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Volumn 200, Issue 3, 2015, Pages 841-861

Comprehensive genetic analysis of paralogous terminal septin subunits Shs1 and Cdc11 in Saccharomyces cerevisiae

Author keywords

Complexes; Cytoskeleton; Filaments; Mutants; Yeast

Indexed keywords

CELL CYCLE PROTEIN; CELL DIVISION CYCLE 10; CELL DIVISION CYCLE 11; CELL DIVISION CYCLE 12; CELL DIVISION CYCLE 3; FUNGAL PROTEIN; SEPTIN; SHS1 PROTEIN; UNCLASSIFIED DRUG; CDC11 PROTEIN, S CEREVISIAE; CDC12 PROTEIN, S CEREVISIAE; CDC3 PROTEIN, S CEREVISIAE; CYTOSKELETON PROTEIN; PROFILIN; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE PROTEIN; SHS1 PROTEIN, S CEREVISIAE;

EID: 84937054079     PISSN: 00166731     EISSN: 19432631     Source Type: Journal    
DOI: 10.1534/genetics.115.176495     Document Type: Article
Times cited : (34)

References (92)
  • 1
    • 47849125967 scopus 로고    scopus 로고
    • A multidimensional chromatography technology for in-depth phosphoproteome analysis
    • Albuquerque, C. P., M. B. Smolka, S. H. Payne, V. Bafna, J. Eng et al., 2008 A multidimensional chromatography technology for in-depth phosphoproteome analysis. Mol. Cell. Proteomics 7: 1389-1396.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1389-1396
    • Albuquerque, C.P.1    Smolka, M.B.2    Payne, S.H.3    Bafna, V.4    Eng, J.5
  • 2
    • 0020050588 scopus 로고
    • The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase
    • Bennetzen, J. L., and B. D. Hall, 1982 The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase. J. Biol. Chem. 257: 3018-3025.
    • (1982) J. Biol. Chem , vol.257 , pp. 3018-3025
    • Bennetzen, J.L.1    Hall, B.D.2
  • 3
    • 46149107653 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae septins: Supramolecular organization of heterooligomers and the mechanism of filament assembly
    • Bertin, A., M. A. McMurray, P. Grob, S. S. Park, G. Garcia, 3rd, et al., 2008 Saccharomyces cerevisiae septins: supramolecular organization of heterooligomers and the mechanism of filament assembly. Proc. Natl. Acad. Sci. USA 105: 8274-8279.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8274-8279
    • Bertin, A.1    McMurray, M.A.2    Grob, P.3    Park, S.S.4    Garcia, G.5
  • 4
    • 78649333504 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5-bisphosphate promotes budding yeast septin filament assembly and organization
    • Bertin, A., M. A. McMurray, L. Thai, G. Garcia, 3rd, V. Votin et al., 2010 Phosphatidylinositol-4,5-bisphosphate promotes budding yeast septin filament assembly and organization. J. Mol. Biol. 404: 711-731.
    • (2010) J. Mol. Biol , vol.404 , pp. 711-731
    • Bertin, A.1    McMurray, M.A.2    Thai, L.3    Garcia, V.4    Votin, G.5
  • 5
    • 84856463805 scopus 로고    scopus 로고
    • Three-dimensional ultrastructure of the septin filament network in Saccharomyces cerevisiae
    • Bertin, A., M. A. McMurray, J. Pierson, L. Thai, K. L. McDonald et al., 2012 Three-dimensional ultrastructure of the septin filament network in Saccharomyces cerevisiae. Mol. Biol. Cell 23: 423-432.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 423-432
    • Bertin, A.1    McMurray, M.A.2    Pierson, J.3    Thai, L.4    McDonald, K.L.5
  • 6
    • 0021668558 scopus 로고
    • A positive selection for mutants lacking orotidine-59-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance
    • Boeke, J. D., F. LaCroute, and G. R. Fink, 1984 A positive selection for mutants lacking orotidine-59-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance. Mol. Gen. Genet. 197: 345-346.
    • (1984) Mol. Gen. Genet , vol.197 , pp. 345-346
    • Boeke, J.D.1    LaCroute, F.2    Fink, G.R.3
  • 7
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCRmediated gene disruption and other applications
    • Brachmann, C. B., A. Davies, G. J. Cost, E. Caputo, J. Li et al., 1998 Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCRmediated gene disruption and other applications. Yeast 14: 115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5
  • 8
    • 84856625798 scopus 로고    scopus 로고
    • High-resolution view of the yeast meiotic program revealed by ribosome profiling
    • Brar, G. A., M. Yassour, N. Friedman, A. Rege, N. T. Ingolia et al., 2012 High-resolution view of the yeast meiotic program revealed by ribosome profiling. Science 335: 552-557.
