메뉴 건너뛰기




Volumn 313, Issue 1, 2008, Pages 320-334

Efficient chaperone-mediated tubulin biogenesis is essential for cell division and cell migration in C. elegans

Author keywords

Actin; CCT; Distal tip cell migration; Embryonic cell division; Microtubule dynamics; Molecular chaperone; Prefoldin; Protein biogenesis; Tubulin; Tubulin homeostasis

Indexed keywords

ALPHA TUBULIN; CHAPERONE; TUBULIN;

EID: 37549021153     PISSN: 00121606     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ydbio.2007.10.022     Document Type: Article
Times cited : (63)

References (81)
  • 1
    • 0142104970 scopus 로고    scopus 로고
    • Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl syndrome
    • Ansley, et al. Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl syndrome. Nature 425 (2003) 628-633
    • (2003) Nature , vol.425 , pp. 628-633
    • Ansley1
  • 2
    • 17244381397 scopus 로고    scopus 로고
    • Identification of a novel tubulin-destabilizing protein related to the chaperone cofactor E
    • Bartolini, et al. Identification of a novel tubulin-destabilizing protein related to the chaperone cofactor E. J. Cell. Sci. 118 (2005) 1197-1207
    • (2005) J. Cell. Sci. , vol.118 , pp. 1197-1207
    • Bartolini1
  • 3
    • 0035735949 scopus 로고    scopus 로고
    • Cytokinesis in the C. elegans embryo: regulating contractile forces and a late role for the central spindle
    • Bowerman B. Cytokinesis in the C. elegans embryo: regulating contractile forces and a late role for the central spindle. Cell Struct. Funct. 26 (2001) 603-607
    • (2001) Cell Struct. Funct. , vol.26 , pp. 603-607
    • Bowerman, B.1
  • 4
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner S. The genetics of Caenorhabditis elegans. Genetics 77 (1974) 71-94
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 5
    • 23644457501 scopus 로고    scopus 로고
    • A cytokinesis furrow is positioned by two consecutive signals
    • Bringmann H., and Hyman A.A. A cytokinesis furrow is positioned by two consecutive signals. Nature 436 (2005) 731-734
    • (2005) Nature , vol.436 , pp. 731-734
    • Bringmann, H.1    Hyman, A.A.2
  • 6
    • 0041669463 scopus 로고    scopus 로고
    • The CCT chaperonin promotes activation of the anaphase-promoting complex through the generation of functional Cdc20
    • Camasses, et al. The CCT chaperonin promotes activation of the anaphase-promoting complex through the generation of functional Cdc20. Mol. Cell 12 (2003) 87-100
    • (2003) Mol. Cell , vol.12 , pp. 87-100
    • Camasses1
  • 7
    • 13444254287 scopus 로고    scopus 로고
    • WormBase: a comprehensive data resource for Caenorhabditis biology and genomics
    • Chen, et al. WormBase: a comprehensive data resource for Caenorhabditis biology and genomics. Nucleic Acids Res. 33 (2005) D383-D389
    • (2005) Nucleic Acids Res. , vol.33
    • Chen1
  • 8
    • 10644253531 scopus 로고    scopus 로고
    • Centriole assembly requires both centriolar and pericentriolar matrix proteins
    • Dammermann, et al. Centriole assembly requires both centriolar and pericentriolar matrix proteins. Dev. Cell 7 (2004) 815-829
    • (2004) Dev. Cell , vol.7 , pp. 815-829
    • Dammermann1
  • 9
    • 0347712936 scopus 로고    scopus 로고
    • Maternally expressed and partially redundant β-tubulins in Caenorhabditis elegans are autoregulated
    • Ellis, et al. Maternally expressed and partially redundant β-tubulins in Caenorhabditis elegans are autoregulated. J. Cell. Sci. 117 (2003) 457-464
    • (2003) J. Cell. Sci. , vol.117 , pp. 457-464
    • Ellis1
  • 10
    • 0032545933 scopus 로고    scopus 로고
    • Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
    • Fire, et al. Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature 391 (1998) 806-811
    • (1998) Nature , vol.391 , pp. 806-811
    • Fire1
  • 11
    • 0034676457 scopus 로고    scopus 로고
    • Functional genomic analysis of C. elegans chromosome I by systematic RNA interference
    • Fraser, et al. Functional genomic analysis of C. elegans chromosome I by systematic RNA interference. Nature 408 (2000) 325-330
    • (2000) Nature , vol.408 , pp. 325-330
    • Fraser1
  • 12
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes β-actin folding
    • Gao, et al. A cytoplasmic chaperonin that catalyzes β-actin folding. Cell 69 (1992) 1043-1050
    • (1992) Cell , vol.69 , pp. 1043-1050
    • Gao1
  • 13
    • 0024431507 scopus 로고
    • Autoregulatory control of β-tubulin mRNA stability in linked to translation elongation
    • Gay. Autoregulatory control of β-tubulin mRNA stability in linked to translation elongation. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 5763-5767
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 5763-5767
    • Gay1
  • 14
    • 0032481303 scopus 로고    scopus 로고
    • A novel protein complex promoting formation of functional α- and γ-tubulin
    • Geissler, et al. A novel protein complex promoting formation of functional α- and γ-tubulin. EMBO J. 17 (1998) 952-966
    • (1998) EMBO J. , vol.17 , pp. 952-966
    • Geissler1
  • 15
    • 33745246007 scopus 로고    scopus 로고
    • Substantial CCT activity is required for cell cycle progression and cytoskeletal organization in mammalian cells
    • Grantham, et al. Substantial CCT activity is required for cell cycle progression and cytoskeletal organization in mammalian cells. Exp. Cell Res. 312 (2006) 2309-2324
    • (2006) Exp. Cell Res. , vol.312 , pp. 2309-2324
    • Grantham1
  • 16
    • 0034676448 scopus 로고    scopus 로고
    • Functional genomic analysis of cell division in C. elegans using RNAi of genes on chromosome III
    • Gönczy, et al. Functional genomic analysis of cell division in C. elegans using RNAi of genes on chromosome III. Nature 408 (2000) 331-336
    • (2000) Nature , vol.408 , pp. 331-336
    • Gönczy1
  • 17
    • 0242497664 scopus 로고    scopus 로고
    • Control of nutrient-sensitive transcription programs by the unconventional prefoldin URI
    • Gstaiger, et al. Control of nutrient-sensitive transcription programs by the unconventional prefoldin URI. Science 302 (2003) 1208-1212
    • (2003) Science , vol.302 , pp. 1208-1212
    • Gstaiger1
  • 18
    • 1642265093 scopus 로고    scopus 로고
    • Cortical control of microtubule stability and polarization
    • Gundersen, et al. Cortical control of microtubule stability and polarization. Curr. Opin. Cell Biol. 16 (2004) 106-112
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 106-112
    • Gundersen1
  • 19
    • 0029836212 scopus 로고    scopus 로고
    • A non-muscle myosin required for embryonic polarity in Caenorhabditis elegans
    • Guo S., and Kemphues K.J. A non-muscle myosin required for embryonic polarity in Caenorhabditis elegans. Nature 382 (1996) 455-458
    • (1996) Nature , vol.382 , pp. 455-458
    • Guo, S.1    Kemphues, K.J.2
  • 20
    • 0037071539 scopus 로고    scopus 로고
    • The kinetically dominant assembly pathway for centrosomal asters in Caenorhabditis elegans is gamma-tubulin dependent
    • Hannak, et al. The kinetically dominant assembly pathway for centrosomal asters in Caenorhabditis elegans is gamma-tubulin dependent. J. Cell Biol. 157 (2002) 591-602
    • (2002) J. Cell Biol. , vol.157 , pp. 591-602
