.4
  • 71
    • 22344453326 scopus 로고    scopus 로고
    • Septin-dependent compartmentalization of the endoplasmic reticulum during yeast polarized growth
    • Luedeke C, Frei SB, Sbalzarini I, Schwarz H, Spang A, Barral Y. Septin-dependent compartmentalization of the endoplasmic reticulum during yeast polarized growth. J Cell Biol 2005; 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
  • 73
    • 3142729153 scopus 로고    scopus 로고
    • Spatial coordination of cytokinetic events by compartmentalization of the cell cortex
    • Dobbelaere J, Barral Y. Spatial coordination of cytokinetic events by compartmentalization of the cell cortex. Science 2004; 305: 393-396.
    • (2004) Science , vol.305 , pp. 393-396
    • Dobbelaere, J.1    Barral, Y.2
  • 74
    • 2642575982 scopus 로고    scopus 로고
    • A barrier to lateral diffusion in the cleavage furrow of dividing mammalian cells
    • Schmidt K, Nichols BJ. A barrier to lateral diffusion in the cleavage furrow of dividing mammalian cells. Curr Biol 2004; 14: 1002-1006.
    • (2004) Curr Biol , vol.14 , pp. 1002-1006
    • Schmidt, K.1    Nichols, B.J.2
  • 75
    • 77953814967 scopus 로고    scopus 로고
    • The annulus of the mouse sperm tail is required to establish a membrane diffusion barrier that is engaged during the late steps of spermiogenesis
    • Kwitny S, Klaus AV, Hunnicutt GR. The annulus of the mouse sperm tail is required to establish a membrane diffusion barrier that is engaged during the late steps of spermiogenesis. Biol Reprod 2010; 82: 669-678.
    • (2010) Biol Reprod , vol.82 , pp. 669-678
    • Kwitny, S.1    Klaus, A.V.2    Hunnicutt, G.R.3
  • 76
    • 58349115398 scopus 로고    scopus 로고
    • Septin-mediated uniform bracing of phospholipid membranes
    • Tanaka-Takiguchi Y, Kinoshita M, Takiguchi K. Septin-mediated uniform bracing of phospholipid membranes. Curr Biol 2009; 19: 140-145.
    • (2009) Curr Biol , vol.19 , pp. 140-145
    • Tanaka-Takiguchi, Y.1    Kinoshita, M.2    Takiguchi, K.3
  • 78
    • 77950595366 scopus 로고    scopus 로고
    • Structural characteristics of BAR domain superfamily to sculpt the membrane
    • Masuda M, Mochizuki N. Structural characteristics of BAR domain superfamily to sculpt the membrane. Semin Cell Dev Biol 2010; 21: 391-398.
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 391-398
    • Masuda, M.1    Mochizuki, N.2
  • 79
    • 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-Cerda J, Cossart P, Lafont F. A role for septins in the interaction between the Listeria monocytogenes invasion protein InlB and the Met receptor. Biophys J 2011; 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-Cerda, J.6    Cossart, P.7    Lafont, F.8
  • 80
    • 54549102288 scopus 로고    scopus 로고
    • Beyond polymer polarity: how the cytoskeleton builds a polarized cell
    • Li R, Gundersen GG. Beyond polymer polarity: how the cytoskeleton builds a polarized cell. Nat Rev Mol Cell Biol 2008; 9: 860-873.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 860-873
    • Li, R.1    Gundersen, G.G.2
  • 81
    • 77957267234 scopus 로고    scopus 로고
    • Cytoskeletal mechanisms for breaking cellular symmetry
    • Mullins RD. Cytoskeletal mechanisms for breaking cellular symmetry. Cold Spring Harb Perspect Biol 2010; 2: a003392.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Mullins, R.D.1
  • 82
    • 0035344650 scopus 로고    scopus 로고
    • Cell control by membrane-cytoskeleton adhesion
    • Sheetz MP. Cell control by membrane-cytoskeleton adhesion. Nat Rev Mol Cell Biol 2001; 2: 392-396.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 392-396
    • Sheetz, M.P.1
  • 83
    • 33749258375 scopus 로고    scopus 로고
    • The yeast actin cytoskeleton: from cellular function to biochemical mechanism
    • Moseley JB, Goode BL. The yeast actin cytoskeleton: from cellular function to biochemical mechanism. Microbiol Mol Biol Rev 2006; 70: 605-645.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 605-645
    • Moseley, J.B.1    Goode, B.L.2
  • 84
    • 0025294640 scopus 로고
    • CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae
    • Adams AE, Johnson DI, Longnecker RM, Sloat BF, Pringle JR. CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae. J Cell Biol 1990; 111: 131-142.
    • (1990) J Cell Biol , vol.111 , pp. 131-142
    • Adams, A.E.1    Johnson, D.I.2    Longnecker, R.M.3    Sloat, B.F.4    Pringle, J.R.5
  • 85
    • 0036514271 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • Evangelista M, Pruyne D, Amberg DC, Boone C, Bretscher A. Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat Cell Biol 2002; 4: 260-269.
    • (2002) Nat Cell Biol , vol.4 , pp. 260-269
    • Evangelista, M.1    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 86
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • Sagot I, Klee SK, Pellman D. Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat Cell Biol 2002; 4: 42-50.
    • (2002) Nat Cell Biol , vol.4 , pp. 42-50
    • Sagot, I.1    Klee, S.K.2    Pellman, D.3
  • 87
    • 6344275302 scopus 로고    scopus 로고
    • Stable and dynamic axes of polarity use distinct formin isoforms in budding yeast
    • Pruyne D, Gao L, Bi E, Bretscher A. Stable and dynamic axes of polarity use distinct formin isoforms in budding yeast. Mol Biol Cell 2004; 15: 4971-4989.
