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Volumn 111, Issue 6, 2014, Pages 2146-2151

Septin assemblies form by diffusion-driven annealing on membranes

Author keywords

Biophysics; Cytoskeleton

Indexed keywords

BIOPHYSICS; CYTOSKELETON;

EID: 84893853665     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1314138111     Document Type: Article
Times cited : (139)

References (38)
  • 1
    • 3142729153 scopus 로고    scopus 로고
    • Spatial coordination of cytokinetic events by compartmentalization of the cell cortex
    • Dobbelaere J, Barral Y (2004) Spatial coordination of cytokinetic events by compartmentalization of the cell cortex. Science 305(5682):393-396.
    • (2004) Science , vol.305 , Issue.5682 , pp. 393-396
    • Dobbelaere, J.1    Barral, Y.2
  • 2
    • 84863011435 scopus 로고    scopus 로고
    • The septin cytoskeleton facilitates membrane retraction during motility and blebbing
    • Gilden JK, Peck S, Chen YC, Krummel MF (2012) The septin cytoskeleton facilitates membrane retraction during motility and blebbing. J Cell Biol 196(1):103-114.
    • (2012) J Cell Biol , vol.196 , Issue.1 , pp. 103-114
    • Gilden, J.K.1    Peck, S.2    Chen, Y.C.3    Krummel, M.F.4
  • 3
    • 0017153996 scopus 로고
    • A highly ordered ring of membrane-associated filaments in budding yeast
    • Byers B, Goetsch L (1976) A highly ordered ring of membrane-associated filaments in budding yeast. J Cell Biol 69(3):717-721.
    • (1976) J Cell Biol , vol.69 , Issue.3 , pp. 717-721
    • Byers, B.1    Goetsch, L.2
  • 4
    • 79952104930 scopus 로고    scopus 로고
    • Septin structure and function in yeast and beyond
    • Oh Y, Bi E (2011) Septin structure and function in yeast and beyond. Trends Cell Biol 21(3):141-148.
    • (2011) Trends Cell Biol , vol.21 , Issue.3 , pp. 141-148
    • Oh, Y.1    Bi, E.2
  • 5
    • 0015105591 scopus 로고
    • Genetic control of the cell division cycle in yeast. Seven genes controlling nuclear division
    • Culotti J, Hartwell LH (1971) Genetic control of the cell division cycle in yeast. Seven genes controlling nuclear division. Exp Cell Res 67(2):389-401
    • (1971) Exp Cell Res , vol.67 , Issue.2 , pp. 389-401
    • Culotti, J.1    Hartwell, L.H.2
  • 6
    • 0031770672 scopus 로고    scopus 로고
    • Identification of septins in neurofibrillary tangles in Alzheimer's disease
    • Kinoshita A, et al. (1998) Identification of septins in neurofibrillary tangles in Alzheimer's disease. Am J Pathol 153(5):1551-1560.
    • (1998) Am J Pathol , vol.153 , Issue.5 , pp. 1551-1560
    • Kinoshita, A.1
  • 7
    • 7944228563 scopus 로고    scopus 로고
    • The pathobiology of the septin gene family
    • Hall PA, Russell SE (2004) The pathobiology of the septin gene family. J Pathol 204(4): 489-505.
    • (2004) J Pathol , vol.204 , Issue.4 , pp. 489-505
    • Hall, P.A.1    Russell, S.E.2
  • 8
    • 80052708779 scopus 로고    scopus 로고
    • Septin genomics: A road less travelled
    • Russell SE, Hall PA (2011) Septin genomics: A road less travelled. Biol Chem 392(8-9): 763-767.
    • (2011) Biol Chem , vol.392 , Issue.8-9 , pp. 763-767
    • Russell, S.E.1    Hall, P.A.2
  • 9
    • 84862635661 scopus 로고    scopus 로고
    • Septin-mediated plant cell invasion by the rice blast fungus, Magnaporthe oryzae
    • Dagdas YF, et al. (2012) Septin-mediated plant cell invasion by the rice blast fungus, Magnaporthe oryzae. Science 336(6088):1590-1595.
