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Volumn 8, Issue 1, 2013, Pages

Katanin Localization Requires Triplet Microtubules in Chlamydomonas reinhardtii

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; EPSILON TUBULIN; INTRAFLAGELLAR TRANSPORT 74 PROTEIN; KATANIN PROTEIN; MICROTUBULE PROTEIN; PACLITAXEL; PROTEIN P60; PROTEIN P80; TUBULIN; UNCLASSIFIED DRUG;

EID: 84872184534     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0053940     Document Type: Article
Times cited : (18)

References (90)
  • 1
    • 0345688612 scopus 로고    scopus 로고
    • Mechanisms of Taxol resistance related to microtubules
    • Orr GA, Verdier-Pinard P, McDaid H, Horwitz SB, (2003) Mechanisms of Taxol resistance related to microtubules. Oncogene 22: 7280-7295.
    • (2003) Oncogene , vol.22 , pp. 7280-7295
    • Orr, G.A.1    Verdier-Pinard, P.2    McDaid, H.3    Horwitz, S.B.4
  • 2
    • 0025921758 scopus 로고
    • The colR4 and colR15 beta-tubulin mutations in Chlamydomonas reinhardtii confer altered sensitivities to microtubule inhibitors and herbicides by enhancing microtubule stability
    • Schibler MJ, Huang B, (1991) The colR4 and colR15 beta-tubulin mutations in Chlamydomonas reinhardtii confer altered sensitivities to microtubule inhibitors and herbicides by enhancing microtubule stability. J Cell Biol 113: 605-614.
    • (1991) J Cell Biol , vol.113 , pp. 605-614
    • Schibler, M.J.1    Huang, B.2
  • 3
    • 18344403503 scopus 로고    scopus 로고
    • Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit
    • Hartman JJ, Mahr J, McNally K, Okawa K, Iwamatsu A, et al. (1998) Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit. Cell 93: 277-287.
    • (1998) Cell , vol.93 , pp. 277-287
    • Hartman, J.J.1    Mahr, J.2    McNally, K.3    Okawa, K.4    Iwamatsu, A.5
  • 4
    • 0029978787 scopus 로고    scopus 로고
    • Katanin, the microtubule-severing ATPase, is concentrated at centrosomes
    • McNally FJ, Okawa K, Iwamatsu A, Vale RD, (1996) Katanin, the microtubule-severing ATPase, is concentrated at centrosomes. J Cell Sci 109 (Pt 3): 561-567.
    • (1996) J Cell Sci , vol.109 , Issue.Pt 3 , pp. 561-567
    • McNally, F.J.1    Okawa, K.2    Iwamatsu, A.3    Vale, R.D.4
  • 5
    • 34247526438 scopus 로고    scopus 로고
    • Three microtubule severing enzymes contribute to the "Pacman-flux" machinery that moves chromosomes
    • Zhang D, Rogers GC, Buster DW, Sharp DJ, (2007) Three microtubule severing enzymes contribute to the "Pacman-flux" machinery that moves chromosomes. J Cell Biol 177: 231-242.
    • (2007) J Cell Biol , vol.177 , pp. 231-242
    • Zhang, D.1    Rogers, G.C.2    Buster, D.W.3    Sharp, D.J.4
  • 6
    • 0034192639 scopus 로고    scopus 로고
    • MEI-1/MEI-2 katanin-like microtubule severing activity is required for Caenorhabditis elegans meiosis
    • Srayko M, Buster DW, Bazirgan OA, McNally FJ, Mains PE, (2000) MEI-1/MEI-2 katanin-like microtubule severing activity is required for Caenorhabditis elegans meiosis. Genes Dev 14: 1072-1084.
    • (2000) Genes Dev , vol.14 , pp. 1072-1084
    • Srayko, M.1    Buster, D.W.2    Bazirgan, O.A.3    McNally, F.J.4    Mains, P.E.5
  • 7
    • 34548838592 scopus 로고    scopus 로고
    • Katanin regulates dynamics of microtubules and biogenesis of motile cilia
    • Sharma N, Bryant J, Wloga D, Donaldson R, Davis RC, et al. (2007) Katanin regulates dynamics of microtubules and biogenesis of motile cilia. J Cell Biol 178: 1065-1079.
    • (2007) J Cell Biol , vol.178 , pp. 1065-1079
    • Sharma, N.1    Bryant, J.2    Wloga, D.3    Donaldson, R.4    Davis, R.C.5
  • 8
    • 39549095614 scopus 로고    scopus 로고
    • Drosophila SPD-2 is an essential centriole component required for PCM recruitment and astral-microtubule nucleation
    • Giansanti MG, Bucciarelli E, Bonaccorsi S, Gatti M, (2008) Drosophila SPD-2 is an essential centriole component required for PCM recruitment and astral-microtubule nucleation. Curr Biol 18: 303-309.
    • (2008) Curr Biol , vol.18 , pp. 303-309
    • Giansanti, M.G.1    Bucciarelli, E.2    Bonaccorsi, S.3    Gatti, M.4
  • 9
    • 3042688773 scopus 로고    scopus 로고
    • The Caenorhabditis elegans centrosomal protein SPD-2 is required for both pericentriolar material recruitment and centriole duplication
    • Pelletier L, Ozlu N, Hannak E, Cowan C, Habermann B, et al. (2004) The Caenorhabditis elegans centrosomal protein SPD-2 is required for both pericentriolar material recruitment and centriole duplication. Curr Biol 14: 863-873.