    • Hannak1
  • 21
    • 0345518025 scopus 로고    scopus 로고
    • Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins
    • Hansen, et al. Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins. J. Cell Biol. 145 (1999) 265-277
    • (1999) J. Cell Biol. , vol.145 , pp. 265-277
    • Hansen1
  • 22
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: from nascent chain to folded protein
    • Hartl F.U., and Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295 (2002) 1852-1859
    • (2002) Science , vol.295 , pp. 1852-1859
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 23
    • 0037442714 scopus 로고    scopus 로고
    • Human MutS homolog MSH4 physically interacts with von Hippel-Lindau tumor suppressor-binding protein 1
    • Her, et al. Human MutS homolog MSH4 physically interacts with von Hippel-Lindau tumor suppressor-binding protein 1. Cancer Res. 63 (2003) 865-872
    • (2003) Cancer Res. , vol.63 , pp. 865-872
    • Her1
  • 24
    • 0034721722 scopus 로고    scopus 로고
    • Genomic analysis of gene expression in C. elegans
    • Hill, et al. Genomic analysis of gene expression in C. elegans. Science 290 (2000) 809-812
    • (2000) Science , vol.290 , pp. 809-812
    • Hill1
  • 25
    • 0027154850 scopus 로고
    • Cortical and cytoplasmic flow polarity in early embryonic cells of Caenorhabditis elegans
    • Hird S.N., and White J.G. Cortical and cytoplasmic flow polarity in early embryonic cells of Caenorhabditis elegans. J. Cell Biol. 121 (1993) 1343-1355
    • (1993) J. Cell Biol. , vol.121 , pp. 1343-1355
    • Hird, S.N.1    White, J.G.2
  • 26
    • 0023581761 scopus 로고
    • Determination of cell division axes in the early embryogenesis of Caenorhabditis elegans
    • Hyman A.A., and White J.G. Determination of cell division axes in the early embryogenesis of Caenorhabditis elegans. J. Cell Biol. 105 (1987) 2123-2135
    • (1987) J. Cell Biol. , vol.105 , pp. 2123-2135
    • Hyman, A.A.1    White, J.G.2
  • 27
    • 18244430352 scopus 로고    scopus 로고
    • CYK-4: a Rho family gtpase activating protein (GAP) required for central spindle formation and cytokinesis
    • Jantsch-Plunger. CYK-4: a Rho family gtpase activating protein (GAP) required for central spindle formation and cytokinesis. J. Cell Biol. 149 (2000) 1391-1404
    • (2000) J. Cell Biol. , vol.149 , pp. 1391-1404
    • Jantsch-Plunger1
  • 28
    • 0037448540 scopus 로고    scopus 로고
    • Systematic functional analysis of the Caenorhabditis elegans genome using RNAi
    • Kamath, et al. Systematic functional analysis of the Caenorhabditis elegans genome using RNAi. Nature 421 (2003) 231-237
    • (2003) Nature , vol.421 , pp. 231-237
    • Kamath1
  • 29
    • 0030903160 scopus 로고    scopus 로고
    • Distinct requirements for somatic and germline expression of a generally expressed Caenorhabditis elegans gene
    • Kelly, et al. Distinct requirements for somatic and germline expression of a generally expressed Caenorhabditis elegans gene. Genetics 146 (1997) 227-238
    • (1997) Genetics , vol.146 , pp. 227-238
    • Kelly1
  • 30
    • 0037459108 scopus 로고    scopus 로고
    • SAS-4 is a centriolar protein that controls centrosome size
    • Kirkham, et al. SAS-4 is a centriolar protein that controls centrosome size. Cell 112 (2003) 575-587
    • (2003) Cell , vol.112 , pp. 575-587
    • Kirkham1
  • 31
    • 0037799920 scopus 로고    scopus 로고
    • PAR proteins regulate microtubule dynamics at the cell cortex in C. elegans
    • Labbe, et al. PAR proteins regulate microtubule dynamics at the cell cortex in C. elegans. Curr. Biol. 13 (2003) 707-714