    • (2012) Science , vol.336 , Issue.6088 , pp. 1590-1595
    • Dagdas, Y.F.1
  • 10
    • 78349239252 scopus 로고    scopus 로고
    • Entrapment of intracytosolic bacteria by septin cage-like structures
    • Mostowy S, et al. (2010) Entrapment of intracytosolic bacteria by septin cage-like structures. Cell Host Microbe 8(5):433-444.
    • (2010) Cell Host Microbe , vol.8 , Issue.5 , pp. 433-444
    • Mostowy, S.1
  • 11
    • 84874267104 scopus 로고    scopus 로고
    • NADPH oxidases regulate septin-mediated cytoskeletal remodeling during plant infection by the rice blast fungus
    • Ryder LS, et al. (2013) NADPH oxidases regulate septin-mediated cytoskeletal remodeling during plant infection by the rice blast fungus. Proc Natl Acad Sci USA 110(8):3179-3184.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.8 , pp. 3179-3184
    • Ryder, L.S.1
  • 12
    • 58149330180 scopus 로고    scopus 로고
    • Amoeboid T lymphocytes require the septin cytoskeleton for cortical integrity and persistent motility
    • Tooley AJ, et al. (2009) Amoeboid T lymphocytes require the septin cytoskeleton for cortical integrity and persistent motility. Nat Cell Biol 11(1):17-26.
    • (2009) Nat Cell Biol , vol.11 , Issue.1 , pp. 17-26
    • Tooley, A.J.1
  • 13
    • 79959435173 scopus 로고    scopus 로고
    • Septin filaments exhibit a dynamic, paired organization that is conserved from yeast to mammals
    • DeMay BS, et al. (2011) Septin filaments exhibit a dynamic, paired organization that is conserved from yeast to mammals. J Cell Biol 193(6):1065-1081.
    • (2011) J Cell Biol , vol.193 , Issue.6 , pp. 1065-1081
    • Demay, B.S.1
  • 14
    • 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 (2002) Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p. J Cell Biol 156(2):315-326.
    • (2002) J Cell Biol , vol.156 , Issue.2 , pp. 315-326
    • Gladfelter, A.S.1    Bose, I.2    Zyla, T.R.3    Bardes, E.S.4    Lew, D.J.5
  • 15
    • 84856812823 scopus 로고    scopus 로고
    • Septins at a glance
    • Beise N, Trimble W (2011) Septins at a glance. J Cell Sci 124(Pt 24):4141-4146.
    • (2011) J Cell Sci , vol.124 , Issue.PART 24 , pp. 4141-4146
    • Beise, N.1    Trimble, W.2
  • 16
    • 84855950538 scopus 로고    scopus 로고
    • Spatial guidance of cell asymmetry: Septin GTPases show the way
    • Spiliotis ET, Gladfelter AS (2012) Spatial guidance of cell asymmetry: Septin GTPases show the way. Traffic 13(2):195-203.
    • (2012) Traffic , vol.13 , Issue.2 , pp. 195-203
    • Spiliotis, E.T.1    Gladfelter, A.S.2
  • 17
    • 46149107653 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae septins: Supramolecular organization of heterooligomers and the mechanism of filament assembly
    • Bertin A, et al. (2008) Saccharomyces cerevisiae septins: Supramolecular organization of heterooligomers and the mechanism of filament assembly. Proc Natl Acad Sci USA 105(24):8274-8279.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.24 , pp. 8274-8279
    • Bertin, A.1
  • 18
    • 14444286600 scopus 로고    scopus 로고
    • Polymerization of purified yeast septins: Evidence that organized filament arrays may not be required for septin function
    • Frazier JA, et al. (1998) Polymerization of purified yeast septins: Evidence that organized filament arrays may not be required for septin function. J Cell Biol 143(3):737-749.