    • (2012) Science , vol.335 , pp. 552-557
    • Brar, G.A.1    Yassour, M.2    Friedman, N.3    Rege, A.4    Ingolia, N.T.5
  • 10
    • 84867477939 scopus 로고    scopus 로고
    • Regulation of the formin Bnr1 by septins anda MARK/Par1-family septin-associated kinase
    • Buttery, S. M., K. Kono, E. Stokasimov, and D. Pellman, 2012 Regulation of the formin Bnr1 by septins anda MARK/Par1-family septin-associated kinase. Mol. Biol. Cell 23: 4041-4053.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 4041-4053
    • Buttery, S.M.1    Kono, K.2    Stokasimov, E.3    Pellman, D.4
  • 11
    • 0017153996 scopus 로고
    • A highly ordered ring of membraneassociated filaments in budding yeast
    • Byers, B., and L. Goetsch, 1976 A highly ordered ring of membraneassociated filaments in budding yeast. J. Cell Biol. 69: 717-721.
    • (1976) J. Cell Biol , vol.69 , pp. 717-721
    • Byers, B.1    Goetsch, L.2
  • 12
    • 0032476582 scopus 로고    scopus 로고
    • The septins are required for the mitosis-specific activation of the Gin4 kinase
    • Carroll, C. W., R. Altman, D. Schieltz, J. R. Yates, and D. Kellogg, 1998 The septins are required for the mitosis-specific activation of the Gin4 kinase. J. Cell Biol. 143: 709-717.
    • (1998) J. Cell Biol , vol.143 , pp. 709-717
    • Carroll, C.W.1    Altman, R.2    Schieltz, D.3    Yates, J.R.4    Kellogg, D.5
  • 13
    • 84905391271 scopus 로고    scopus 로고
    • Polarization of the endoplasmic reticulum by ERseptin tethering
    • Chao, J. T., A. K. Wong, S. Tavassoli, B. P. Young, A. Chruscicki et al., 2014 Polarization of the endoplasmic reticulum by ERseptin tethering. Cell 158: 620-632.
    • (2014) Cell , vol.158 , pp. 620-632
    • Chao, J.T.1    Wong, A.K.2    Tavassoli, S.3    Young, B.P.4    Chruscicki, A.5
  • 14
    • 0032422848 scopus 로고    scopus 로고
    • Cell integrity and morphogenesis in a budding yeast septin mutant
    • Cid, V. J., L. Adamíková, R. Cenamor,, M. Molina, and M. Sánchez et al., 1998 Cell integrity and morphogenesis in a budding yeast septin mutant. Microbiology 144: 3463-3467.
    • (1998) Microbiology , vol.144 , pp. 3463-3467
    • Cid, V.J.1    Adamíková, L.2    Cenamor, R.3    Molina, M.4    Sánchez, M.5
  • 15
    • 3142729153 scopus 로고    scopus 로고
    • Spatial coordination of cytokinetic events by compartmentalization of the cell cortex
    • Dobbelaere, J., and Y. Barral, 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
  • 16
    • 0037345639 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of septin dynamics during the cell cycle
    • Dobbelaere, J., M. S. Gentry, R. L. Hallberg, and Y. Barral, 2003 Phosphorylation-dependent regulation of septin dynamics during the cell cycle. Dev. Cell 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
  • 17
    • 84865067659 scopus 로고    scopus 로고
    • Optimization of ordered plasmid assembly by gap repair in Saccharomyces cerevisiae
    • Eckert-Boulet, N., M. L. Pedersen, B. O. Krogh, and M. Lisby, 2012 Optimization of ordered plasmid assembly by gap repair in Saccharomyces cerevisiae. Yeast 29: 323-334.
    • (2012) Yeast , vol.29 , pp. 323-334
    • Eckert-Boulet, N.1    Pedersen, M.L.2    Krogh, B.O.3    Lisby, M.4
  • 19
    • 44349113516 scopus 로고    scopus 로고
    • The septins function in G1 pathways that influence the pattern of cell growth in budding yeast
    • e2022.2021-e2022.2014
    • Egelhofer, T. A., J. Villen, D. McCusker, S. P. Gygi and D. R. Kellogg, 2008 The septins function in G1 pathways that influence the pattern of cell growth in budding yeast. PLoS One 3: e2022.2021-e2022.2014.
    • (2008) PLoS One , vol.3
    • Egelhofer, T.A.1    Villen, J.2    McCusker, D.3    Gygi, S.P.4    Kellogg, D.R.5
  • 20
    • 33845337082 scopus 로고    scopus 로고
    • Checkpoint proteins control morphogenetic events during DNA replication stress in Saccharomyces cerevisiae
    • Enserink, J. M., M. B. Smolka, H. Zhou, and R. D. Kolodner, 2006 Checkpoint proteins control morphogenetic events during DNA replication stress in Saccharomyces cerevisiae. J. Cell Biol. 175: 729-741.