    • (2003) Curr. Biol. , vol.13 , pp. 707-714
    • Labbe1
  • 32
    • 0242286609 scopus 로고    scopus 로고
    • A novel step in β-tubulin folding is important for heterodimer formation in Saccharomyces cerevisiae
    • Lacefield S., and Solomon F. A novel step in β-tubulin folding is important for heterodimer formation in Saccharomyces cerevisiae. Genetics 165 (2003) 531-541
    • (2003) Genetics , vol.165 , pp. 531-541
    • Lacefield, S.1    Solomon, F.2
  • 33
    • 33745368757 scopus 로고    scopus 로고
    • Consequences of defective tubulin folding on heterodimer levels, mitosis and spindle morphology in Saccharomyces cerevisiae
    • Lacefield, et al. Consequences of defective tubulin folding on heterodimer levels, mitosis and spindle morphology in Saccharomyces cerevisiae. Genetics 173 (2006) 635-646
    • (2006) Genetics , vol.173 , pp. 635-646
    • Lacefield1
  • 34
    • 0042921209 scopus 로고    scopus 로고
    • TAC-1, a regulator of microtubule length in the C. elegans embryo
    • Le Bot, et al. TAC-1, a regulator of microtubule length in the C. elegans embryo. Curr. Biol. 13 (2003) 1499-1505
    • (2003) Curr. Biol. , vol.13 , pp. 1499-1505
    • Le Bot1
  • 35
    • 0031590734 scopus 로고    scopus 로고
    • Subunit characterization of the Caenorhabditis elegans chaperonin containing TCP-1 and expression pattern of the gene encoding CCT-1
    • Leroux M.R., and Candido P.M. Subunit characterization of the Caenorhabditis elegans chaperonin containing TCP-1 and expression pattern of the gene encoding CCT-1. Biochem. Biophys. Res. Commun. 241 (1997) 687-692
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 687-692
    • Leroux, M.R.1    Candido, P.M.2
  • 36
    • 0034611628 scopus 로고    scopus 로고
    • Protein folding: versatility of the cytosolic chaperonin TRiC/CCT
    • Leroux M.R., and Hartl F.U. Protein folding: versatility of the cytosolic chaperonin TRiC/CCT. Curr. Biol. 10 (2000) R260-R264
    • (2000) Curr. Biol. , vol.10
    • Leroux, M.R.1    Hartl, F.U.2
  • 37
    • 0345201713 scopus 로고    scopus 로고
    • MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin
    • Leroux, et al. MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin. EMBO J. 18 (1999) 6730-6743
    • (1999) EMBO J. , vol.18 , pp. 6730-6743
    • Leroux1
  • 38
    • 20344385029 scopus 로고    scopus 로고
    • CCT chaperonin complex is required for the biogenesis of functional Plk1
    • Liu, et al. CCT chaperonin complex is required for the biogenesis of functional Plk1. Mol. Cell. Biol. 25 (2005) 4993-5010
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4993-5010
    • Liu1
  • 39
    • 0034669110 scopus 로고    scopus 로고
    • Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations
    • Llorca, et al. Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations. EMBO J. 19 (2000) 5971-5979
    • (2000) EMBO J. , vol.19 , pp. 5971-5979
    • Llorca1
  • 40
    • 18744404214 scopus 로고    scopus 로고
    • Review: postchaperonin tubulin folding cofactors and their role in microtubule dynamics
    • Lopez-Fanarraga, et al. Review: postchaperonin tubulin folding cofactors and their role in microtubule dynamics. J. Struct. Biol. 135 (2001) 219-229
    • (2001) J. Struct. Biol. , vol.135 , pp. 219-229
    • Lopez-Fanarraga1
  • 41
    • 1842585903 scopus 로고    scopus 로고
    • Molecular clamp mechanism of substrate binding by hydrophobic coiled coil resides of the archaeal chaperone prefoldin
    • Lundin, et al. Molecular clamp mechanism of substrate binding by hydrophobic coiled coil resides of the archaeal chaperone prefoldin. PNAS 101 (2004) 4367-4372