    • (2004) Curr Biol , vol.14 , pp. 863-873
    • Pelletier, L.1    Ozlu, N.2    Hannak, E.3    Cowan, C.4    Habermann, B.5
  • 10
    • 33748440647 scopus 로고    scopus 로고
    • Sequential protein recruitment in C. elegans centriole formation
    • Delattre M, Canard C, Gonczy P, (2006) Sequential protein recruitment in C. elegans centriole formation. Curr Biol 16: 1844-1849.
    • (2006) Curr Biol , vol.16 , pp. 1844-1849
    • Delattre, M.1    Canard, C.2    Gonczy, P.3
  • 12
    • 48849104246 scopus 로고    scopus 로고
    • Functional characterization of the microtubule-binding and -destabilizing domains of CPAP and d-SAS-4
    • Hsu WB, Hung LY, Tang CJ, Su CL, Chang Y, et al. (2008) Functional characterization of the microtubule-binding and-destabilizing domains of CPAP and d-SAS-4. Exp Cell Res 314: 2591-2602.
    • (2008) Exp Cell Res , vol.314 , pp. 2591-2602
    • Hsu, W.B.1    Hung, L.Y.2    Tang, C.J.3    Su, C.L.4    Chang, Y.5
  • 13
    • 78650437294 scopus 로고    scopus 로고
    • Centrioles regulate centrosome size by controlling the rate of Cnn incorporation into the PCM
    • Conduit PT, Brunk K, Dobbelaere J, Dix CI, Lucas EP, et al. (2010) Centrioles regulate centrosome size by controlling the rate of Cnn incorporation into the PCM. Curr Biol 20: 2178-2186.
    • (2010) Curr Biol , vol.20 , pp. 2178-2186
    • Conduit, P.T.1    Brunk, K.2    Dobbelaere, J.3    Dix, C.I.4    Lucas, E.P.5
  • 14
    • 35348903253 scopus 로고    scopus 로고
    • Drosophila Spd-2 recruits PCM to the sperm centriole, but is dispensable for centriole duplication
    • Dix CI, Raff JW, (2007) Drosophila Spd-2 recruits PCM to the sperm centriole, but is dispensable for centriole duplication. Curr Biol 17: 1759-1764.
    • (2007) Curr Biol , vol.17 , pp. 1759-1764
    • Dix, C.I.1    Raff, J.W.2
  • 15
    • 0033825277 scopus 로고    scopus 로고
    • Microtubule minus-end anchorage of centrosomal and non-centrosomal sites: the role of ninein
    • Mogensen M, Malik A, Piel M, Bouckson-Castaing V, Bornens M, (2000) Microtubule minus-end anchorage of centrosomal and non-centrosomal sites: the role of ninein. Journal of Cell Science 113: 3013-3023.
    • (2000) Journal of Cell Science , vol.113 , pp. 3013-3023
    • Mogensen, M.1    Malik, A.2    Piel, M.3    Bouckson-Castaing, V.4    Bornens, M.5
  • 16
    • 34247124794 scopus 로고    scopus 로고
    • hNinein is required for targeting spindle-associated protein Astrin to the centrosome during the S and G2 phases
    • Cheng TS, Hsiao YL, Lin CC, Hsu CM, Chang MS, et al. (2007) hNinein is required for targeting spindle-associated protein Astrin to the centrosome during the S and G2 phases. Exp Cell Res 313: 1710-1721.
    • (2007) Exp Cell Res , vol.313 , pp. 1710-1721
    • Cheng, T.S.1    Hsiao, Y.L.2    Lin, C.C.3    Hsu, C.M.4    Chang, M.S.5
  • 17
    • 34447514268 scopus 로고    scopus 로고
    • Structure and duplication of the centrosome
    • Azimzadeh J, Bornens M, (2007) Structure and duplication of the centrosome. J Cell Sci 120: 2139-2142.
    • (2007) J Cell Sci , vol.120 , pp. 2139-2142
    • Azimzadeh, J.1    Bornens, M.2
  • 18
    • 0038421025 scopus 로고    scopus 로고
    • Elucidation of basal body and centriole functions in Chlamydomonas reinhardtii
    • Dutcher SK, (2003) Elucidation of basal body and centriole functions in Chlamydomonas reinhardtii. Traffic 4: 443-451.
    • (2003) Traffic , vol.4 , pp. 443-451
    • Dutcher, S.K.1
  • 19
    • 0031750484 scopus 로고    scopus 로고
    • Chlamydomonas kinesin-II-dependent intraflagellar transport (IFT): IFT particles contain proteins required for ciliary assembly in Caenorhabditis elegans sensory neurons
    • Cole DG, Diener DR, Himelblau AL, Beech PL, Fuster JC, et al. (1998) Chlamydomonas kinesin-II-dependent intraflagellar transport (IFT): IFT particles contain proteins required for ciliary assembly in Caenorhabditis elegans sensory neurons. J Cell Biol 141: 993-1008.