    • (2006) J. Cell Biol , vol.175 , pp. 729-741
    • Enserink, J.M.1    Smolka, M.B.2    Zhou, H.3    Kolodner, R.D.4
  • 21
    • 26844470092 scopus 로고    scopus 로고
    • Nucleotide binding and filament assembly of recombinant yeast septin complexes
    • Farkasovsky, M., P. Herter, B. Voss, and A. Wittinghofer, 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
  • 22
    • 80052211310 scopus 로고    scopus 로고
    • The reconstructed ancestral subunit a functions as both V-ATPase isoforms Vph1p and Stv1p in Saccharomyces cerevisiae
    • Finnigan, G. C., V. Hanson-Smith, B. D. Houser, H. J. Park, and T. H. Stevens, 2011 The reconstructed ancestral subunit a functions as both V-ATPase isoforms Vph1p and Stv1p in Saccharomyces cerevisiae. Mol. Biol. Cell 22: 3176-3191.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3176-3191
    • Finnigan, G.C.1    Hanson-Smith, V.2    Houser, B.D.3    Park, H.J.4    Stevens, T.H.5
  • 23
    • 84937061343 scopus 로고    scopus 로고
    • The carboxy-terminal tails of septins Cdc11 and Shs1 recruit myosin-II binding factor Bni5 to the bud neck
    • Genetics
    • Finnigan, G. C., E. A. Booth, A. Duvalyan, E. N. Liao and J. Thorner, 2015 The carboxy-terminal tails of septins Cdc11 and Shs1 recruit myosin-II binding factor Bni5 to the bud neck in Saccharomyces cerevisiae. Genetics 821-840.
    • (2015) Saccharomyces cerevisiae , pp. 821-840
    • Finnigan, G.C.1    Booth, E.A.2    Duvalyan, A.3    Liao, E.N.4    Thorner, J.5
  • 24
    • 0026315451 scopus 로고
    • Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: Localization of the CDC11 gene product and the timing of events at the budding site
    • Ford, S. K., and J. R. Pringle, 1991 Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: localization of the CDC11 gene product and the timing of events at the budding site. Dev. Genet. 12: 281-292.
    • (1991) Dev. Genet , vol.12 , pp. 281-292
    • Ford, S.K.1    Pringle, J.R.2
  • 25
    • 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., M. L. Wong, M. S. Longtine, J. R. Pringle, M. Mann et al., 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
  • 27
    • 84862908117 scopus 로고    scopus 로고
    • Subunit-dependent modulation of septin assembly: Budding yeast septin Shs1 promotes ring and gauze formation
    • Garcia, 3rd, G., A. Bertin, Z. Li, Y. Song, M. A. McMurray et al., 2011 Subunit-dependent modulation of septin assembly: budding yeast septin Shs1 promotes ring and gauze formation. J. Cell Biol. 195: 993-1004.
    • (2011) J. Cell Biol , vol.195 , pp. 993-1004
    • Garcia, G.1    Bertin, A.2    Li, Z.3    Song, Y.4    McMurray, M.A.5
  • 28
    • 18844452708 scopus 로고    scopus 로고
    • Interplay between septin organization, cell cycle and cell shape in yeast
    • Gladfelter, A. S., L. Kozubowski, T. R. Zyla, and D. J. Lew, 2005 Interplay between septin organization, cell cycle and cell shape in yeast. J. Cell Sci. 118: 1617-1628.
    • (2005) J. Cell Sci , vol.118 , pp. 1617-1628
    • Gladfelter, A.S.1    Kozubowski, L.2    Zyla, T.R.3    Lew, D.J.4
  • 29
    • 0032873415 scopus 로고    scopus 로고
    • Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae
    • Goldstein, A. L., and J. H. McCusker, 1999 Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae. Yeast 15: 1541-1553.
    • (1999) Yeast , vol.15 , pp. 1541-1553
    • Goldstein, A.L.1    McCusker, J.H.2
  • 30
    • 44949151700 scopus 로고    scopus 로고
    • Sep7 is essential to modify septin ring dynamics and inhibit cell separation during Candida albicans hyphal growth
    • Gonzalez-Novo, A., J. Correa-Bordes, L. Labrador, M. Sanchez, C. R. Vazquez de Aldana et al., 2008 Sep7 is essential to modify septin ring dynamics and inhibit cell separation during Candida albicans hyphal growth. Mol. Biol. Cell 19: 1509-1518.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1509-1518
    • Gonzalez-Novo, A.1    Correa-Bordes, J.2    Labrador, L.3    Sanchez, M.4    Vazquez de Aldana, C.R.5
  • 31
    • 0023429491 scopus 로고
    • Immunofluorescence localization of the Saccharomyces cerevisiae CDC12 gene product to the vicinity of the 10-nm filaments in the mother-bud neck
    • Haarer, B. K., and J. R. Pringle, 1987 Immunofluorescence localization of the Saccharomyces cerevisiae CDC12 gene product to the vicinity of the 10-nm filaments in the mother-bud neck. Mol. Cell. Biol. 7: 3678-3687.