    • (1998) J Cell Biol , vol.143 , Issue.3 , pp. 737-749
    • Frazier, J.A.1
  • 19
    • 39149138430 scopus 로고    scopus 로고
    • Structural insights shed light onto septin assemblies and function
    • Barral Y, Kinoshita M (2008) Structural insights shed light onto septin assemblies and function. Curr Opin Cell Biol 20(1):12-18.
    • (2008) Curr Opin Cell Biol , vol.20 , Issue.1 , pp. 12-18
    • Barral, Y.1    Kinoshita, M.2
  • 20
    • 34547211102 scopus 로고    scopus 로고
    • The Caenorhabditis elegans septin complex is nonpolar
    • John CM, et al. (2007) The Caenorhabditis elegans septin complex is nonpolar. EMBO J 26(14):3296-3307.
    • (2007) EMBO J , vol.26 , Issue.14 , pp. 3296-3307
    • John, C.M.1
  • 21
    • 34548818799 scopus 로고    scopus 로고
    • Structural insight into filament formation by mammalian septins
    • Sirajuddin M, et al. (2007) Structural insight into filament formation by mammalian septins. Nature 449(7160):311-315.
    • (2007) Nature , vol.449 , Issue.7160 , pp. 311-315
    • Sirajuddin, M.1
  • 22
    • 78649333504 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5-bisphosphate promotes budding yeast septin filament assembly and organization
    • Bertin A, et al. (2010) Phosphatidylinositol-4,5-bisphosphate promotes budding yeast septin filament assembly and organization. J Mol Biol 404(4):711-731.
    • (2010) J Mol Biol , vol.404 , Issue.4 , pp. 711-731
    • Bertin, A.1
  • 23
    • 0033576647 scopus 로고    scopus 로고
    • Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP
    • Zhang J, et al. (1999) Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP. Curr Biol 9(24):1458-1467.
    • (1999) Curr Biol , vol.9 , Issue.24 , pp. 1458-1467
    • Zhang, J.1
  • 24
    • 0037383708 scopus 로고    scopus 로고
    • Molecular dissection of a yeast septin: Distinct domains are required for septin interaction, localization, and function
    • Casamayor A, SnyderM(2003) Molecular dissection of a yeast septin: Distinct domains are required for septin interaction, localization, and function. Mol Cell Biol 23(8): 2762-2777.
    • (2003) Mol Cell Biol , vol.23 , Issue.8 , pp. 2762-2777
    • Casamayor, A.1    Snyder, M.2
  • 25
    • 0023789421 scopus 로고
    • Direct demonstration of actin filament annealing in vitro
    • Murphy DB, Gray RO, Grasser WA, Pollard TD (1988) Direct demonstration of actin filament annealing in vitro. J Cell Biol 106(6):1947-1954.
    • (1988) J Cell Biol , vol.106 , Issue.6 , pp. 1947-1954
    • Murphy, D.B.1    Gray, R.O.2    Grasser, W.A.3    Pollard, T.D.4
  • 26
    • 26844562643 scopus 로고    scopus 로고
    • Counting cytokinesis proteins globally and locally in fission yeast
    • Wu JQ, Pollard TD (2005) Counting cytokinesis proteins globally and locally in fission yeast. Science 310(5746):310-314.
    • (2005) Science , vol.310 , Issue.5746 , pp. 310-314
    • Wu, J.Q.1    Pollard, T.D.2
  • 27
    • 70349906784 scopus 로고    scopus 로고
    • A CAAX motif can compensate for the PH domain of Num1 for cortical dynein attachment
    • Tang X, Punch JJ, Lee WL (2009) A CAAX motif can compensate for the PH domain of Num1 for cortical dynein attachment. Cell Cycle 8(19):3182-3190.
    • (2009) Cell Cycle , vol.8 , Issue.19 , pp. 3182-3190
    • Tang, X.1    Punch, J.J.2    Lee, W.L.3
  • 28
    • 0027533269 scopus 로고
    • Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape
    • Gittes F, Mickey B, Nettleton J, Howard J (1993) Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape. J Cell Biol 120(4): 923-934.
    • (1993) J Cell Biol , vol.120 , Issue.4 , pp. 923-934
    • Gittes, F.1    Mickey, B.2    Nettleton, J.3    Howard, J.4
  • 29
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison T, Kirschner M (1984) Dynamic instability of microtubule growth. Nature 312(5991):237-242.
    • (1984) Nature , vol.312 , Issue.5991 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 30
    • 0342519467 scopus 로고
    • Cytochalasin B: Microfilaments and "contractile" processes
    • Estensen RD, et al. (1971) Cytochalasin B: Microfilaments and "contractile" processes. Science 173(3994):356-359.
    • (1971) Science , vol.173 , Issue.3994 , pp. 356-359
    • Estensen, R.D.1
  • 31
    • 0029982293 scopus 로고    scopus 로고
    • A purified Drosophila septin complex forms filaments and exhibits GTPase activity
    • Field CM, et al. (1996) A purified Drosophila septin complex forms filaments and exhibits GTPase activity. J Cell Biol 133(3):605-616.
    • (1996) J Cell Biol , vol.133 , Issue.3 , pp. 605-616
    • Field, C.M.1
  • 32
    • 84865739164 scopus 로고    scopus 로고
    • Septin ring size scaling and dynamics require the coiled-coil region of Shs1p
    • Meseroll RA, Howard L, Gladfelter AS (2012) Septin ring size scaling and dynamics require the coiled-coil region of Shs1p. Mol Biol Cell 23(17):3391-3406.
    • (2012) Mol Biol Cell , vol.23 , Issue.17 , pp. 3391-3406
    • Meseroll, R.A.1    Howard, L.2    Gladfelter, A.S.3
  • 34
    • 11244348910 scopus 로고    scopus 로고
    • A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus
    • Chen Y, Bjornson K, Redick SD, Erickson HP (2005) A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus. Biophys J 88(1): 505-514.
    • (2005) Biophys J , vol.88 , Issue.1 , pp. 505-514
    • Chen, Y.1    Bjornson, K.2    Redick, S.D.3    Erickson, H.P.4
  • 35
    • 84881461304 scopus 로고    scopus 로고
    • The unusual dynamics of parasite actin result from isodesmic polymerization
    • Skillman KM, et al. (2013) The unusual dynamics of parasite actin result from isodesmic polymerization. Nat Commun 4:2285.
    • (2013) Nat Commun , vol.4 , pp. 2285
    • Skillman, K.M.1
  • 36
    • 33749165924 scopus 로고    scopus 로고
    • Structural insights into yeast septin organization from polarized fluorescence microscopy
    • Vrabioiu AM, Mitchison TJ (2006) Structural insights into yeast septin organization from polarized fluorescence microscopy. Nature 443(7110):466-469.
    • (2006) Nature , vol.443 , Issue.7110 , pp. 466-469
    • Vrabioiu, A.M.1    Mitchison, T.J.2
  • 37
    • 84856395033 scopus 로고    scopus 로고
    • Rapid and quantitative imaging of excitation polarized fluorescence reveals ordered septin dynamics in live yeast
    • DeMay BS, Noda N, Gladfelter AS, Oldenbourg R (2011) Rapid and quantitative imaging of excitation polarized fluorescence reveals ordered septin dynamics in live yeast. Biophys J 101(4):985-994.
    • (2011) Biophys J , vol.101 , Issue.4 , pp. 985-994
    • Demay, B.S.1    Noda, N.2    Gladfelter, A.S.3    Oldenbourg, R.4
  • 38
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider CA, Rasband WS, Eliceiri KW (2012) NIH Image to ImageJ: 25 years of image analysis. Nat Methods 9(7):671-675.
    • (2012) Nat Methods , vol.9 , Issue.7 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.