    • (2004) PNAS , vol.101 , pp. 4367-4372
    • Lundin1
  • 42
    • 0035128859 scopus 로고    scopus 로고
    • Large-scale analysis of gene function in Caenorhabditis elegans by high-throughput RNAi
    • Maeda, et al. Large-scale analysis of gene function in Caenorhabditis elegans by high-throughput RNAi. Curr. Biol. 11 (2001) 171-176
    • (2001) Curr. Biol. , vol.11 , pp. 171-176
    • Maeda1
  • 43
    • 0037011162 scopus 로고    scopus 로고
    • Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT
    • Martin-Benito, et al. Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT. EMBO J. 21 (2002) 6377-6386
    • (2002) EMBO J. , vol.21 , pp. 6377-6386
    • Martin-Benito1
  • 44
    • 33846238951 scopus 로고    scopus 로고
    • Divergent substrate-binding mechanisms reveal an evolutionary specialization of eukaryotic prefoldin compared to its archaeal counterpart
    • Martin-Benito, et al. Divergent substrate-binding mechanisms reveal an evolutionary specialization of eukaryotic prefoldin compared to its archaeal counterpart. Structure 15 (2007) 101-110
    • (2007) Structure , vol.15 , pp. 101-110
    • Martin-Benito1
  • 45
    • 3242683216 scopus 로고    scopus 로고
    • Gene expression profiling of cells, tissues, and developmental stages of the nematode C. elegans
    • McKay, et al. Gene expression profiling of cells, tissues, and developmental stages of the nematode C. elegans. Cold Spring Harbor Symp. Quant. Biol. 68 (2003) 159-169
    • (2003) Cold Spring Harbor Symp. Quant. Biol. , vol.68 , pp. 159-169
    • McKay1
  • 46
    • 0027293897 scopus 로고
    • Chaperonin-mediated folding of vertebrate actin-related protein and γ-tubulin
    • Melki, et al. Chaperonin-mediated folding of vertebrate actin-related protein and γ-tubulin. J. Cell Biol. 122 (1993) 1301-1310
    • (1993) J. Cell Biol. , vol.122 , pp. 1301-1310
    • Melki1
  • 47
    • 0037062473 scopus 로고    scopus 로고
    • Regulatory interaction of phosducin-like protein with the cytosolic chaperonin complex
    • McLaughlin, et al. Regulatory interaction of phosducin-like protein with the cytosolic chaperonin complex. PNAS 99 (2002) 7962-7967
    • (2002) PNAS , vol.99 , pp. 7962-7967
    • McLaughlin1
  • 48
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison T., and Kirschner M. Dynamic instability of microtubule growth. Nature 312 (1984) 237-242
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 49
    • 0032491539 scopus 로고    scopus 로고
    • MM-1, a novel c-Myc-associating protein that represses transcriptional activity of c-Myc
    • Mori, et al. MM-1, a novel c-Myc-associating protein that represses transcriptional activity of c-Myc. J. Biol. Chem. 273 (1998) 29794-29800
    • (1998) J. Biol. Chem. , vol.273 , pp. 29794-29800
    • Mori1
  • 50
    • 33645521057 scopus 로고    scopus 로고
    • Two phases of astral microtubule activity during cytokinesis in C. elegans embryos
    • Motegi, et al. Two phases of astral microtubule activity during cytokinesis in C. elegans embryos. Dev. Cell 10 (2006) 509-520
    • (2006) Dev. Cell , vol.10 , pp. 509-520
    • Motegi1
  • 51
    • 4544316472 scopus 로고    scopus 로고
    • Cortical flows powered by asymmetrical contraction transport PAR proteins to establish and maintain anterior-posterior polarity in the early C. elegans embryo
    • Munro, et al. Cortical flows powered by asymmetrical contraction transport PAR proteins to establish and maintain anterior-posterior polarity in the early C. elegans embryo. Dev. Cell 7 (2004) 413-424
    • (2004) Dev. Cell , vol.7 , pp. 413-424