    • (1998) J Cell Biol , vol.141 , pp. 993-1008
    • Cole, D.G.1    Diener, D.R.2    Himelblau, A.L.3    Beech, P.L.4    Fuster, J.C.5
  • 20
    • 0035899865 scopus 로고    scopus 로고
    • Localization of intraflagellar transport protein IFT52 identifies basal body transitional fibers as the docking site for IFT particles
    • Deane JA, Cole DG, Seeley ES, Diener DR, Rosenbaum JL, (2001) Localization of intraflagellar transport protein IFT52 identifies basal body transitional fibers as the docking site for IFT particles. Curr Biol 11: 1586-1590.
    • (2001) Curr Biol , vol.11 , pp. 1586-1590
    • Deane, J.A.1    Cole, D.G.2    Seeley, E.S.3    Diener, D.R.4    Rosenbaum, J.L.5
  • 21
    • 0016686163 scopus 로고
    • BALD-2: a mutation affecting the formation of doublet and triplet sets of microtubules in Chlamydomonas reinhardtii
    • Goodenough UW, StClair HS, (1975) BALD-2: a mutation affecting the formation of doublet and triplet sets of microtubules in Chlamydomonas reinhardtii. J Cell Biol 66: 480-491.
    • (1975) J Cell Biol , vol.66 , pp. 480-491
    • Goodenough, U.W.1    StClair, H.S.2
  • 22
    • 0031867055 scopus 로고    scopus 로고
    • The UNI3 gene is required for assembly of basal bodies of Chlamydomonas and encodes delta-tubulin, a new member of the tubulin superfamily
    • Dutcher SK, Trabuco EC, (1998) The UNI3 gene is required for assembly of basal bodies of Chlamydomonas and encodes delta-tubulin, a new member of the tubulin superfamily. Mol Biol Cell 9: 1293-1308.
    • (1998) Mol Biol Cell , vol.9 , pp. 1293-1308
    • Dutcher, S.K.1    Trabuco, E.C.2
  • 23
    • 2942633899 scopus 로고    scopus 로고
    • Bld10p, a novel protein essential for basal body assembly in Chlamydomonas: localization to the cartwheel, the first ninefold symmetrical structure appearing during assembly
    • Matsuura K, Lefebvre PA, Kamiya R, Hirono M, (2004) Bld10p, a novel protein essential for basal body assembly in Chlamydomonas: localization to the cartwheel, the first ninefold symmetrical structure appearing during assembly. J Cell Biol 165: 663-671.
    • (2004) J Cell Biol , vol.165 , pp. 663-671
    • Matsuura, K.1    Lefebvre, P.A.2    Kamiya, R.3    Hirono, M.4
  • 25
    • 48449085139 scopus 로고    scopus 로고
    • SAS-6 is a cartwheel protein that establishes the 9-fold symmetry of the centriole
    • Nakazawa Y, Hiraki M, Kamiya R, Hirono M, (2007) SAS-6 is a cartwheel protein that establishes the 9-fold symmetry of the centriole. Curr Biol 17: 2169-2174.
    • (2007) Curr Biol , vol.17 , pp. 2169-2174
    • Nakazawa, Y.1    Hiraki, M.2    Kamiya, R.3    Hirono, M.4
  • 26
    • 0020162181 scopus 로고
    • Uniflagellar mutants of Chlamydomonas: evidence for the role of basal bodies in transmission of positional information
    • Huang B, Ramanis Z, Dutcher SK, Luck DJ, (1982) Uniflagellar mutants of Chlamydomonas: evidence for the role of basal bodies in transmission of positional information. Cell 29: 745-753.
    • (1982) Cell , vol.29 , pp. 745-753
    • Huang, B.1    Ramanis, Z.2    Dutcher, S.K.3    Luck, D.J.4
  • 27
    • 38749106600 scopus 로고    scopus 로고
    • The Uni2 phosphoprotein is a cell cycle regulated component of the basal body maturation pathway in Chlamydomonas reinhardtii
    • Piasecki BP, LaVoie M, Tam LW, Lefebvre PA, Silflow CD, (2008) The Uni2 phosphoprotein is a cell cycle regulated component of the basal body maturation pathway in Chlamydomonas reinhardtii. Mol Biol Cell 19: 262-273.
    • (2008) Mol Biol Cell , vol.19 , pp. 262-273
    • Piasecki, B.P.1    LaVoie, M.2    Tam, L.W.3    Lefebvre, P.A.4    Silflow, C.D.5
  • 28
    • 63049112724 scopus 로고    scopus 로고
    • The UNI1 and UNI2 genes function in the transition of triplet to doublet microtubules between the centriole and cilium in Chlamydomonas
    • Piasecki BP, Silflow CD, (2009) The UNI1 and UNI2 genes function in the transition of triplet to doublet microtubules between the centriole and cilium in Chlamydomonas. Mol Biol Cell 20: 368-378.
    • (2009) Mol Biol Cell , vol.20 , pp. 368-378
    • Piasecki, B.P.1    Silflow, C.D.2
  • 29
    • 84872170562 scopus 로고    scopus 로고
    • VFL3 encodes a conserved protein needed for probasal body attachment J Cell Biol
    • Iyaduri KB, Silflow CD, (2004) VFL3 encodes a conserved protein needed for probasal body attachment J Cell Biol. 45: A167.
