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Volumn 212, Issue 2, 2002, Pages 70-80

HSP90 function is required for morphogenesis in ascidian and echinoid embryos

Author keywords

Epithelium; Gastrulation; Mesenchyme; Molecular chaperone

Indexed keywords

CHAPERONE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; RADICICOL;

EID: 0036938724     PISSN: 0949944X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00427-002-0212-9     Document Type: Review
Times cited : (18)

References (50)
  • 1
    • 0028589101 scopus 로고
    • A role for HSP90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with HSP90
    • Aligue R, Akhavan-Niak H, Russell P (1994) A role for HSP90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with HSP90. EMBO J 13:6099-6106
    • (1994) EMBO J. , vol.13 , pp. 6099-6106
    • Aligue, R.1    Akhavan-Niak, H.2    Russell, P.3
  • 2
    • 0027062705 scopus 로고
    • Microfilaments, cell shape changes, and the formation of primary mesenchyme in sea urchin embryos
    • Anstrom JA (1992) Microfilaments, cell shape changes, and the formation of primary mesenchyme in sea urchin embryos. J Exp Zool 264:312-322
    • (1992) J. Exp. Zool. , vol.264 , pp. 312-322
    • Anstrom, J.A.1
  • 3
    • 0023683808 scopus 로고
    • Development of myoplasm-enriched embryos
    • Bates WR (1988) Development of myoplasm-enriched embryos. Dev Biol 129:241-252
    • (1988) Dev. Biol. , vol.129 , pp. 241-252
    • Bates, W.R.1
  • 4
    • 0023132087 scopus 로고
    • Alkaline phosphatase expression in ascidian egg fragments and andromerogons
    • Bates WR, Jeffery WR (1987) Alkaline phosphatase expression in ascidian egg fragments and andromerogons. Dev Biol 119:382-389
    • (1987) Dev. Biol. , vol.119 , pp. 382-389
    • Bates, W.R.1    Jeffery, W.R.2
  • 5
    • 0022779172 scopus 로고
    • Translational activation of maternal mRNA encoding the heat-shock protein HSP90 during sea urchin embryogenesis
    • Bédard P-A, Brandhorst BP (1986) Translational activation of maternal mRNA encoding the heat-shock protein HSP90 during sea urchin embryogenesis. Dev Biol 117:286-293
    • (1986) Dev. Biol. , vol.117 , pp. 286-293
    • Bédard, P.-A.1    Brandhorst, B.P.2
  • 7
    • 0034625366 scopus 로고    scopus 로고
    • Ubiquination of neural nitric oxide synthase in vitro and in vivo
    • Bender AT, Demady DR, Osawa Y (2000) Ubiquination of neural nitric oxide synthase in vitro and in vivo. J Biol Chem 275:17407-17411
    • (2000) J. Biol. Chem. , vol.275 , pp. 17407-17411
    • Bender, A.T.1    Demady, D.R.2    Osawa, Y.3
  • 8
    • 0025773669 scopus 로고
    • Role of the extracellular matrix in tissue-specific gene expression in the sea urchin embryo
    • Benson S, Rawson R, Killian C, Wilt F (1991) Role of the extracellular matrix in tissue-specific gene expression in the sea urchin embryo. Mol Reprod Dev 29:220-226
    • (1991) Mol. Reprod. Dev. , vol.29 , pp. 220-226
    • Benson, S.1    Rawson, R.2    Killian, C.3    Wilt, F.4
  • 9
    • 0035543255 scopus 로고    scopus 로고
    • NO/cGMP signaling and HSP90 activity represses metamorphosis in the sea urchin Lytechinus pictus
    • 2001
    • Bishop CD, Brandhorst BP (2001) NO/cGMP signaling and HSP90 activity represses metamorphosis in the sea urchin Lytechinus pictus. Biol Bull 2001:394-404
    • (2001) Biol. Bull. , pp. 394-404
    • Bishop, C.D.1    Brandhorst, B.P.2
  • 10
    • 0035339386 scopus 로고    scopus 로고
    • Regulation of metamorphosis in ascidians involves NO/cGMP signaling and HSP90
    • Bishop CD, Bates WR, Brandhorst BP (2001) Regulation of metamorphosis in ascidians involves NO/cGMP signaling and HSP90. J Exp Zool 289:374-384
    • (2001) J. Exp. Zool. , vol.289 , pp. 374-384
    • Bishop, C.D.1    Bates, W.R.2    Brandhorst, B.P.3
  • 11
    • 0033168520 scopus 로고    scopus 로고
    • HSP90's secrets unfold: New insights from structural and functional studies
    • Caplan AJ (1999) HSP90's secrets unfold: new insights from structural and functional studies. Trends Cell Biol 9:262-268
    • (1999) Trends Cell Biol. , vol.9 , pp. 262-268
