메뉴 건너뛰기




Volumn 140, Issue 6, 2006, Pages 805-812

Heat shock protein 40/DjB1 is required for thermotolerance in early phase

Author keywords

DjB1 (Hsp40 DnajB1 Hdj1); Hsp70; Knockout mice; Molecular chaperone; Thermotolerance

Indexed keywords

HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN 40; PROTEIN DJB1; PROTEIN DNAJ; UNCLASSIFIED DRUG; ANTIBODY; BISBENZIMIDE; DNAJB1 PROTEIN, MOUSE; HEAT SHOCK PROTEIN 70;

EID: 34250670010     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvj212     Document Type: Article
Times cited : (14)

References (48)
  • 1
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B. and Horwich, A.L. (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 2
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • 647
    • Frydman, J. (2001) Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70, 603-647
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 603
    • Frydman, J.1
  • 3
    • 0037040541 scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F.U. and Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858
    • (1858) Science , vol.295 , pp. 1852
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 4
    • 33646127577 scopus 로고    scopus 로고
    • Cell 125, 443-451
    • Bukau, B., Weissman, J., and Horwich, A. (2006) Molecular chaperones and protein quality control. Cell 125, 443-451
    • (2006)
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 5
    • 0642377466 scopus 로고    scopus 로고
    • More than folding: Localized functions of cytosolic chaperones
    • Young, J.C., Barral, J.M., and Hartl, F.U. (2003) More than folding: localized functions of cytosolic chaperones. Trends Biochem. Sci. 28, 541-547
    • (2003) Trends Biochem. Sci , vol.28 , pp. 541-547
    • Young, J.C.1    Barral, J.M.2    Hartl, F.U.3
  • 6
    • 2342651518 scopus 로고    scopus 로고
    • Molecular chaperones and the stress of oncogenesis
    • Mosser, D.D. and Morimoto, R.I. (2004) Molecular chaperones and the stress of oncogenesis. Oncogene 23, 2907-2918
    • (2004) Oncogene , vol.23 , pp. 2907-2918
    • Mosser, D.D.1    Morimoto, R.I.2
  • 7
    • 0347122087 scopus 로고    scopus 로고
    • Hsp70 promotes antigen-presenting cell function and converts T-cell tolerance to autoimmunity in vivo
    • Millar, D.G., Garza, K.M., Odermatt, B., Elford, A.R., Ono, N., Li, Z., and Ohashi, P.S. (2003) Hsp70 promotes antigen-presenting cell function and converts T-cell tolerance to autoimmunity in vivo. Nat. Med. 9, 1469-1476
    • (2003) Nat. Med , vol.9 , pp. 1469-1476
    • Millar, D.G.1    Garza, K.M.2    Odermatt, B.3    Elford, A.R.4    Ono, N.5    Li, Z.6    Ohashi, P.S.7
  • 8
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman, J., Nimmesgern, E., Ohtsuka, K., and Hartl, F.U. (1994) Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370, 111-117
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F.U.4
  • 10
    • 0029051966 scopus 로고
    • Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
    • Freeman, B.C., Myers, M.P., Schumacher, R., and Morimoto, R.I. (1995) Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J. 14, 2281-2292
    • (1995) EMBO J , vol.14 , pp. 2281-2292
    • Freeman, B.C.1    Myers, M.P.2    Schumacher, R.3    Morimoto, R.I.4
  • 11
    • 0029741321 scopus 로고    scopus 로고
    • Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40
    • Minami, Y., Hohfeld, J., Ohtsuka, K., and Hartl, F.U. (1996) Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40. J. Biol. Chem. 271, 19617-19624
    • (1996) J. Biol. Chem , vol.271 , pp. 19617-19624
    • Minami, Y.1    Hohfeld, J.2    Ohtsuka, K.3    Hartl, F.U.4
  • 12
    • 0033634924 scopus 로고    scopus 로고
    • Mammalian HSP40/DNAJ homologs: Cloning of novel cDNAs and a proposal for their classification and nomenclature
    • Ohtsuka, K. and Hata, M. (2000) Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature. Cell Stress Chaperones 5, 98-112
    • (2000) Cell Stress Chaperones , vol.5 , pp. 98-112
    • Ohtsuka, K.1    Hata, M.2
  • 13
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: Conservation and adaptation of chaperone function