    • (1987) Mol. Cell. Biol , vol.7 , pp. 3678-3687
    • Haarer, B.K.1    Pringle, J.R.2
  • 32
    • 82755189600 scopus 로고    scopus 로고
    • Mammalian septins: Dynamic heteromers with roles in cellular morphogenesis and compartmentalization
    • Hall, P. A., and S. E. Russell, 2012 Mammalian septins: dynamic heteromers with roles in cellular morphogenesis and compartmentalization. J. Pathol. 226: 287-299.
    • (2012) J. Pathol , vol.226 , pp. 287-299
    • Hall, P.A.1    Russell, S.E.2
  • 33
    • 0029091449 scopus 로고
    • Repacking protein cores with backbone freedom: Structure prediction for coiled coils
    • Harbury, P. B., B. Tidor, and P. S. Kim, 1995 Repacking protein cores with backbone freedom: structure prediction for coiled coils. Proc. Natl. Acad. Sci. USA 92: 8408-8412.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8408-8412
    • Harbury, P.B.1    Tidor, B.2    Kim, P.S.3
  • 35
    • 0017893311 scopus 로고
    • Cell division from a genetic perspective
    • Hartwell, L. H., 1978 Cell division from a genetic perspective. J. Cell Biol. 77: 627-637.
    • (1978) J. Cell Biol , vol.77 , pp. 627-637
    • Hartwell, L.H.1
  • 36
    • 0015954720 scopus 로고
    • Genetic control of the cell division cycle in yeast
    • Hartwell, L. H., J. Culotti, J. R. Pringle, and B. J. Reid, 1974 Genetic control of the cell division cycle in yeast. Science 183: 46-51.
    • (1974) Science , vol.183 , pp. 46-51
    • Hartwell, L.H.1    Culotti, J.2    Pringle, J.R.3    Reid, B.J.4
  • 37
    • 84872277354 scopus 로고    scopus 로고
    • Posttranslational modifications and assembly of septin heteropolymers and higherorder structures
    • Hernandez-Rodriguez, Y., and M. Momany, 2012 Posttranslational modifications and assembly of septin heteropolymers and higherorder structures. Curr. Opin. Microbiol. 15: 660-668.
    • (2012) Curr. Opin. Microbiol , vol.15 , pp. 660-668
    • Hernandez-Rodriguez, Y.1    Momany, M.2
  • 38
    • 0035195046 scopus 로고    scopus 로고
    • Nis1 encoded by YNL078W: A new neck protein of Saccharomyces cerevisiae
    • Iwase, M., and A. Toh-e, 2001 Nis1 encoded by YNL078W: a new neck protein of Saccharomyces cerevisiae. Genes Genet. Syst. 76: 335-343.
    • (2001) Genes Genet. Syst , vol.76 , pp. 335-343
    • Iwase, M.1    Toh-E, A.2
  • 39
    • 35048848041 scopus 로고    scopus 로고
    • Shs1 plays separable roles in septin organization and cytokinesis in Saccharomyces cerevisiae
    • Iwase, M., J. Luo, E. Bi, and A. Toh-e, 2007 Shs1 plays separable roles in septin organization and cytokinesis in Saccharomyces cerevisiae. Genetics 177: 215-229.
    • (2007) Genetics , vol.177 , pp. 215-229
    • Iwase, M.1    Luo, J.2    Bi, E.3    Toh-E, A.4
  • 40
    • 84926482977 scopus 로고    scopus 로고
    • Cytosolic chaperones mediate quality control of higher-order septin assembly in budding yeast
    • Johnson, C. R., A. D. Weems, J. M. Brewer, J. Thorner, and M. A. McMurray, 2015 Cytosolic chaperones mediate quality control of higher-order septin assembly in budding yeast. Mol. Biol. Cell 26: 1323-1344.
    • (2015) Mol. Biol. Cell , vol.26 , pp. 1323-1344
    • Johnson, C.R.1    Weems, A.D.2    Brewer, J.M.3    Thorner, J.4    McMurray, M.A.5
  • 41
    • 0033615965 scopus 로고    scopus 로고
    • Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins
    • Johnson, E. S., and G. Blobel, 1999 Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins. J. Cell Biol. 147: 981-994.
    • (1999) J. Cell Biol , vol.147 , pp. 981-994
    • Johnson, E.S.1    Blobel, G.2
  • 42
    • 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, H. B., B. K. Haarer, and J. R. Pringle, 1991 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. 112: 535-544.