    • Caplan, A.J.1
  • 12
    • 0029760873 scopus 로고    scopus 로고
    • A new member of the HSP90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock
    • Chen C-F, Chen Y, Dai K, Chen P-L, Riley DJ, Lee W-H (1996) A new member of the HSP90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock. Mol Cell Biol 16:4691-4699
    • (1996) Mol. Cell Biol. , vol.16 , pp. 4691-4699
    • Chen, C.-F.1    Chen, Y.2    Dai, K.3    Chen, P.-L.4    Riley, D.J.5    Lee, W.-H.6
  • 13
    • 0031020541 scopus 로고    scopus 로고
    • Tissue-specific expression of an hsc90 gene and nuclear translocation of the HSC90-related protein during amphibian embryogenesis
    • Coumailleau P, Bonnanfant-Jais M-L, Laine M-C, Angelier N (1997) Tissue-specific expression of an hsc90 gene and nuclear translocation of the HSC90-related protein during amphibian embryogenesis. Dev Genes Evol 206:397-406
    • (1997) Dev. Genes Evol. , vol.206 , pp. 397-406
    • Coumailleau, P.1    Bonnanfant-Jais, M.-L.2    Laine, M.-C.3    Angelier, N.4
  • 14
    • 0028363670 scopus 로고
    • Mutations in HsP83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila
    • Cutforth T, Rubin G (1994) Mutations in HsP83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. Cell 77:1027-1036
    • (1994) Cell , vol.77 , pp. 1027-1036
    • Cutforth, T.1    Rubin, G.2
  • 15
    • 0030808079 scopus 로고    scopus 로고
    • Geldanamycin, heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus
    • Czar MJ, Galigniana MD, Silverstein AM, Pratt WB (1997) Geldanamycin, heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus. Biochemistry 36:7776-7785
    • (1997) Biochemistry , vol.36 , pp. 7776-7785
    • Czar, M.J.1    Galigniana, M.D.2    Silverstein, A.M.3    Pratt, W.B.4
  • 16
    • 0035881540 scopus 로고    scopus 로고
    • The BMP/CHORDIN antagonism controls sensory pigment cell specification and differentiation in the ascidian embryo
    • Darras S, Nishida H (2001) The BMP/CHORDIN antagonism controls sensory pigment cell specification and differentiation in the ascidian embryo. Dev Biol 236:271-88
    • (2001) Dev. Biol. , vol.236 , pp. 271-288
    • Darras, S.1    Nishida, H.2
  • 17
    • 0025900617 scopus 로고
    • Spatial mechanisms of gene regulation in metazoan embryos
    • Davidson EH (1991) Spatial mechanisms of gene regulation in metazoan embryos. Development 113:1-26
    • (1991) Development , vol.113 , pp. 1-26
    • Davidson, E.H.1
  • 18
    • 0027269688 scopus 로고
    • Dynamic Hsp83 RNA localization during Drosophila oogenesis and embryogenesis
    • Ding D, Parkhurst SM, Halsell SR, Lipshitz HD (1993) Dynamic Hsp83 RNA localization during Drosophila oogenesis and embryogenesis. Mol Cell Biol 13:3773-3781
    • (1993) Mol. Cell Biol. , vol.13 , pp. 3773-3781
    • Ding, D.1    Parkhurst, S.M.2    Halsell, S.R.3    Lipshitz, H.D.4
  • 19
    • 0033523284 scopus 로고    scopus 로고
    • Cell movements in the sea urchin embryo
    • Ettensohn CA (1999) Cell movements in the sea urchin embryo. Cuff Opin Gen Dev 9:461-465
    • (1999) Cuff. Opin. Gen. Dev. , vol.9 , pp. 461-465
    • Ettensohn, C.A.1
  • 20
    • 0021951808 scopus 로고
    • Three cell recongition changes accompany the ingression of sea urchin primary mesenchyme cells
    • Fink RD, McClay DR (1985) Three cell recongition changes accompany the ingression of sea urchin primary mesenchyme cells. Dev Biol 107:66-74
    • (1985) Dev. Biol. , vol.107 , pp. 66-74
    • Fink, R.D.1    McClay, D.R.2
  • 21
    • 0004068679 scopus 로고    scopus 로고
    • Cells, embryos, and evolution
    • Blackwell, Oxford
    • Gerhart J, Kirschner M(1997) Cells, embryos, and evolution. Blackwell, Oxford
    • (1997)
    • Gerhart, J.1    Kirschner, M.2
  • 22
    • 0021914548 scopus 로고
    • The origin of pigment cells in embryos of the sea urchin Strongylocentrotus purpuratus
    • Gibson AW, Burke RD (1985) The origin of pigment cells in embryos of the sea urchin Strongylocentrotus purpuratus. Dev Biol 107:414-419
    • (1985) Dev. Biol. , vol.107 , pp. 414-419
    • Gibson, A.W.1    Burke, R.D.2