    • (2004) , vol.45
    • Iyaduri, K.B.1    Silflow, C.D.2
  • 30
    • 0035795416 scopus 로고    scopus 로고
    • The Vfl1 Protein in Chlamydomonas localizes in a rotationally asymmetric pattern at the distal ends of the basal bodies
    • Silflow CD, LaVoie M, Tam LW, Tousey S, Sanders M, et al. (2001) The Vfl1 Protein in Chlamydomonas localizes in a rotationally asymmetric pattern at the distal ends of the basal bodies. J Cell Biol 153: 63-74.
    • (2001) J Cell Biol , vol.153 , pp. 63-74
    • Silflow, C.D.1    LaVoie, M.2    Tam, L.W.3    Tousey, S.4    Sanders, M.5
  • 31
    • 0027071802 scopus 로고
    • Mutational analysis of centrin: an EF-hand protein associated with three distinct contractile fibers in the basal body apparatus of Chlamydomonas
    • Taillon BE, Adler SA, Suhan JP, Jarvik JW, (1992) Mutational analysis of centrin: an EF-hand protein associated with three distinct contractile fibers in the basal body apparatus of Chlamydomonas. J Cell Biol 119: 1613-1624.
    • (1992) J Cell Biol , vol.119 , pp. 1613-1624
    • Taillon, B.E.1    Adler, S.A.2    Suhan, J.P.3    Jarvik, J.W.4
  • 32
    • 17444447828 scopus 로고
    • Cellular asymmetry in Chlamydomonas reinhardtii
    • Holmes JA, Dutcher SK, (1989) Cellular asymmetry in Chlamydomonas reinhardtii. J Cell Sci 94 (Pt 2): 273-285.
    • (1989) J Cell Sci , vol.94 , Issue.Pt 2 , pp. 273-285
    • Holmes, J.A.1    Dutcher, S.K.2
  • 33
    • 0029197696 scopus 로고
    • Mating and tetrad analysis in Chlamydomonas reinhardtii
    • Dutcher SK, (1995) Mating and tetrad analysis in Chlamydomonas reinhardtii. Methods Cell Biol 47: 531-540.
    • (1995) Methods Cell Biol , vol.47 , pp. 531-540
    • Dutcher, S.K.1
  • 34
    • 0035152423 scopus 로고    scopus 로고
    • Extragenic bypass suppressors of mutations in the essential gene BLD2 promote assembly of basal bodies with abnormal microtubules in Chlamydomonas reinhardtii
    • Preble AM, Giddings TH Jr, Dutcher SK, (2001) Extragenic bypass suppressors of mutations in the essential gene BLD2 promote assembly of basal bodies with abnormal microtubules in Chlamydomonas reinhardtii. Genetics 157: 163-181.
    • (2001) Genetics , vol.157 , pp. 163-181
    • Preble, A.M.1    Giddings Jr., T.H.2    Dutcher, S.K.3
  • 35
    • 0032091887 scopus 로고    scopus 로고
    • Identification of the gene encoding the tryptophan synthase beta-subunit from Chlamydomonas reinhardtii
    • Palombella AL, Dutcher SK, (1998) Identification of the gene encoding the tryptophan synthase beta-subunit from Chlamydomonas reinhardtii. Plant Physiol 117: 455-464.
    • (1998) Plant Physiol , vol.117 , pp. 455-464
    • Palombella, A.L.1    Dutcher, S.K.2
  • 36
    • 0026694203 scopus 로고
    • Tryptophan analog resistance mutations in Chlamydomonas reinhardtii
    • Dutcher SK, Galloway RE, Barclay WR, Poortinga G, (1992) Tryptophan analog resistance mutations in Chlamydomonas reinhardtii. Genetics 131: 593-607.
    • (1992) Genetics , vol.131 , pp. 593-607
    • Dutcher, S.K.1    Galloway, R.E.2    Barclay, W.R.3    Poortinga, G.4
  • 39
    • 0035395939 scopus 로고    scopus 로고
    • Control of cell division by a retinoblastoma protein homolog in Chlamydomonas
    • Umen JG, Goodenough UW, (2001) Control of cell division by a retinoblastoma protein homolog in Chlamydomonas. Genes Dev 15: 1652-1661.
    • (2001) Genes Dev , vol.15 , pp. 1652-1661
    • Umen, J.G.1    Goodenough, U.W.2
  • 40
    • 0035904396 scopus 로고    scopus 로고
    • A Streptomyces rimosus aphVIII gene coding for a new type phosphotransferase provides stable antibiotic resistance to Chlamydomonas reinhardtii
    • Sizova I, Fuhrmann M, Hegemann P, (2001) A Streptomyces rimosus aphVIII gene coding for a new type phosphotransferase provides stable antibiotic resistance to Chlamydomonas reinhardtii. Gene 277: 221-229.
    • (2001) Gene , vol.277 , pp. 221-229
    • Sizova, I.1    Fuhrmann, M.2    Hegemann, P.3
  • 41
    • 19044380672 scopus 로고    scopus 로고
    • Functional genomics of eukaryotic photosynthesis using insertional mutagenesis of Chlamydomonas reinhardtii
    • Dent RM, Haglund CM, Chin BL, Kobayashi MC, Niyogi KK, (2005) Functional genomics of eukaryotic photosynthesis using insertional mutagenesis of Chlamydomonas reinhardtii. Plant Physiol 137: 545-556.