    • Cheetham, M.E. and Caplan, A.J. (1998) Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones 3, 28-36
    • (1998) Cell Stress Chaperones , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 15
    • 12144291154 scopus 로고    scopus 로고
    • Tid1, a cochaperone of the heat shock 70 protein and the mammalian counterpart of the Drosophila tumor suppressor 1(2)tid, is critical for early embryonic development and cell survival
    • Lo, J.F., Hayashi, M., Woo-Kim, S., Tian, B., Huang, J.F., Fearns, C., Takayama, S., Zapata, J.M., Yang, Y., and Lee, J.D. (2004) Tid1, a cochaperone of the heat shock 70 protein and the mammalian counterpart of the Drosophila tumor suppressor 1(2)tid, is critical for early embryonic development and cell survival. Mol. Cell. Biol. 24, 2226-2236
    • (2004) Mol. Cell. Biol , vol.24 , pp. 2226-2236
    • Lo, J.F.1    Hayashi, M.2    Woo-Kim, S.3    Tian, B.4    Huang, J.F.5    Fearns, C.6    Takayama, S.7    Zapata, J.M.8    Yang, Y.9    Lee, J.D.10
  • 17
    • 0032930952 scopus 로고    scopus 로고
    • Mrj encodes a DnaJ-related co-chaperone that is essential for murine placental development
    • Hunter, P.J., Swanson, B.J., Haendel, M.A., Lyons, G.E., and Cross, J.C. (1999) Mrj encodes a DnaJ-related co-chaperone that is essential for murine placental development. Development 126, 1247-1258
    • (1999) Development , vol.126 , pp. 1247-1258
    • Hunter, P.J.1    Swanson, B.J.2    Haendel, M.A.3    Lyons, G.E.4    Cross, J.C.5
  • 20
    • 0026529566 scopus 로고
    • Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells
    • Hattori, H., Liu, Y.C., Tohnai, I., Ueda, M., Kaneda, T., Kobayashi, T., Tanabe, K., and Ohtsuka, K. (1992) Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells. Cell Struct. Funct. 17, 77-86
    • (1992) Cell Struct. Funct , vol.17 , pp. 77-86
    • Hattori, H.1    Liu, Y.C.2    Tohnai, I.3    Ueda, M.4    Kaneda, T.5    Kobayashi, T.6    Tanabe, K.7    Ohtsuka, K.8
  • 21
    • 0032103439 scopus 로고    scopus 로고
    • The J-domain family and the recruitment of chaperone power
    • Kelley, W.L. (1998) The J-domain family and the recruitment of chaperone power. Trends Biochem. Sci. 23, 222-227
    • (1998) Trends Biochem. Sci , vol.23 , pp. 222-227
    • Kelley, W.L.1
  • 22
    • 0030830249 scopus 로고    scopus 로고
    • The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding
    • Terada, K., Kanazawa, M., Bukau, B., and Mori, M. (1997) The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding. J. Cell Biol. 139, 1089-1095
    • (1997) J. Cell Biol , vol.139 , pp. 1089-1095
    • Terada, K.1    Kanazawa, M.2    Bukau, B.3    Mori, M.4
  • 23
    • 0034637603 scopus 로고    scopus 로고
    • Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70
    • Terada, K. and Mori, M. (2000) Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70. J. Biol. Chem. 275, 24728-24734
    • (2000) J. Biol. Chem , vol.275 , pp. 24728-24734
    • Terada, K.1    Mori, M.2
  • 24
    • 1842785349 scopus 로고    scopus 로고
    • Modulation of chaperone activities of Hsp70 and Hsp70-2 by a mammalian DnaJ/Hsp40 homolog, DjA4
    • Hafizur, R.M., Yano, M., Gotoh, T., Mori, M., and Terada, K. (2004) Modulation of chaperone activities of Hsp70 and Hsp70-2 by a mammalian DnaJ/Hsp40 homolog, DjA4. J. Biochem. 135, 193-200
    • (2004) J. Biochem , vol.135 , pp. 193-200
    • Hafizur, R.M.1    Yano, M.2    Gotoh, T.3    Mori, M.4    Terada, K.5
  • 25
    • 0035042529 scopus 로고    scopus 로고
    • hsp70-DnaJ chaperone pairs prevent nitric oxide-mediated apoptosis in RAW 264.7 macrophages
    • Gotoh, T., Terada, K., and Mori, M. (2001) hsp70-DnaJ chaperone pairs prevent nitric oxide-mediated apoptosis in RAW 264.7 macrophages. Cell Death Differ. 8, 357-366
    • (2001) Cell Death Differ , vol.8 , pp. 357-366
    • Gotoh, T.1    Terada, K.2    Mori, M.3
  • 26
    • 1842843854 scopus 로고    scopus 로고
    • hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria
    • Gotoh, T., Terada, K., Oyadomari, S., and Mori, M. (2004) hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria. Cell Death Differ. 11, 390-402