  • 23
    • 0033581021 scopus 로고    scopus 로고
    • The importance of ATP binding and hydrolysis by HSP90 in formation and function of protein heterocomplexes
    • Grenert JP, Johnson BD, Toft DO (1999) The importance of ATP binding and hydrolysis by HSP90 in formation and function of protein heterocomplexes. J Biol Chem 274:17525-17533
    • (1999) J. Biol. Chem. , vol.274 , pp. 17525-17533
    • Grenert, J.P.1    Johnson, B.D.2    Toft, D.O.3
  • 24
    • 0032478703 scopus 로고    scopus 로고
    • Modular folding and evidence for phosphorylation induced stabilization of an HSP90-dependent kinase
    • Hartson SD, Ottinger EA, Huang W, Barany G, Burn P, Matts RL (1998) Modular folding and evidence for phosphorylation induced stabilization of an HSP90-dependent kinase. J Biol Chem 273:8475-8482
    • (1998) J. Biol. Chem. , vol.273 , pp. 8475-8482
    • Hartson, S.D.1    Ottinger, E.A.2    Huang, W.3    Barany, G.4    Burn, P.5    Matts, R.L.6
  • 25
    • 0027533823 scopus 로고
    • Major temporal and spatial patterns of gene expression of the sea urchin embryo
    • Kingsley PD, Angerer LM, Angerer RC (1993) Major temporal and spatial patterns of gene expression of the sea urchin embryo. Dev Biol 155:216-234
    • (1993) Dev. Biol. , vol.155 , pp. 216-234
    • Kingsley, P.D.1    Angerer, L.M.2    Angerer, R.C.3
  • 28
    • 0034491506 scopus 로고    scopus 로고
    • Adaptive evolution of larvae and life cycles
    • McEdward LR (2000) Adaptive evolution of larvae and life cycles. Semin Cell Dev Biol 11:403-409
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 403-409
    • McEdward, L.R.1
  • 29
    • 0029037110 scopus 로고
    • Mutational analysis of HSP90 function: Interactions with a steroid hormone receptor and a protein kinase
    • Nathan D, Lindquist S (1995) Mutational analysis of HSP90 function: interactions with a steroid hormone receptor and a protein kinase. Mol Cell Biol 15:3917-3925
    • (1995) Mol. Cell Biol. , vol.15 , pp. 3917-3925
    • Nathan, D.1    Lindquist, S.2
  • 30
    • 0030933688 scopus 로고    scopus 로고
    • Analysis of the temporal expression of endoderm-specific alkaline phosphatase during development of the ascidian Halocynthia roretzi
    • Nishida H, Kumano G (1997) Analysis of the temporal expression of endoderm-specific alkaline phosphatase during development of the ascidian Halocynthia roretzi. Dev Growth Differ 39:199-205
    • (1997) Dev. Growth Differ. , vol.39 , pp. 199-205
    • Nishida, H.1    Kumano, G.2
  • 31
    • 0032787306 scopus 로고    scopus 로고
    • The benzoquinone ansamycin geldanamycin stimulates proteolytic degredation of focal adhesion kinase
    • Ochel H-J, Schulte TW, Nguyen P, Trepel J, Neckers L (1999) The benzoquinone ansamycin geldanamycin stimulates proteolytic degredation of focal adhesion kinase. Mol Genet Metab 66:24-30
    • (1999) Mol. Genet. Metab. , vol.66 , pp. 24-30
    • Ochel, H.-J.1    Schulte, T.W.2    Nguyen, P.3    Trepel, J.4    Neckers, L.5
  • 32
  • 33
    • 0022476610 scopus 로고
    • The fate of the small micromeres in sea urchin development
    • Pehrson JR, Cohen LH (1986) The fate of the small micromeres in sea urchin development. Dev Biol 113:552-566
    • (1986) Dev. Biol. , vol.113 , pp. 552-566
    • Pehrson, J.R.1    Cohen, L.H.2
  • 34
    • 0031895351 scopus 로고    scopus 로고
    • The HSP90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors
    • Pratt WB (1998) The HSP90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exp Biol Med 217:420-434
    • (1998) Proc. Soc. Exp. Biol. Med. , vol.217 , pp. 420-434
    • Pratt, W.B.1
  • 35
    • 0034892432 scopus 로고    scopus 로고
    • HSP90: Chaperoning signal transduction
    • Richter K, Buchner J (2001) HSP90: chaperoning signal transduction. J Cell Physiol 188:281-290
    • (2001) J. Cell Physiol. , vol.188 , pp. 281-290
    • Richter, K.1    Buchner, J.2
  • 36
    • 0032569851 scopus 로고    scopus 로고
    • HSP90 as a capacitor for morphological evolution
    • Rutherford SL, Lindquist S (1998) HSP90 as a capacitor for morphological evolution. Nature 396:336-342