    • (2005) Plant Physiol , vol.137 , pp. 545-556
    • Dent, R.M.1    Haglund, C.M.2    Chin, B.L.3    Kobayashi, M.C.4    Niyogi, K.K.5
  • 42
    • 0029360727 scopus 로고
    • Efficient isolation and mapping of Arabidopsis thaliana T-DNA insert junctions by thermal asymmetric interlaced PCR
    • Liu YG, Mitsukawa N, Oosumi T, Whittier RF, (1995) Efficient isolation and mapping of Arabidopsis thaliana T-DNA insert junctions by thermal asymmetric interlaced PCR. Plant J 8: 457-463.
    • (1995) Plant J , vol.8 , pp. 457-463
    • Liu, Y.G.1    Mitsukawa, N.2    Oosumi, T.3    Whittier, R.F.4
  • 43
    • 0024507215 scopus 로고
    • Construction of mutant and chimeric genes using the polymerase chain reaction
    • Vallette F, Mege E, Reiss A, Adesnik M, (1989) Construction of mutant and chimeric genes using the polymerase chain reaction. Nucleic Acids Res 17: 723-733.
    • (1989) Nucleic Acids Res , vol.17 , pp. 723-733
    • Vallette, F.1    Mege, E.2    Reiss, A.3    Adesnik, M.4
  • 44
    • 33744521045 scopus 로고    scopus 로고
    • Two flagellar genes, AGG2 and AGG3, mediate orientation to light in Chlamydomonas
    • Iomini C, Li L, Mo W, Dutcher SK, Piperno G, (2006) Two flagellar genes, AGG2 and AGG3, mediate orientation to light in Chlamydomonas. Curr Biol 16: 1147-1153.
    • (2006) Curr Biol , vol.16 , pp. 1147-1153
    • Iomini, C.1    Li, L.2    Mo, W.3    Dutcher, S.K.4    Piperno, G.5
  • 45
    • 0031893765 scopus 로고    scopus 로고
    • High-efficiency transformation of Chlamydomonas reinhardtii by electroporation
    • Shimogawara K, Fujiwara S, Grossman A, Usuda H, (1998) High-efficiency transformation of Chlamydomonas reinhardtii by electroporation. Genetics 148: 1821-1828.
    • (1998) Genetics , vol.148 , pp. 1821-1828
    • Shimogawara, K.1    Fujiwara, S.2    Grossman, A.3    Usuda, H.4
  • 46
    • 33847212762 scopus 로고    scopus 로고
    • Understanding microtubule organizing centers by comparing mutant and wild-type structures with electron tomography
    • O'Toole ET, Giddings TH Jr, Dutcher SK, (2007) Understanding microtubule organizing centers by comparing mutant and wild-type structures with electron tomography. Methods Cell Biol 79: 125-143.
    • (2007) Methods Cell Biol , vol.79 , pp. 125-143
    • O'Toole, E.T.1    Giddings Jr., T.H.2    Dutcher, S.K.3
  • 47
    • 0038159661 scopus 로고    scopus 로고
    • Three-dimensional organization of basal bodies from wild-type and delta-tubulin deletion strains of Chlamydomonas reinhardtii
    • O'Toole ET, Giddings TH, McIntosh JR, Dutcher SK, (2003) Three-dimensional organization of basal bodies from wild-type and delta-tubulin deletion strains of Chlamydomonas reinhardtii. Mol Biol Cell 14: 2999-3012.
    • (2003) Mol Biol Cell , vol.14 , pp. 2999-3012
    • O'Toole, E.T.1    Giddings, T.H.2    McIntosh, J.R.3    Dutcher, S.K.4
  • 48
    • 0142025252 scopus 로고    scopus 로고
    • Cryoimmobilization and three-dimensional visualization of C. elegans ultrastructure
    • Muller-Reichert T, Hohenberg H, O'Toole ET, McDonald K, (2003) Cryoimmobilization and three-dimensional visualization of C. elegans ultrastructure. J Microsc 212: 71-80.
    • (2003) J Microsc , vol.212 , pp. 71-80
    • Muller-Reichert, T.1    Hohenberg, H.2    O'Toole, E.T.3    McDonald, K.4
  • 49
    • 0031422417 scopus 로고    scopus 로고
    • Dual-axis tomography: an approach with alignment methods that preserve resolution
    • Mastronarde DN, (1997) Dual-axis tomography: an approach with alignment methods that preserve resolution. J Struct Biol 120: 343-352.
    • (1997) J Struct Biol , vol.120 , pp. 343-352
    • Mastronarde, D.N.1
  • 50
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer JR, Mastronarde DN, McIntosh JR, (1996) Computer visualization of three-dimensional image data using IMOD. J Struct Biol 116: 71-76.
    • (1996) J Struct Biol , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 51
    • 0017394208 scopus 로고
    • Non-specific stimulation of the autolytic system in gametes from Chlamydomonas reinhardii
    • Claes H, (1977) Non-specific stimulation of the autolytic system in gametes from Chlamydomonas reinhardii. Exp Cell Res 108: 221-229.
    • (1977) Exp Cell Res , vol.108 , pp. 221-229
    • Claes, H.1
  • 52
    • 0029187094 scopus 로고
    • Purification of basal bodies and basal body complexes from Chlamydomonas reinhardtii
    • Dutcher SK, (1995) Purification of basal bodies and basal body complexes from Chlamydomonas reinhardtii. Methods Cell Biol 47: 323-334.