    • (2004) Mol Biol Cell , vol.15 , pp. 4971-4989
    • Pruyne, D.1    Gao, L.2    Bi, E.3    Bretscher, A.4
  • 89
    • 33845689351 scopus 로고    scopus 로고
    • Roles of type II myosin and a tropomyosin isoform in retrograde actin flow in budding yeast
    • Huckaba TM, Lipkin T, Pon LA. Roles of type II myosin and a tropomyosin isoform in retrograde actin flow in budding yeast. J Cell Biol 2006; 175: 957-969.
    • (2006) J Cell Biol , vol.175 , pp. 957-969
    • Huckaba, T.M.1    Lipkin, T.2    Pon, L.A.3
  • 91
    • 35548961325 scopus 로고    scopus 로고
    • Mammalian SEPT2 is required for scaffolding nonmuscle myosin II and its kinases
    • Joo E, Surka MC, Trimble WS. Mammalian SEPT2 is required for scaffolding nonmuscle myosin II and its kinases. Dev Cell 2007; 13: 677-690.
    • (2007) Dev Cell , vol.13 , pp. 677-690
    • Joo, E.1    Surka, M.C.2    Trimble, W.S.3
  • 92
    • 34247618242 scopus 로고    scopus 로고
    • Anillin and the septins promote asymmetric ingression of the cytokinetic furrow
    • Maddox AS, Lewellyn L, Desai A, Oegema K. Anillin and the septins promote asymmetric ingression of the cytokinetic furrow. Dev Cell 2007; 12: 827-835.
    • (2007) Dev Cell , vol.12 , pp. 827-835
    • Maddox, A.S.1    Lewellyn, L.2    Desai, A.3    Oegema, K.4
  • 93
    • 0028101021 scopus 로고
    • Orientation of spindle axis and distribution of plasma membrane proteins during cell division in polarized MDCKII cells
    • Reinsch S, Karsenti E. Orientation of spindle axis and distribution of plasma membrane proteins during cell division in polarized MDCKII cells. J Cell Biol 1994; 126: 1509-1526.
    • (1994) J Cell Biol , vol.126 , pp. 1509-1526
    • Reinsch, S.1    Karsenti, E.2
  • 94
    • 34548289288 scopus 로고    scopus 로고
    • Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7
    • Kremer BE, Adang LA, Macara IG. Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7. Cell 2007; 130: 837-850.
    • (2007) Cell , vol.130 , pp. 837-850
    • Kremer, B.E.1    Adang, L.A.2    Macara, I.G.3
  • 96
    • 67649710254 scopus 로고    scopus 로고
    • Septin functions in the mammalian cytoskeleton
    • In: Hall PA, Russell SEH Pringle JR, editors. Chichester: John Wiley & Sons; -.
    • Spiliotis ET, Nelson WJ. Septin functions in the mammalian cytoskeleton. In: Hall PA, Russell SEH Pringle JR, editors. The Septins. Chichester: John Wiley & Sons; 2008, pp. 229-246.
    • (2008) The Septins , pp. 229-246
    • Spiliotis, E.T.1    Nelson, W.J.2
  • 98
    • 77957868249 scopus 로고    scopus 로고
    • Post-translational modifications of microtubules
    • Wloga D, Gaertig J. Post-translational modifications of microtubules. J Cell Sci 2010; 123: 3447-3455.
    • (2010) J Cell Sci , vol.123 , pp. 3447-3455
    • Wloga, D.1    Gaertig, J.2
  • 99
    • 77953590866 scopus 로고    scopus 로고
    • Regulation of microtubule organization and functions by septin GTPases
    • Spiliotis ET. Regulation of microtubule organization and functions by septin GTPases. Cytoskeleton (Hoboken) 2010; 67: 339-345.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 339-345
    • Spiliotis, E.T.1
  • 101
    • 15244346231 scopus 로고    scopus 로고
    • A mitotic septin scaffold required for Mammalian chromosome congression and segregation
    • Spiliotis ET, Kinoshita M, Nelson WJ. A mitotic septin scaffold required for Mammalian chromosome congression and segregation. Science 2005; 307: 1781-1785.
    • (2005) Science , vol.307 , pp. 1781-1785
    • Spiliotis, E.T.1    Kinoshita, M.2    Nelson, W.J.3
  • 102
    • 79961115058 scopus 로고    scopus 로고
    • Septin GTPases spatially guide microtubule organization and plus end dynamics in polarizing epithelia
    • 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.
    • (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
  • 103
    • 70350446761 scopus 로고    scopus 로고
    • Traffic control: regulation of kinesin motors
    • Verhey KJ, Hammond JW. Traffic control: regulation of kinesin motors. Nat Rev Mol Cell Biol 2009; 10: 765-777.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 765-777
    • Verhey, K.J.1    Hammond, J.W.2
  • 105
    • 26244468767 scopus 로고    scopus 로고
    • Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4
    • 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.
    • (2005) Mol Biol Cell , vol.16 , pp. 4648-4659
    • Kremer, B.E.1    Haystead, T.2    Macara, I.G.3
  • 106
    • 0036645506 scopus 로고    scopus 로고
    • Microtubule capture by the cleavage apparatus is required for proper spindle positioning in yeast
    • 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.
    • (2002) Genes Dev , vol.16 , pp. 1627-1639
    • Kusch, J.1    Meyer, A.2    Snyder, M.P.3    Barral, Y.4


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