    • (1991) J. Cell Biol , vol.112 , pp. 535-544
    • Kim, H.B.1    Haarer, B.K.2    Pringle, J.R.3
  • 43
    • 0036786491 scopus 로고    scopus 로고
    • Bni5p, a septin-interacting protein, is required for normal septin function and cytokinesis in Saccharomyces cerevisiae
    • Lee, P. R., S. Song, H. S. Ro, C. J. Park, J. Lippincott et al., 2002 Bni5p, a septin-interacting protein, is required for normal septin function and cytokinesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 22: 6906-6920.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 6906-6920
    • Lee, P.R.1    Song, S.2    Ro, H.S.3    Park, C.J.4    Lippincott, J.5
  • 44
    • 0034123011 scopus 로고    scopus 로고
    • Septin-dependent assembly of a cell cycleregulatory module in Saccharomyces cerevisiae
    • Longtine, M. S., C. L. Theesfeld, J. N. McMillan, E. Weaver, J. R. Pringle et al., 2000 Septin-dependent assembly of a cell cycleregulatory module in Saccharomyces cerevisiae. Mol. Cell. Biol. 20: 4049-4061.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 4049-4061
    • Longtine, M.S.1    Theesfeld, C.L.2    McMillan, J.N.3    Weaver, E.4    Pringle, J.R.5
  • 45
    • 84873022045 scopus 로고    scopus 로고
    • The structure and properties of septin 3: A possible missing link in septin filament formation
    • Macedo, J. N., N. F. Valadares, I. A. Marques, F. Ferreira, J. C. Damalio et al., 2013 The structure and properties of septin 3: a possible missing link in septin filament formation. Biochem. J. 450: 95-105.
    • (2013) Biochem. J , vol.450 , pp. 95-105
    • McEdo, J.N.1    Valadares, N.F.2    Marques, I.A.3    Ferreira, F.4    Damalio, J.C.5
  • 46
    • 71049147069 scopus 로고    scopus 로고
    • Septins: Molecular partitioning and the generation of cellular asymmetry
    • McMurray, M. A., and J. Thorner, 2009 Septins: molecular partitioning and the generation of cellular asymmetry. Cell Div. 4: 18.11-18.40.
    • (2009) Cell Div , vol.4 , pp. 1811-1840
    • McMurray, M.A.1    Thorner, J.2
  • 47
    • 79954496756 scopus 로고    scopus 로고
    • Septin filament formation is essential in budding yeast
    • McMurray, M. A., A. Bertin, G. Garcia, 3rd, L. Lam, E. Nogales et al., 2011 Septin filament formation is essential in budding yeast. Dev. Cell 20: 540-549.
    • (2011) Dev. Cell , vol.20 , pp. 540-549
    • McMurray, M.A.1    Bertin, A.2    Garcia, G.3    Lam, L.4    Nogales, E.5
  • 48
    • 79955368638 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of the F-BAR protein Hof1 during cytokinesis
    • Meitinger, F., M. E. Boehm, A. Hofmann, B. Hub, H. Zentgraf et al., 2011 Phosphorylation-dependent regulation of the F-BAR protein Hof1 during cytokinesis. Genes Dev. 25: 875-888.
    • (2011) Genes Dev , vol.25 , pp. 875-888
    • Meitinger, F.1    Boehm, M.E.2    Hofmann, A.3    Hub, B.4    Zentgraf, H.5
  • 49
    • 84877104017 scopus 로고    scopus 로고
    • Dual function of the NDR-kinase Dbf2 in the regulation of the F-BAR protein Hof1 during cytokinesis
    • Meitinger, F., S. Palani, B. Hub, and G. Pereira, 2013 Dual function of the NDR-kinase Dbf2 in the regulation of the F-BAR protein Hof1 during cytokinesis. Mol. Biol. Cell 24: 1290-1304.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1290-1304
    • Meitinger, F.1    Palani, S.2    Hub, B.3    Pereira, G.4
  • 50
    • 84865739164 scopus 로고    scopus 로고
    • Septin ring size scaling and dynamics require the coiled-coil region of Shs1p
    • Meseroll, R. A., L. Howard, and A. S. Gladfelter, 2012 Septin ring size scaling and dynamics require the coiled-coil region of Shs1p. Mol. Biol. Cell 23: 3391-3406.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3391-3406
    • Meseroll, R.A.1    Howard, L.2    Gladfelter, A.S.3
  • 52
    • 0032578776 scopus 로고    scopus 로고
    • Shs1p: A novel member of septin that interacts with spa2p, involved in polarized growth in Saccharomyces cerevisiae
    • Mino, A., K. Tanaka, T. Kamei, M. Umikawa, T. Fujiwara et al., 1998 Shs1p: a novel member of septin that interacts with spa2p, involved in polarized growth in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 251: 732-736.
    • (1998) Biochem. Biophys. Res. Commun , vol.251 , pp. 732-736
    • Mino, A.1    Tanaka, K.2    Kamei, T.3    Umikawa, M.4    Fujiwara, T.5
  • 53
    • 0031080575 scopus 로고    scopus 로고
    • The Aspergillus nidulans septin encoding gene, aspB, is essential for growth
    • Momany, M., and J. E. Hamer, 1997 The Aspergillus nidulans septin encoding gene, aspB, is essential for growth. Fungal Genet. Biol. 21: 92-100.
