메뉴 건너뛰기




Volumn 238, Issue 2, 1999, Pages 333-341

Hsc40, a new member of the hsp40 family, exhibits similar expression profile to that of hsc70 in mammalian cells

Author keywords

Heat shock; hsc40; hsc70; hsp40; hsp70; Stress response

Indexed keywords

HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; UNCLASSIFIED DRUG;

EID: 0032849845     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(99)00333-9     Document Type: Article
Times cited : (10)

References (39)
  • 1
    • 0025130463 scopus 로고
    • Identification of a protein altered in mutants resistant to microtubule inhibitors as a member of the major heat shock protein (hsp70) family
    • Ahmad S., Ahuja R., Venner T.J., Gupta R.S. Identification of a protein altered in mutants resistant to microtubule inhibitors as a member of the major heat shock protein (hsp70) family. Mol. Cell. Biol. 10:(10):1990;5160-5165.
    • (1990) Mol. Cell. Biol. , vol.10 , Issue.10 , pp. 5160-5165
    • Ahmad, S.1    Ahuja, R.2    Venner, T.J.3    Gupta, R.S.4
  • 2
    • 0032406050 scopus 로고    scopus 로고
    • Stress proteins and apoptosis in prenatal development, cancer, and medicine
    • Anderson. Stress proteins and apoptosis in prenatal development, cancer, and medicine. Cell Stress and Chaperones. 3:(4):1998;209-212.
    • (1998) Cell Stress and Chaperones , vol.3 , Issue.4 , pp. 209-212
    • Anderson1
  • 3
    • 0031815373 scopus 로고    scopus 로고
    • MSH-1, a new member of the dnaJ family of proteins, is a male germ cell-specific gene product
    • Berruti G., Perego L., Borgonovo B., Martegani E. MSH-1, a new member of the dnaJ family of proteins, is a male germ cell-specific gene product. Exp. Cell Res. 239:(2):1998;430-441.
    • (1998) Exp. Cell Res. , vol.239 , Issue.2 , pp. 430-441
    • Berruti, G.1    Perego, L.2    Borgonovo, B.3    Martegani, E.4
  • 4
    • 0028879136 scopus 로고
    • Cysteine string protein, a dnaJ family member, is present on diverse secretory vesicles
    • Braun J.E.A., Scheller R.H. Cysteine string protein, a dnaJ family member, is present on diverse secretory vesicles. Neuropharmacology. 34:(11):1995;1361-1369.
    • (1995) Neuropharmacology , vol.34 , Issue.11 , pp. 1361-1369
    • Braun, J.E.A.1    Scheller, R.H.2
  • 5
    • 0027509361 scopus 로고
    • The constitutive and stress inducible forms of hsp70 exhibit functional similarities and interact with one another in an ATP-dependent fashion
    • Brown C.R., Martin R.L., Hansen W.J., Beckmann R.P., Welch W.J. The constitutive and stress inducible forms of hsp70 exhibit functional similarities and interact with one another in an ATP-dependent fashion. J. Cell Biol. 120:(5):1993;1101-1112.
    • (1993) J. Cell Biol. , vol.120 , Issue.5 , pp. 1101-1112
    • Brown, C.R.1    Martin, R.L.2    Hansen, W.J.3    Beckmann, R.P.4    Welch, W.J.5
  • 6
    • 0031149356 scopus 로고    scopus 로고
    • The dnaJ-like cysteine string protein and exocytotic neurotransmitter release
    • Buchner E., Gundersen C. The dnaJ-like cysteine string protein and exocytotic neurotransmitter release. Trends Neuro. 20:(5):1997;223-227.
    • (1997) Trends Neuro. , vol.20 , Issue.5 , pp. 223-227
    • Buchner, E.1    Gundersen, C.2
  • 8
    • 0026696593 scopus 로고
    • Human homologues of the bacterial heat-shock protein dnaJ are preferentially expressed in neurons
    • Cheetham M.E., Brion J.P., Anderton B.H. Human homologues of the bacterial heat-shock protein dnaJ are preferentially expressed in neurons. Biochem. J. 248:1992;469-476.
    • (1992) Biochem. J. , vol.248 , pp. 469-476
    • Cheetham, M.E.1    Brion, J.P.2    Anderton, B.H.3
  • 9
    • 0027216523 scopus 로고
    • Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein
    • Chellaiah A., Davis A., Mohanakumar T. Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein. Biochim. Biophys. Acta. 1174:1993;111-113.
    • (1993) Biochim. Biophys. Acta , vol.1174 , pp. 111-113
    • Chellaiah, A.1    Davis, A.2    Mohanakumar, T.3
  • 10
    • 0030112717 scopus 로고    scopus 로고
    • Amplification and altered expression of the hsc70/U14 snoRNA gene in a heat resistant Chinese hamster cell line
    • Chen M.S., Featherstone T., Laszlo A. Amplification and altered expression of the hsc70/U14 snoRNA gene in a heat resistant Chinese hamster cell line. Cell Stress and Chaperones. 1:(1):1996;47-61.
    • (1996) Cell Stress and Chaperones , vol.1 , Issue.1 , pp. 47-61
    • Chen, M.S.1    Featherstone, T.2    Laszlo, A.3
  • 12
    • 0032571320 scopus 로고    scopus 로고
    • The role of DnaJ-like proteins in glucocorticoid receptor-hsp90 heterocomplex assembly by the reconstituted hsp90-p60-hsp70 fodosome complex
    • Dittmar K.D., Banach M., Galigniana M.D., Pratt W.B. The role of DnaJ-like proteins in glucocorticoid receptor-hsp90 heterocomplex assembly by the reconstituted hsp90-p60-hsp70 fodosome complex. J. Biol. Chem. 273:(13):1998;7358-7366.
    • (1998) J. Biol. Chem. , vol.273 , Issue.13 , pp. 7358-7366
    • Dittmar, K.D.1    Banach, M.2    Galigniana, M.D.3    Pratt, W.B.4