    • (1995) Methods Cell Biol , vol.47 , pp. 323-334
    • Dutcher, S.K.1
  • 53
    • 0022379356 scopus 로고
    • A nucleus-basal body connector in Chlamydomonas reinhardtii that may function in basal body localization or segregation
    • Wright RL, Salisbury J, Jarvik JW, (1985) A nucleus-basal body connector in Chlamydomonas reinhardtii that may function in basal body localization or segregation. J Cell Biol 101: 1903-1912.
    • (1985) J Cell Biol , vol.101 , pp. 1903-1912
    • Wright, R.L.1    Salisbury, J.2    Jarvik, J.W.3
  • 54
    • 0001408674 scopus 로고
    • Temperature-Sensitive, Assembly-Defective Flagella Mutants of CHLAMYDOMONAS REINHARDTII
    • Adams GM, Huang B, Luck DJ, (1982) Temperature-Sensitive, Assembly-Defective Flagella Mutants of CHLAMYDOMONAS REINHARDTII. Genetics 100: 579-586.
    • (1982) Genetics , vol.100 , pp. 579-586
    • Adams, G.M.1    Huang, B.2    Luck, D.J.3
  • 55
    • 0021334462 scopus 로고
    • Genetic dissection of the central pair microtubules of the flagella of Chlamydomonas reinhardtii
    • Dutcher SK, Huang B, Luck DJ, (1984) Genetic dissection of the central pair microtubules of the flagella of Chlamydomonas reinhardtii. J Cell Biol 98: 229-236.
    • (1984) J Cell Biol , vol.98 , pp. 229-236
    • Dutcher, S.K.1    Huang, B.2    Luck, D.J.3
  • 56
    • 4143093686 scopus 로고    scopus 로고
    • PF15p is the chlamydomonas homologue of the Katanin p80 subunit and is required for assembly of flagellar central microtubules
    • Dymek EE, Lefebvre PA, Smith EF, (2004) PF15p is the chlamydomonas homologue of the Katanin p80 subunit and is required for assembly of flagellar central microtubules. Eukaryot Cell 3: 870-879.
    • (2004) Eukaryot Cell , vol.3 , pp. 870-879
    • Dymek, E.E.1    Lefebvre, P.A.2    Smith, E.F.3
  • 57
    • 0035995284 scopus 로고    scopus 로고
    • Functional diversity of axonemal dyneins as studied in Chlamydomonas mutants
    • Kamiya R, (2002) Functional diversity of axonemal dyneins as studied in Chlamydomonas mutants. Int Rev Cytol 219: 115-155.
    • (2002) Int Rev Cytol , vol.219 , pp. 115-155
    • Kamiya, R.1
  • 58
  • 59
    • 0035899903 scopus 로고    scopus 로고
    • The bld1 mutation identifies the Chlamydomonas osm-6 homolog as a gene required for flagellar assembly
    • Brazelton WJ, Amundsen CD, Silflow CD, Lefebvre PA, (2001) The bld1 mutation identifies the Chlamydomonas osm-6 homolog as a gene required for flagellar assembly. Curr Biol 11: 1591-1594.
    • (2001) Curr Biol , vol.11 , pp. 1591-1594
    • Brazelton, W.J.1    Amundsen, C.D.2    Silflow, C.D.3    Lefebvre, P.A.4
  • 60
    • 84864340750 scopus 로고    scopus 로고
    • Whole-Genome Sequencing to Identify Mutants and Polymorphisms in Chlamydomonas reinhardtii
    • Dutcher SK, Li L, Lin H, Meyer L, Giddings TH Jr, et al. (2012) Whole-Genome Sequencing to Identify Mutants and Polymorphisms in Chlamydomonas reinhardtii. G3 (Bethesda) 2: 15-22.
    • (2012) G3 (Bethesda) , vol.2 , pp. 15-22
    • Dutcher, S.K.1    Li, L.2    Lin, H.3    Meyer, L.4    Giddings Jr., T.H.5
  • 61
    • 0035795413 scopus 로고    scopus 로고
    • Protein particles in Chlamydomonas flagella undergo a transport cycle consisting of four phases
    • Iomini C, Babaev-Khaimov V, Sassaroli M, Piperno G, (2001) Protein particles in Chlamydomonas flagella undergo a transport cycle consisting of four phases. J Cell Biol 153: 13-24.
    • (2001) J Cell Biol , vol.153 , pp. 13-24
    • Iomini, C.1    Babaev-Khaimov, V.2    Sassaroli, M.3    Piperno, G.4
  • 62
    • 72449151681 scopus 로고    scopus 로고
    • Retrograde intraflagellar transport mutants identify complex A proteins with multiple genetic interactions in Chlamydomonas reinhardtii
    • Iomini C, Li L, Esparza JM, Dutcher SK, (2009) Retrograde intraflagellar transport mutants identify complex A proteins with multiple genetic interactions in Chlamydomonas reinhardtii. Genetics 183: 885-896.
    • (2009) Genetics , vol.183 , pp. 885-896
    • Iomini, C.1    Li, L.2    Esparza, J.M.3    Dutcher, S.K.4
  • 63
    • 0029199751 scopus 로고
    • High-resolution imaging of flagella
    • Kozminski KG, (1995) High-resolution imaging of flagella. Methods Cell Biol 47: 263-271.