    • (1997) Fungal Genet. Biol , vol.21 , pp. 92-100
    • Momany, M.1    Hamer, J.E.2
  • 54
    • 0035985207 scopus 로고    scopus 로고
    • Cell cycle-dependent assembly of a Gin4-septin complex
    • Mortensen, E. M., H. McDonald, J. Yates, 3rd, and D. R. Kellogg, 2002 Cell cycle-dependent assembly of a Gin4-septin complex. Mol. Biol. Cell 13: 2091-2105.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2091-2105
    • Mortensen, E.M.1    McDonald, H.2    Yates, J.3    Kellogg, D.R.4
  • 55
    • 0022504637 scopus 로고
    • Genealogy of principal strains of the Yeast Genetic Stock Center
    • Mortimer, R. K., and J. R. Johnston, 1986 Genealogy of principal strains of the Yeast Genetic Stock Center. Genetics 113: 35-43.
    • (1986) Genetics , vol.113 , pp. 35-43
    • Mortimer, R.K.1    Johnston, J.R.2
  • 56
    • 84857457272 scopus 로고    scopus 로고
    • Septins: The fourth component of the cytoskeleton
    • Mostowy, S., and P. Cossart, 2012 Septins: the fourth component of the cytoskeleton. Nat. Rev. Mol. Cell Biol. 13: 183-194.
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , pp. 183-194
    • Mostowy, S.1    Cossart, P.2
  • 57
    • 0030858237 scopus 로고    scopus 로고
    • Helix propensities are identical in proteins and peptides
    • Myers, J. K., C. N. Pace, and J. M. Scholtz, 1997 Helix propensities are identical in proteins and peptides. Biochemistry 36: 10923-10929.
    • (1997) Biochemistry , vol.36 , pp. 10923-10929
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 58
    • 49449093766 scopus 로고    scopus 로고
    • Role of nucleotide binding in septin-septin interactions and septin localization in Saccharomyces cerevisiae
    • Nagaraj, S., A. Rajendran, C. E. Jackson, and M. S. Longtine, 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
  • 59
    • 81255176779 scopus 로고    scopus 로고
    • Sporulation in the budding yeast Saccharomyces cerevisiae
    • Neiman, A. M., 2011 Sporulation in the budding yeast Saccharomyces cerevisiae. Genetics 189: 737-765.
    • (2011) Genetics , vol.189 , pp. 737-765
    • Neiman, A.M.1
  • 60
    • 67449110962 scopus 로고    scopus 로고
    • Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage furrow and septum formation in S. cerevisiae
    • Nishihama, R., J. H. Schreiter, M. Onishi, E. A. Vallen, J. Hanna et al., 2009 Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage furrow and septum formation in S. cerevisiae. J. Cell Biol. 185: 995-1012.
    • (2009) J. Cell Biol , vol.185 , pp. 995-1012
    • Nishihama, R.1    Schreiter, J.H.2    Onishi, M.3    Vallen, E.A.4    Hanna, J.5
  • 61
    • 80052719413 scopus 로고    scopus 로고
    • New insights into the phylogenetic distribution and evolutionary origins of the septins
    • Nishihama, R., M. Onishi, and J. R. Pringle, 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
  • 62
    • 84923321595 scopus 로고    scopus 로고
    • Architecture and dynamic remodelling of the septin cytoskeleton during the cell cycle
    • Ong, K., C. Wloka, S. Okada, T. Svitkina,, and E. Bi, 2014 Architecture and dynamic remodelling of the septin cytoskeleton during the cell cycle. Nat. Commun. 5: 5698.5691-5698.5610.
    • (2014) Nat. Commun , vol.5
    • Ong, K.1    Wloka, C.2    Okada, S.3    Svitkina, T.4    Bi, E.5
  • 63
    • 34547121710 scopus 로고    scopus 로고
    • Analysis of septins across kingdoms reveals orthology and new motifs
    • Pan, F., R. L. Malmberg, and M. Momany, 2007 Analysis of septins across kingdoms reveals orthology and new motifs. BMC Evol. Biol. 7: 103-119.
    • (2007) BMC Evol. Biol , vol.7 , pp. 103-119
    • Pan, F.1    Malmberg, R.L.2    Momany, M.3
  • 64
    • 51349107479 scopus 로고    scopus 로고
    • Fifty years of coiled-coils and alpha-helical bundles: A close relationship between sequence and structure
    • Parry, D. A., R. D. Fraser, and J. M. Squire, 2008 Fifty years of coiled-coils and alpha-helical bundles: a close relationship between sequence and structure. J. Struct. Biol. 163: 258-269.