    • Munro1
  • 52
    • 0034212508 scopus 로고    scopus 로고
    • The spd-2 gene is required for polarization of the anteroposterior axis and formation of the sperm asters in the Caenorhabditis elegans zygote
    • O'Connell, et al. The spd-2 gene is required for polarization of the anteroposterior axis and formation of the sperm asters in the Caenorhabditis elegans zygote. Dev. Biol. 222 (2000) 55-70
    • (2000) Dev. Biol. , vol.222 , pp. 55-70
    • O'Connell1
  • 53
    • 1542330120 scopus 로고    scopus 로고
    • An evolutionary conserved gene required for proper microtubule architecture in Caenorhabditis elegans
    • Ogawa, et al. An evolutionary conserved gene required for proper microtubule architecture in Caenorhabditis elegans. Genes Cells 9 (2004) 83-93
    • (2004) Genes Cells , vol.9 , pp. 83-93
    • Ogawa1
  • 54
    • 3843093899 scopus 로고    scopus 로고
    • Kinetics and binding sites for interaction of the prefoldin with a group II chaperonin
    • Okochi, et al. Kinetics and binding sites for interaction of the prefoldin with a group II chaperonin. J. Biol. Chem. 279 (2004) 31788-31795
    • (2004) J. Biol. Chem. , vol.279 , pp. 31788-31795
    • Okochi1
  • 55
    • 2542620764 scopus 로고    scopus 로고
    • Roles for two partially redundant α-tubulins during mitosis in early Caenorhabditis elegans embryos
    • Phillips, et al. Roles for two partially redundant α-tubulins during mitosis in early Caenorhabditis elegans embryos. Cell Motil. Cytoskelet. 58 (2004) 112-126
    • (2004) Cell Motil. Cytoskelet. , vol.58 , pp. 112-126
    • Phillips1
  • 56
    • 0346463132 scopus 로고    scopus 로고
    • The mbk-2 kinase is required for inactivation of MEI-1/katanin in the one-cell Caenorhabditis elegans embryo
    • Quintin, et al. The mbk-2 kinase is required for inactivation of MEI-1/katanin in the one-cell Caenorhabditis elegans embryo. EMBO Rep. 4 (2003) 1175-1181
    • (2003) EMBO Rep. , vol.4 , pp. 1175-1181
    • Quintin1
  • 57
    • 0028133187 scopus 로고
    • Mutations in the Caenorhabditis elegans b-tubulin gene mec-7: effects on microtubule assembly and stability and on tubulin autoregulation
    • Savage, et al. Mutations in the Caenorhabditis elegans b-tubulin gene mec-7: effects on microtubule assembly and stability and on tubulin autoregulation. J. Cell. Sci. 107 (1994) 2165-2175
    • (1994) J. Cell. Sci. , vol.107 , pp. 2165-2175
    • Savage1
  • 58
    • 0033521523 scopus 로고    scopus 로고
    • Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system
    • Siegers, et al. Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J. 18 (1999) 75-84
    • (1999) EMBO J. , vol.18 , pp. 75-84
    • Siegers1
  • 59
    • 0141613640 scopus 로고    scopus 로고
    • TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes
    • Siegers, et al. TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J. 22 (2003) 5230-5240
    • (2003) EMBO J. , vol.22 , pp. 5230-5240
    • Siegers1
  • 60
    • 0033680802 scopus 로고    scopus 로고
    • Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins
    • Siegert, et al. Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell 103 (2000) 621-632
    • (2000) Cell , vol.103 , pp. 621-632
    • Siegert1
  • 61
    • 1542298437 scopus 로고    scopus 로고
    • Genome-wide RNAi of C. elegans using the hypersensitive rrf-3 strain reveals novel gene functions
    • Simmer, et al. Genome-wide RNAi of C. elegans using the hypersensitive rrf-3 strain reveals novel gene functions. PLoS Biol. 1 (2003) 77-84
    • (2003) PLoS Biol. , vol.1 , pp. 77-84
    • Simmer1
  • 62
    • 1042278172 scopus 로고    scopus 로고
    • Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding
    • Simons, et al. Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding. J. Biol. Chem. 279 (2004) 4196-4203
    • (2004) J. Biol. Chem. , vol.279 , pp. 4196-4203
    • Simons1
  • 63
    • 4444366942 scopus 로고    scopus 로고
    • zyg-9 and cul-2 regulate progression through meiosis II and polarity establishment in C. elegans
    • Sonneville R., and Gönczy P. zyg-9 and cul-2 regulate progression through meiosis II and polarity establishment in C. elegans. Development 131 (2004) 3527-3543
    • (2004) Development , vol.131 , pp. 3527-3543
    • Sonneville, R.1    Gönczy, P.2
  • 64
    • 15844431376 scopus 로고    scopus 로고
    • Full-genome RNAi profiling of early embryogenesis in Caenorhabditis elegans
    • Sönnichsen, et al. Full-genome RNAi profiling of early embryogenesis in Caenorhabditis elegans. Nature 434 (2005) 462-469
    • (2005) Nature , vol.434 , pp. 462-469
    • Sönnichsen1
  • 65
    • 7444231693 scopus 로고    scopus 로고
    • Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets
    • Spiess, et al. Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. TRENDS Cell Biol. 14 (2004) 598-604
    • (2004) TRENDS Cell Biol. , vol.14 , pp. 598-604
    • Spiess1
  • 66
    • 22944457527 scopus 로고    scopus 로고
    • Identification and characterization of factors required for microtubule growth and nucleation in the early C. elegans embryo
    • Srayko, et al. Identification and characterization of factors required for microtubule growth and nucleation in the early C. elegans embryo. Dev. Cell 9 (2005) 223-236
    • (2005) Dev. Cell , vol.9 , pp. 223-236
    • Srayko1
  • 67
    • 0027358886 scopus 로고
    • The t-complex polypeptide complex is a chaperonin for tubulin and actin in vivo
    • Sternlicht, et al. The t-complex polypeptide complex is a chaperonin for tubulin and actin in vivo. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 9422-9426
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 9422-9426
    • Sternlicht1
  • 68
    • 33646381898 scopus 로고    scopus 로고
    • PhLP modulates CCT-mediated actin and tubulin folding via ternary complexes with substrates
    • Stirling, et al. PhLP modulates CCT-mediated actin and tubulin folding via ternary complexes with substrates. J. Biol. Chem. 281 (2006) 7012-7021
    • (2006) J. Biol. Chem. , vol.281 , pp. 7012-7021
    • Stirling1
  • 69
    • 34250376054 scopus 로고    scopus 로고
    • Functional interaction between phosducin-like protein 2 and cytosolic chaperonin is essential for cytoskeletal protein function and cell cycle progression
    • Stirling, et al. Functional interaction between phosducin-like protein 2 and cytosolic chaperonin is essential for cytoskeletal protein function and cell cycle progression. Mol. Biol. Cell 18 (2007) 2336-2345
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2336-2345
    • Stirling1
  • 70
    • 0021064382 scopus 로고
    • Generation of asymmetry and segregation of germ-line granules in early C. elegans embryos
    • Strome S., and Wood W.B. Generation of asymmetry and segregation of germ-line granules in early C. elegans embryos. Cell 35 (1983) 15-25
    • (1983) Cell , vol.35 , pp. 15-25
    • Strome, S.1    Wood, W.B.2
  • 71
    • 0033521588 scopus 로고    scopus 로고
    • In vivo translated polypeptides are sequestered in a protected folding environment
    • Thulasiraman, et al. In vivo translated polypeptides are sequestered in a protected folding environment. EMBO J. 18 (1999) 85-95
    • (1999) EMBO J. , vol.18 , pp. 85-95
    • Thulasiraman1