    • (2004) Cell Death Differ , vol.11 , pp. 390-402
    • Gotoh, T.1    Terada, K.2    Oyadomari, S.3    Mori, M.4
  • 27
    • 0027495527 scopus 로고
    • A novel negative selection for homologous recombinants using diphtheria toxin A fragment gene
    • Yagi, T., Nada, S., Watanabe, N., Tamemoto, H., Kohmura, N., Ikawa, Y., and Aizawa, S. (1993) A novel negative selection for homologous recombinants using diphtheria toxin A fragment gene. Anal. Biochem. 214, 77-86
    • (1993) Anal. Biochem , vol.214 , pp. 77-86
    • Yagi, T.1    Nada, S.2    Watanabe, N.3    Tamemoto, H.4    Kohmura, N.5    Ikawa, Y.6    Aizawa, S.7
  • 29
    • 0036556685 scopus 로고    scopus 로고
    • Characterization and functional analysis of a heart-enriched DnaJ/ Hsp40 homolog dj4/DjA4
    • Abdul, K.M., Terada, K., Gotoh, T., Hafizur, R.M., and Mori, M. (2002) Characterization and functional analysis of a heart-enriched DnaJ/ Hsp40 homolog dj4/DjA4. Cell Stress Chaperones 7, 156-166
    • (2002) Cell Stress Chaperones , vol.7 , pp. 156-166
    • Abdul, K.M.1    Terada, K.2    Gotoh, T.3    Hafizur, R.M.4    Mori, M.5
  • 30
    • 0030739208 scopus 로고    scopus 로고
    • Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis
    • Mosser, D.D., Caron, A.W., Bourget, L., Denis-Larose, C., and Massie, B. (1997) Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis. Mol. Cell. Biol. 17, 5317-5327
    • (1997) Mol. Cell. Biol , vol.17 , pp. 5317-5327
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3    Denis-Larose, C.4    Massie, B.5
  • 31
    • 0031469912 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells
    • Michels, A.A., Kanon, B., Konings, A.W., Ohtsuka, K., Bensaude, O., and Kampinga, H.H. (1997) Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells. J. Biol. Chem. 272, 33283-33289
    • (1997) J. Biol. Chem , vol.272 , pp. 33283-33289
    • Michels, A.A.1    Kanon, B.2    Konings, A.W.3    Ohtsuka, K.4    Bensaude, O.5    Kampinga, H.H.6
  • 32
    • 0027158545 scopus 로고
    • Structure and organisation of a murine gene encoding small heat-shock protein Hsp25
    • Gaestel, M., Gotthardt, R., and Muller, T. (1993) Structure and organisation of a murine gene encoding small heat-shock protein Hsp25. Gene 128, 279-283
    • (1993) Gene , vol.128 , pp. 279-283
    • Gaestel, M.1    Gotthardt, R.2    Muller, T.3
  • 33
    • 0026773690 scopus 로고
    • Development of acute thermotolerance in 1929 cells: Lack of HSP28 synthesis and phosphorylation
    • Lee, Y.J., Hou, Z.Z., Curetty, L., and Borrelli, M.J. (1992) Development of acute thermotolerance in 1929 cells: Lack of HSP28 synthesis and phosphorylation. J. Cell. Physiol. 152, 118-125
    • (1992) J. Cell. Physiol , vol.152 , pp. 118-125
    • Lee, Y.J.1    Hou, Z.Z.2    Curetty, L.3    Borrelli, M.J.4
  • 34
    • 0027311871 scopus 로고
    • A stress-inducible 40 kDa protein (hsp40): Purification by modified two-dimensional gel electrophoresis and co-localization with hsc70(p73) in heat-shocked HeLa cells
    • Hattori, H., Kaneda, T., Lokeshwar, B., Laszlo, A., and Ohtsuka, K. (1993) A stress-inducible 40 kDa protein (hsp40): purification by modified two-dimensional gel electrophoresis and co-localization with hsc70(p73) in heat-shocked HeLa cells. J. Cell Sci. 104, 629-638
    • (1993) J. Cell Sci , vol.104 , pp. 629-638
    • Hattori, H.1    Kaneda, T.2    Lokeshwar, B.3    Laszlo, A.4    Ohtsuka, K.5
  • 35
    • 0021767876 scopus 로고
    • Hsp70 accelerates the recovery of nucleolar morphology after heat shock
    • Pelham, H.R. (1984) Hsp70 accelerates the recovery of nucleolar morphology after heat shock. EMBO J. 3, 3095-3100
    • (1984) EMBO J , vol.3 , pp. 3095-3100
    • Pelham, H.R.1
  • 36
    • 0029911025 scopus 로고    scopus 로고
    • Heat shock causes protein aggregation and reduced protein solubility at the centrosome and other cytoplasmic locations
    • Vidair, C.A., Huang, R.N., and Doxsey, S.J. (1996) Heat shock causes protein aggregation and reduced protein solubility at the centrosome and other cytoplasmic locations. Int. J. Hyperthermia 12, 681-695