    • (1995) Methods Cell Biol , vol.47 , pp. 263-271
    • Kozminski, K.G.1
  • 65
    • 0028241107 scopus 로고
    • The Chlamydomonas FLA10 gene encodes a novel kinesin-homologous protein
    • Walther Z, Vashishtha M, Hall JL, (1994) The Chlamydomonas FLA10 gene encodes a novel kinesin-homologous protein. J Cell Biol 126: 175-188.
    • (1994) J Cell Biol , vol.126 , pp. 175-188
    • Walther, Z.1    Vashishtha, M.2    Hall, J.L.3
  • 66
    • 79955009072 scopus 로고    scopus 로고
    • Novel asymmetrically localizing components of human centrosomes identified by complementary proteomics methods
    • Jakobsen L, Vanselow K, Skogs M, Toyoda Y, Lundberg E, et al. (2011) Novel asymmetrically localizing components of human centrosomes identified by complementary proteomics methods. EMBO J 30: 1520-1535.
    • (2011) EMBO J , vol.30 , pp. 1520-1535
    • Jakobsen, L.1    Vanselow, K.2    Skogs, M.3    Toyoda, Y.4    Lundberg, E.5
  • 67
    • 0024025965 scopus 로고
    • Extensive restriction fragment length polymorphisms in a new isolate of Chlamydomonas reinhardtii
    • Gross CH, Ranum LP, Lefebvre PA, (1988) Extensive restriction fragment length polymorphisms in a new isolate of Chlamydomonas reinhardtii. Curr Genet 13: 503-508.
    • (1988) Curr Genet , vol.13 , pp. 503-508
    • Gross, C.H.1    Ranum, L.P.2    Lefebvre, P.A.3
  • 70
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales E, Wolf SG, Downing KH, (1998) Structure of the alpha beta tubulin dimer by electron crystallography. Nature 391: 199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 71
    • 0024116724 scopus 로고
    • The lost neuromotor apparatus of Chlamydomonas: rediscovered
    • Salisbury JL, (1988) The lost neuromotor apparatus of Chlamydomonas: rediscovered. J Protozool 35: 574-577.
    • (1988) J Protozool , vol.35 , pp. 574-577
    • Salisbury, J.L.1
  • 73
    • 0022539766 scopus 로고
    • Cytoplasmic microtubules containing acetylated alpha-tubulin in Chlamydomonas reinhardtii: spatial arrangement and properties
    • LeDizet M, Piperno G, (1986) Cytoplasmic microtubules containing acetylated alpha-tubulin in Chlamydomonas reinhardtii: spatial arrangement and properties. J Cell Biol 103: 13-22.
    • (1986) J Cell Biol , vol.103 , pp. 13-22
    • LeDizet, M.1    Piperno, G.2
  • 74
    • 3242885644 scopus 로고    scopus 로고
    • The ultrastructure of the Chlamydomonas reinhardtii basal apparatus: identification of an early marker of radial asymmetry inherent in the basal body
    • Geimer S, Melkonian M, (2004) The ultrastructure of the Chlamydomonas reinhardtii basal apparatus: identification of an early marker of radial asymmetry inherent in the basal body. J Cell Sci 117: 2663-2674.
    • (2004) J Cell Sci , vol.117 , pp. 2663-2674
    • Geimer, S.1    Melkonian, M.2
  • 75
    • 0024843525 scopus 로고
    • Nucleus-basal body connector in Chlamydomonas: evidence for a role in basal body segregation and against essential roles in mitosis or in determining cell polarity
    • Wright RL, Adler SA, Spanier JG, Jarvik JW, (1989) Nucleus-basal body connector in Chlamydomonas: evidence for a role in basal body segregation and against essential roles in mitosis or in determining cell polarity. Cell Motil Cytoskeleton 14: 516-526.
    • (1989) Cell Motil Cytoskeleton , vol.14 , pp. 516-526
    • Wright, R.L.1    Adler, S.A.2    Spanier, J.G.3    Jarvik, J.W.4
  • 76
    • 0028826392 scopus 로고
    • Loss of spatial control of the mitotic spindle apparatus in a Chlamydomonas reinhardtii mutant strain lacking basal bodies
    • Ehler LL, Holmes JA, Dutcher SK, (1995) Loss of spatial control of the mitotic spindle apparatus in a Chlamydomonas reinhardtii mutant strain lacking basal bodies. Genetics 141: 945-960.
    • (1995) Genetics , vol.141 , pp. 945-960
    • Ehler, L.L.1    Holmes, J.A.2    Dutcher, S.K.3
  • 77
    • 0034763779 scopus 로고    scopus 로고
    • Basal body replication in green algae-when and where does it start?
    • Lechtreck KF, Bornens M, (2001) Basal body replication in green algae-when and where does it start? Eur J Cell Biol 80: 631-641.
    • (2001) Eur J Cell Biol , vol.80 , pp. 631-641
    • Lechtreck, K.F.1    Bornens, M.2
  • 78
    • 0014323355 scopus 로고
    • Fine structure of cell division in Chlamydomonas reinhardi. Basal bodies and microtubules
    • Johnson UG, Porter KR, (1968) Fine structure of cell division in Chlamydomonas reinhardi. Basal bodies and microtubules. J Cell Biol 38: 403-425.