    • (2008) J. Struct. Biol , vol.163 , pp. 258-269
    • Parry, D.A.1    Fraser, R.D.2    Squire, J.M.3
  • 65
    • 77953570400 scopus 로고    scopus 로고
    • Origins and development of the septin field
    • edited by P. A. Hall, S. E. H. Russell, and J. R. Pringle. Wiley, Chichester, West Sussex, UK
    • Pringle, J. R., 2008 Origins and development of the septin field, pp. 7-34 in The Septins, edited by P. A. Hall, S. E. H. Russell, and J. R. Pringle. Wiley, Chichester, West Sussex, UK.
    • (2008) The Septins , pp. 7-34
    • Pringle, J.R.1
  • 67
    • 68949184722 scopus 로고    scopus 로고
    • Septins, a novel group of GTP-binding proteins: Relevance in hemostasis, neuropathology and oncogenesis
    • Roeseler, S., K. Sandrock, I. Bartsch, and B. Zieger, 2009 Septins, a novel group of GTP-binding proteins: relevance in hemostasis, neuropathology and oncogenesis. Klin. Padiatr. 221: 150-155.
    • (2009) Klin. Padiatr , vol.221 , pp. 150-155
    • Roeseler, S.1    Sandrock, K.2    Bartsch, I.3    Zieger, B.4
  • 68
    • 0025979877 scopus 로고
    • Targeting, disruption, replacement, and allele rescue: Integrative DNA transformation in yeast
    • Rothstein, R., 1991 Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol. 194: 281-301.
    • (1991) Methods Enzymol , vol.194 , pp. 281-301
    • Rothstein, R.1
  • 69
    • 80255140317 scopus 로고    scopus 로고
    • The emerging functions of septins in metazoans
    • Saarikangas, J., and Y. Barral, 2011 The emerging functions of septins in metazoans. EMBO Rep. 12: 1118-1126.
    • (2011) EMBO Rep , vol.12 , pp. 1118-1126
    • Saarikangas, J.1    Barral, Y.2
  • 71
    • 0028519206 scopus 로고
    • Cell division: Septins in common?
    • Sanders, L., and C. M. Field, 1994 Cell division: Septins in common? Curr. Biol. 4: 907-910.
    • (1994) Curr. Biol , vol.4 , pp. 907-910
    • Sanders, L.1    Field, C.M.2
  • 72
    • 0037910282 scopus 로고    scopus 로고
    • Septins, under Cla4p regulation, and the chitin ring are required for neck integrity in budding yeast
    • Schmidt, M., A. Varma, T. Drgon, B. Bowers, and E. Cabib, 2003 Septins, under Cla4p regulation, and the chitin ring are required for neck integrity in budding yeast. Mol. Biol. Cell 14: 2128-2141.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2128-2141
    • Schmidt, M.1    Varma, A.2    Drgon, T.3    Bowers, B.4    Cabib, E.5
  • 73
    • 84868247055 scopus 로고    scopus 로고
    • Mammalian SEPT9 isoforms direct microtubule-dependent arrangements of septin core heteromers
    • Sellin, M. E., S. Stenmark, and M. Gullberg, 2012 Mammalian SEPT9 isoforms direct microtubule-dependent arrangements of septin core heteromers. Mol. Biol. Cell 23: 4242-4255.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 4242-4255
    • Sellin, M.E.1    Stenmark, S.2    Gullberg, M.3
  • 74
    • 84901228103 scopus 로고    scopus 로고
    • Cell type-specific expression of SEPT3-homology subgroup members controls the subunit number of heteromeric septin complexes
    • Sellin, M. E., S. Stenmark, and M. Gullberg, 2014 Cell type-specific expression of SEPT3-homology subgroup members controls the subunit number of heteromeric septin complexes. Mol. Biol. Cell 25: 1594-1607.
    • (2014) Mol. Biol. Cell , vol.25 , pp. 1594-1607
    • Sellin, M.E.1    Stenmark, S.2    Gullberg, M.3
  • 75
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner, N. C., R. E. Campbell, P. A. Steinbach, B. N. Giepmans, A. E. Palmer et al., 2004 Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat. Biotechnol. 22: 1567-1572.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5
  • 76
    • 3042722112 scopus 로고    scopus 로고
    • Optimized cassettes for fluorescent protein tagging in Saccharomyces cerevisiae
    • Sheff, M. A., and K. S. Thorn, 2004 Optimized cassettes for fluorescent protein tagging in Saccharomyces cerevisiae. Yeast 21: 661-670.
    • (2004) Yeast , vol.21 , pp. 661-670
    • Sheff, M.A.1    Thorn, K.S.2
  • 78
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter, 1989 A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 79
    • 34548818799 scopus 로고    scopus 로고
    • Structural insight into filament formation by mammalian septins
    • Sirajuddin, M., M. Farkasovsky, F. Hauer, D. Kuhlmann, I. G. Macara et al., 2007 Structural insight into filament formation by mammalian septins. Nature 449: 311-315.