    • (1996) Int. J. Hyperthermia , vol.12 , pp. 681-695
    • Vidair, C.A.1    Huang, R.N.2    Doxsey, S.J.3
  • 37
    • 23044444001 scopus 로고    scopus 로고
    • Hsp70 protects mitotic cells against heat-induced centrosome damage and division abnormalities
    • Hut, H.M., Kampinga, H.H., and Sibon, O.C. (2005) Hsp70 protects mitotic cells against heat-induced centrosome damage and division abnormalities. Mol. Biol. Cell 16, 3776-3785
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3776-3785
    • Hut, H.M.1    Kampinga, H.H.2    Sibon, O.C.3
  • 38
    • 0025824364 scopus 로고
    • Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins
    • Luke, M.M., Sutton, A., and Arndt, K.T. (1991) Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins. J. Cell Biol. 114, 623-638
    • (1991) J. Cell Biol , vol.114 , pp. 623-638
    • Luke, M.M.1    Sutton, A.2    Arndt, K.T.3
  • 39
    • 0025745326 scopus 로고
    • Characterization of YDJ1: A yeast homologue of the bacterial dnaJ protein
    • Caplan, A.J. and Douglas, M.G. (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J. Cell Biol. 114, 609-621
    • (1991) J. Cell Biol , vol.114 , pp. 609-621
    • Caplan, A.J.1    Douglas, M.G.2
  • 40
    • 0032053658 scopus 로고    scopus 로고
    • Characterization of HSE sequences in human Hsp40 gene: Structural and promoter analysis
    • Hata, M. and Ohtsuka, K. (1998) Characterization of HSE sequences in human Hsp40 gene: structural and promoter analysis. Biochim. Biophys. Acta 1397, 43-55
    • (1998) Biochim. Biophys. Acta , vol.1397 , pp. 43-55
    • Hata, M.1    Ohtsuka, K.2
  • 41
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto, R. (1998) Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev. 12, 3788-3796
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, R.1
  • 42
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-specific transcriptional repressors
    • Shi, Y., Mosser, D.D., and Morimoto, R.I. (1998) Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev. 12, 654-666
    • (1998) Genes Dev , vol.12 , pp. 654-666
    • Shi, Y.1    Mosser, D.D.2    Morimoto, R.I.3
  • 43
    • 25444440843 scopus 로고    scopus 로고
    • Stress inhibits nucleocytoplasmic shuttling of heat shock protein hsc70
    • Kodiha, M., Chu, A., Lazrak, O., and Stochaj, U. (2005) Stress inhibits nucleocytoplasmic shuttling of heat shock protein hsc70. Am. J. Physiol.-Cell Physiol. 4, 1034-1041
    • (2005) Am. J. Physiol.-Cell Physiol , vol.4 , pp. 1034-1041
    • Kodiha, M.1    Chu, A.2    Lazrak, O.3    Stochaj, U.4
  • 44
    • 0029670788 scopus 로고    scopus 로고
    • Molecular chaperones and the centrosome. A role for HSP 73 in centrosomal repair following heat shock treatment
    • Brown, C.R., Hong-Brown, L.Q., Doxsey, S.J., and Welch, W.J. (1996) Molecular chaperones and the centrosome. A role for HSP 73 in centrosomal repair following heat shock treatment. J. Biol. Chem. 271, 833-840
    • (1996) J. Biol. Chem , vol.271 , pp. 833-840
    • Brown, C.R.1    Hong-Brown, L.Q.2    Doxsey, S.J.3    Welch, W.J.4
  • 45
    • 0027441406 scopus 로고
    • Expression of the murine small heat shock proteins hsp 25 and alpha B crystallin in the absence of stress
    • Klemenz, R., Andres, A.C., Frohli, E., Schafer, R., and Aoyama, A. (1993) Expression of the murine small heat shock proteins hsp 25 and alpha B crystallin in the absence of stress. J. Cell Biol. 120, 639-645
    • (1993) J. Cell Biol , vol.120 , pp. 639-645
    • Klemenz, R.1    Andres, A.C.2    Frohli, E.3    Schafer, R.4    Aoyama, A.5
  • 46
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • Young, J.C., Moarefi, I., and Hartl, F.U. (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, F.U.3
  • 48
    • 0034193778 scopus 로고    scopus 로고
    • The nucleolus: An old factory with unexpected capabilities
    • Olson, M.O., Dundr, M., and Szebeni, A. (2000) The nucleolus: an old factory with unexpected capabilities. Trends Cell Biol. 10, 189-196
    • (2000) Trends Cell Biol , vol.10 , pp. 189-196
    • Olson, M.O.1    Dundr, M.2    Szebeni, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.