  • 72
    • 0032578911 scopus 로고    scopus 로고
    • Specific interference by ingested dsRNA
    • Timmons L., and Fire A. Specific interference by ingested dsRNA. Nature 395 (1998) 854
    • (1998) Nature , vol.395 , pp. 854
    • Timmons, L.1    Fire, A.2
  • 73
    • 0029941650 scopus 로고    scopus 로고
    • Identification of a novel protein (VBP-1) binding to the von Hippel-Lindau (VHL) tumor suppressor gene product
    • Tsuchiya, et al. Identification of a novel protein (VBP-1) binding to the von Hippel-Lindau (VHL) tumor suppressor gene product. Cancer Res. 56 (1996) 2881-2885
    • (1996) Cancer Res. , vol.56 , pp. 2881-2885
    • Tsuchiya1
  • 74
    • 0032577573 scopus 로고    scopus 로고
    • Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
    • Vainberg, et al. Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin. Cell 93 (1998) 863-873
    • (1998) Cell , vol.93 , pp. 863-873
    • Vainberg1
  • 75
    • 0024094432 scopus 로고
    • Dynamic instability of individual microtubules analyzed by light microscopy: rate constants and transition frequencies
    • Walker, et al. Dynamic instability of individual microtubules analyzed by light microscopy: rate constants and transition frequencies. J. Cell Biol. 107 (1988) 1437-1448
    • (1988) J. Cell Biol. , vol.107 , pp. 1437-1448
    • Walker1
  • 76
    • 37549069143 scopus 로고    scopus 로고
    • Composition and function of the eukaryotic cytosolic chaperonin-containing TCP-1
    • Bukau B. (Ed), Oxford University Press, Oxford
    • Willison K.R. Composition and function of the eukaryotic cytosolic chaperonin-containing TCP-1. In: Bukau B. (Ed). Molecular Chaperones: Frontiers in Molecular Biology (1999), Oxford University Press, Oxford
    • (1999) Molecular Chaperones: Frontiers in Molecular Biology
    • Willison, K.R.1
  • 77
    • 0344392858 scopus 로고    scopus 로고
    • Mutations is a β-tubulin disrupt spindle orientation and microtubule dynamics in the early Caenorhabditis elegans embryo
    • Wright A.J., and Hunter C.P. Mutations is a β-tubulin disrupt spindle orientation and microtubule dynamics in the early Caenorhabditis elegans embryo. Mol. Biol. Cell 14 (2003) 4512-4525
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4512-4525
    • Wright, A.J.1    Hunter, C.P.2
  • 78
    • 0026650749 scopus 로고
    • TCP1 complex is a molecular chaperone in tubulin biogenesis
    • Yaffe, et al. TCP1 complex is a molecular chaperone in tubulin biogenesis. Nature 358 (1992) 245-248
    • (1992) Nature , vol.358 , pp. 245-248
    • Yaffe1
  • 79
    • 0033601303 scopus 로고    scopus 로고
    • Cytosolic chaperonin is up-regulated during cell growth
    • Yokota, et al. Cytosolic chaperonin is up-regulated during cell growth. J. Biol. Chem. 274 (1999) 37070-37078
    • (1999) J. Biol. Chem. , vol.274 , pp. 37070-37078
    • Yokota1
  • 80
    • 21244434862 scopus 로고    scopus 로고
    • Facilitated release of substrate protein from prefoldin by chaperonin
    • Zako, et al. Facilitated release of substrate protein from prefoldin by chaperonin. FEBS Lett. 579 (2005) 3718-3724
    • (2005) FEBS Lett. , vol.579 , pp. 3718-3724
    • Zako1
  • 81
    • 0035422776 scopus 로고    scopus 로고
    • Roles for 147 embryonic lethal genes on C. elegans chromosome I identified by RNA interference and video microscopy
    • Zipperlen, et al. Roles for 147 embryonic lethal genes on C. elegans chromosome I identified by RNA interference and video microscopy. EMBO J. 20 (2001) 3984-3992
    • (2001) EMBO J. , vol.20 , pp. 3984-3992
    • Zipperlen1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.