    • (2007) Nature , vol.449 , pp. 311-315
    • Sirajuddin, M.1    Farkasovsky, M.2    Hauer, F.3    Kuhlmann, D.4    McAra, I.G.5
  • 80
  • 81
    • 33845348182 scopus 로고    scopus 로고
    • An FHA domain-mediated protein interaction network of Rad53 reveals its role in polarized cell growth
    • Smolka, M. B., S. H. Chen, P. S. Maddox, J. M. Enserink, C. P. Albuquerque et al., 2006 An FHA domain-mediated protein interaction network of Rad53 reveals its role in polarized cell growth. J. Cell Biol. 175: 743-753.
    • (2006) J. Cell Biol , vol.175 , pp. 743-753
    • Smolka, M.B.1    Chen, S.H.2    Maddox, P.S.3    Enserink, J.M.4    Albuquerque, C.P.5
  • 82
    • 34547499407 scopus 로고    scopus 로고
    • Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases
    • Smolka, M. B., C. P. Albuquerque, S. H. Chen, and H. Zhou, 2007 Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases. Proc. Natl. Acad. Sci. USA 104: 10364-10369.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10364-10369
    • Smolka, M.B.1    Albuquerque, C.P.2    Chen, S.H.3    Zhou, H.4
  • 83
    • 58349115398 scopus 로고    scopus 로고
    • Septinmediated uniform bracing of phospholipid membranes
    • Tanaka-Takiguchi, Y., M. Kinoshita, and K. Takiguchi, 2009 Septinmediated uniform bracing of phospholipid membranes. Curr. Biol. 19: 140-145.
    • (2009) Curr. Biol , vol.19 , pp. 140-145
    • Tanaka-Takiguchi, Y.1    Kinoshita, M.2    Takiguchi, K.3
  • 84
    • 0036046999 scopus 로고    scopus 로고
    • Phosphorylation of the septin cdc3 in g1 by the cdc28 kinase is essential for efficient septin ring disassembly
    • Tang, C. S., and S. I. Reed, 2002 Phosphorylation of the septin cdc3 in g1 by the cdc28 kinase is essential for efficient septin ring disassembly. Cell Cycle 1: 42-49.
    • (2002) Cell Cycle , vol.1 , pp. 42-49
    • Tang, C.S.1    Reed, S.I.2
  • 85
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson, 1994 CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 86
    • 1442334322 scopus 로고    scopus 로고
    • Septin collar formation in budding yeast requires GTP binding and direct phosphorylation by the PAK, Cla4
    • Versele, M., and J. Thorner, 2004 Septin collar formation in budding yeast requires GTP binding and direct phosphorylation by the PAK, Cla4. J. Cell Biol. 164: 701-715.
    • (2004) J. Cell Biol , vol.164 , pp. 701-715
    • Versele, M.1    Thorner, J.2
  • 87
    • 4644251602 scopus 로고    scopus 로고
    • Protein-protein interactions governing septin heteropentamer assembly and septin filament organization in Saccharomyces cerevisiae
    • Versele, M., B. Gullbrand, M. J. Shulewitz, V. J. Cid, S. Bahmanyar et al., 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
  • 88
    • 84901339707 scopus 로고    scopus 로고
    • Higher-order septin assembly is driven by GTP-promoted conformational changes: Evidence from unbiased mutational analysis in Saccharomyces cerevisiae
    • Weems, A. D., C. R. Johnson, J. L. Argueso, and M. A. McMurray, 2014 Higher-order septin assembly is driven by GTP-promoted conformational changes: evidence from unbiased mutational analysis in Saccharomyces cerevisiae. Genetics 196: 711-727.
    • (2014) Genetics , vol.196 , pp. 711-727
    • Weems, A.D.1    Johnson, C.R.2    Argueso, J.L.3    McMurray, M.A.4
  • 90
    • 80052713192 scopus 로고    scopus 로고
    • Structural and biochemical properties of Sept7, a unique septin required for filament formation
    • Zent, E., I. Vetter, and A. Wittinghofer, 2011 Structural and biochemical properties of Sept7, a unique septin required for filament formation. Biol. Chem. 392: 791-797.
    • (2011) Biol. Chem , vol.392 , pp. 791-797
    • Zent, E.1    Vetter, I.2    Wittinghofer, A.3
  • 91
    • 0033576647 scopus 로고    scopus 로고
    • Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP
    • Zhang, J., C. Kong, H. Xie, P. S. McPherson, S. Grinstein et al., 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
  • 92
    • 3843146246 scopus 로고    scopus 로고
    • An efficient onestep site-directed and site-saturation mutagenesis protocol
    • Zheng, L., U. Baumann and J. L. Reymond, 2004 An efficient onestep site-directed and site-saturation mutagenesis protocol. Nucleic Acids Res. 32: e115.111-e115.115.
    • (2004) Nucleic Acids Res , vol.32 , pp. e115111-e115115
    • Zheng, L.1    Baumann, U.2    Reymond, J.L.3


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