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 37
    • 0030029444 scopus 로고    scopus 로고
    • Specific localization of zebrafish HSP90α mRNA to myoD-expressing cells suggest a role for HSP90α during normal muscle development
    • Sass JB, Weinberg ES, Krone PH (1996) Specific localization of zebrafish HSP90α mRNA to myoD-expressing cells suggest a role for HSP90α during normal muscle development. Mech Dev 54:195-204
    • (1996) Mech. Dev. , vol.54 , pp. 195-204
    • Sass, J.B.1    Weinberg, E.S.2    Krone, P.H.3
  • 38
    • 0003610685 scopus 로고
    • Developmental biology of ascidians
    • Cambridge University Press, Cambridge
    • Satoh N (1994) Developmental biology of ascidians. Cambridge University Press, Cambridge
    • (1994)
    • Satoh, N.1
  • 39
    • 0031915021 scopus 로고    scopus 로고
    • Integrin signaling and tyrosin phosphorylation: Just the FAKs?
    • Schlaepfer DD, Hunter T (1998) Integrin signaling and tyrosin phosphorylation: just the FAKs? Trends Cell Biol 8:152-157
    • (1998) Trends Cell Biol. , vol.8 , pp. 152-157
    • Schlaepfer, D.D.1    Hunter, T.2
  • 41
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the N-terminal domain of HSP90 and shares important biologic activities with geldanamycin
    • Schulte TW, Akinaga S, Sullivan W, Stensgard B, Toft D, Neckers LM (1998) Antibiotic radicicol binds to the N-terminal domain of HSP90 and shares important biologic activities with geldanamycin. Cell Stress Chaperones 3:100-108
    • (1998) Cell Stress Chaperones , vol.3 , pp. 100-108
    • Schulte, T.W.1    Akinaga, S.2    Sullivan, W.3    Stensgard, B.4    Toft, D.5    Neckers, L.M.6
  • 42
    • 0032554763 scopus 로고    scopus 로고
    • Targeting of the protein chaperone HSP90 by the transformation suppressing agent radicicol
    • Sharma SV, Agatsuma T, Nakano H (1998) Targeting of the protein chaperone HSP90 by the transformation suppressing agent radicicol. Oncogene 16:2639-2645
    • (1998) Oncogene , vol.16 , pp. 2639-2645
    • Sharma, S.V.1    Agatsuma, T.2    Nakano, H.3
  • 43
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an HSP90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich N (1997) Crystal structure of an HSP90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89:239-250
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.6
  • 46
    • 0027193607 scopus 로고
    • Heat shock gene expression and cell cycle changes during mammalian embryonic development
    • Walsh D, Li K, Wass J, Dolnikov A, Zeng F, Zhe L, Edwards M (1993) Heat shock gene expression and cell cycle changes during mammalian embryonic development. Dev Genet 14:127-136
    • (1993) Dev. Genet. , vol.14 , pp. 127-136
    • Walsh, D.1    Li, K.2    Wass, J.3    Dolnikov, A.4    Zeng, F.5    Zhe, L.6    Edwards, M.7
  • 48
    • 0017558844 scopus 로고
    • Segregation during cleavage of a factor determining endodermal alkaline phosphatase development in ascidian embryos
    • Whittaker JR (1977) Segregation during cleavage of a factor determining endodermal alkaline phosphatase development in ascidian embryos. J Exp Zool 202:139-154
    • (1977) J. Exp. Zool. , vol.202 , pp. 139-154
    • Whittaker, J.R.1
  • 49
    • 0035939668 scopus 로고    scopus 로고
    • HSP90: A specialized but essential protein folding tool
    • Young JC, Moarefi I, Hartl UF (2001) HSP90: a specialized but essential protein folding tool. J Cell Biol 154:267-273
    • (2001) J. Cell Biol. , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, U.F.3
  • 50
    • 0032980876 scopus 로고    scopus 로고
    • Genetic analysis of viable HSP90 alleles reveals a critical role in Drosophila spermatogenesis
    • Yue L, Karr TL, Nathan DF, Swift H, Srinivasan S, Lindquist S (1999) Genetic analysis of viable HSP90 alleles reveals a critical role in Drosophila spermatogenesis. Genetics 151: 1065-1079
    • (1999) Genetics , vol.151 , pp. 1065-1079
    • Yue, L.1    Karr, T.L.2    Nathan, D.F.3    Swift, H.4    Srinivasan, S.5    Lindquist, S.6


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