    • (1968) J Cell Biol , vol.38 , pp. 403-425
    • Johnson, U.G.1    Porter, K.R.2
  • 79
    • 0014094209 scopus 로고
    • Flagellar motion and fine structure of the flagellar apparatus in Chlamydomonas
    • Ringo DL, (1967) Flagellar motion and fine structure of the flagellar apparatus in Chlamydomonas. J Cell Biol 33: 543-571.
    • (1967) J Cell Biol , vol.33 , pp. 543-571
    • Ringo, D.L.1
  • 80
    • 0038159661 scopus 로고    scopus 로고
    • Three-dimensional organization of basal bodies from wild-type and d-tubulin deletion strains of Chlamydomonas reinhardtii
    • O'Toole E, Giddings T, McIntosh J, Dutcher S (2003) Three-dimensional organization of basal bodies from wild-type and d-tubulin deletion strains of Chlamydomonas reinhardtii. Mol Biol Cell.
    • (2003) Mol Biol Cell
    • O'Toole, E.1    Giddings, T.2    McIntosh, J.3    Dutcher, S.4
  • 81
    • 0029035184 scopus 로고
    • Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila
    • Gaertig J, Cruz MA, Bowen J, Gu L, Pennock DG, et al. (1995) Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila. J Cell Biol 129: 1301-1310.
    • (1995) J Cell Biol , vol.129 , pp. 1301-1310
    • Gaertig, J.1    Cruz, M.A.2    Bowen, J.3    Gu, L.4    Pennock, D.G.5
  • 83
    • 63049095708 scopus 로고    scopus 로고
    • Katanin knockdown supports a role for microtubule severing in release of basal bodies before mitosis in Chlamydomonas
    • Rasi MQ, Parker JD, Feldman JL, Marshall WF, Quarmby LM, (2009) Katanin knockdown supports a role for microtubule severing in release of basal bodies before mitosis in Chlamydomonas. Mol Biol Cell 20: 379-388.
    • (2009) Mol Biol Cell , vol.20 , pp. 379-388
    • Rasi, M.Q.1    Parker, J.D.2    Feldman, J.L.3    Marshall, W.F.4    Quarmby, L.M.5
  • 84
    • 84869138052 scopus 로고    scopus 로고
    • PF19 encodes the p60 catalytic subunit of katanin and is required for assembly of the flagellar central apparatus in Chlamydomonas
    • Dymek EE, Smith EF, (2012) PF19 encodes the p60 catalytic subunit of katanin and is required for assembly of the flagellar central apparatus in Chlamydomonas. J Cell Sci 125: 3357-3366.
    • (2012) J Cell Sci , vol.125 , pp. 3357-3366
    • Dymek, E.E.1    Smith, E.F.2
  • 86
    • 76249128028 scopus 로고    scopus 로고
    • Nek4 status differentially alters sensitivity to distinct microtubule poisons
    • Doles J, Hemann MT, (2010) Nek4 status differentially alters sensitivity to distinct microtubule poisons. Cancer Res 70: 1033-1041.
    • (2010) Cancer Res , vol.70 , pp. 1033-1041
    • Doles, J.1    Hemann, M.T.2
  • 87
    • 84859006925 scopus 로고    scopus 로고
    • Identification of a novel role of Septin 10 in paclitaxel-resistance in cancers through a functional genomics screen
    • Xu M, Takanashi M, Oikawa K, Nishi H, Isaka K, et al. (2012) Identification of a novel role of Septin 10 in paclitaxel-resistance in cancers through a functional genomics screen. Cancer Sci 103: 821-827.
    • (2012) Cancer Sci , vol.103 , pp. 821-827
    • Xu, M.1    Takanashi, M.2    Oikawa, K.3    Nishi, H.4    Isaka, K.5
  • 88
    • 26244468767 scopus 로고    scopus 로고
    • Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4
    • Kremer BE, Haystead T, Macara IG, (2005) Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4. Mol Biol Cell 16: 4648-4659.
    • (2005) Mol Biol Cell , vol.16 , pp. 4648-4659
    • Kremer, B.E.1    Haystead, T.2    Macara, I.G.3
  • 89
    • 84862760137 scopus 로고    scopus 로고
    • Whole-genome studies identify solute carrier transporters in cellular susceptibility to paclitaxel
    • Njiaju UO, Gamazon ER, Gorsic LK, Delaney SM, Wheeler HE, et al. (2012) Whole-genome studies identify solute carrier transporters in cellular susceptibility to paclitaxel. Pharmacogenet Genomics 22: 498-507.
    • (2012) Pharmacogenet Genomics , vol.22 , pp. 498-507
    • Njiaju, U.O.1    Gamazon, E.R.2    Gorsic, L.K.3    Delaney, S.M.4    Wheeler, H.E.5
  • 90
    • 84867858942 scopus 로고    scopus 로고
    • Random Mutagenesis of beta-Tubulin Defines a Set of Dispersed Mutations That Confer Paclitaxel Resistance
    • Yin S, Zeng C, Hari M, Cabral F, (2012) Random Mutagenesis of beta-Tubulin Defines a Set of Dispersed Mutations That Confer Paclitaxel Resistance. Pharm Res 29: 2994-3006.
    • (2012) Pharm Res , vol.29 , pp. 2994-3006
    • Yin, S.1    Zeng, C.2    Hari, M.3    Cabral, F.4


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