  • 13
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman J., Nimmesgern E., Ohtsuka K., Hart F.U. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature. 370:1994;111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hart, F.U.4
  • 14
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, hsp70, and hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover J.R., Lindquist S. Hsp104, hsp70, and hsp40: A novel chaperone system that rescues previously aggregated proteins. Cell. 94:1998;73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 15
    • 0024461263 scopus 로고
    • β-Internexin is a microtubule-associated protein identical to the 70-kDa heat-shock cognate protein and the clathrin uncoating ATPase
    • Green L.A.D., Liem R.K.H. β-Internexin is a microtubule-associated protein identical to the 70-kDa heat-shock cognate protein and the clathrin uncoating ATPase. J. Biol. Chem. 264:(26):1989;15210-15215.
    • (1989) J. Biol. Chem. , vol.264 , Issue.26 , pp. 15210-15215
    • Green, L.A.D.1    Liem, R.K.H.2
  • 16
    • 0032568541 scopus 로고    scopus 로고
    • Role of the J-domain in the cooperation of hsp40 with hsp70
    • Greene M.K., Moskos K., Landry S.J. Role of the J-domain in the cooperation of hsp40 with hsp70. Proc. Natl. Acad. Sci. USA. 95:1998;6108-6113.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6108-6113
    • Greene, M.K.1    Moskos, K.2    Landry, S.J.3
  • 17
    • 0030735086 scopus 로고    scopus 로고
    • Destablization of peptide binding and interdomain communication by an E543K mutation in the bovine 70-kDa heat shock cognate protein, a molecular chaperone
    • Ha J.H., Hellman U., Johnson E.R., Li L., McKay D.B., Sousa M.C., Takeda S., Wernstedt C., Wilbanks S.M. Destablization of peptide binding and interdomain communication by an E543K mutation in the bovine 70-kDa heat shock cognate protein, a molecular chaperone. J. Biol. Chem. 272:(44):1997;27796-27803.
    • (1997) J. Biol. Chem. , vol.272 , Issue.44 , pp. 27796-27803
    • Ha, J.H.1    Hellman, U.2    Johnson, E.R.3    Li, L.4    McKay, D.B.5    Sousa, M.C.6    Takeda, S.7    Wernstedt, C.8    Wilbanks, S.M.9
  • 18
    • 0030589609 scopus 로고    scopus 로고
    • Genomic cloning of a human heat shock protein 40 (hsp40) gene (HSPF1) and its chromosomal localization to 19p13.2
    • Hata M., Okumura K., Seto M., Ohtsuka K. Genomic cloning of a human heat shock protein 40 (hsp40) gene (HSPF1) and its chromosomal localization to 19p13.2. Genomics. 38:1996;446-449.
    • (1996) Genomics , vol.38 , pp. 446-449
    • Hata, M.1    Okumura, K.2    Seto, M.3    Ohtsuka, K.4
  • 19
    • 0032053658 scopus 로고    scopus 로고
    • Characterization of HSE sequences in human hsp40 gene: Structural and promoter analysis
    • Hata M., Ohtsuka K. Characterization of HSE sequences in human hsp40 gene: structural and promoter analysis. Biochim. Biophys. Acta. 1397:(1):1998;43-55.
    • (1998) Biochim. Biophys. Acta , vol.1397 , Issue.1 , pp. 43-55
    • Hata, M.1    Ohtsuka, K.2
  • 21
    • 15844372190 scopus 로고    scopus 로고
    • A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein
    • Karzai A.W., McMacken R. A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein. J. Biol. Chem. 271:(19):1996;11236-11246.
    • (1996) J. Biol. Chem. , vol.271 , Issue.19 , pp. 11236-11246
    • Karzai, A.W.1    McMacken, R.2
  • 22
    • 0032103439 scopus 로고    scopus 로고
    • The J-domain family and the recruitment of chaperone power
    • Kelley W.L. The J-domain family and the recruitment of chaperone power. Trends Biochem. Sci. 23:1998;222-227.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 222-227
    • Kelley, W.L.1
  • 23
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist S. The heat-shock response. Annu. Rev. Biochem. 55:1986;1151-1191.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 24
    • 0032561360 scopus 로고    scopus 로고
    • Protein folding activity of hsp70 is modified differentially by the hsp40 co-chaperones sis1 and ydj1
    • Lu Z., Cyr D.M. Protein folding activity of hsp70 is modified differentially by the hsp40 co-chaperones sis1 and ydj1. J. Biol. Chem. 273:(43):1998;27824-27830.
    • (1998) J. Biol. Chem. , vol.273 , Issue.43 , pp. 27824-27830
    • Lu, Z.1    Cyr, D.M.2
  • 25
    • 0032489556 scopus 로고    scopus 로고
    • The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist hsp70 in protein folding
    • Lu Z., Cyr D.M. The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist hsp70 in protein folding. J. Biol. Chem. 273:(10):1998;5970-5978.
    • (1998) J. Biol. Chem. , vol.273 , Issue.10 , pp. 5970-5978
    • Lu, Z.1    Cyr, D.M.2
  • 26
    • 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.T., Ohtsuka K., Bensaude O., Kampinga H.H. Hsp70 and hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells. J. Biol. Chem. 272:(52):1997;33283-33289.
    • (1997) J. Biol. Chem. , vol.272 , Issue.52 , pp. 33283-33289
    • Michels, A.A.1    Kanon, B.2    Konings, A.W.T.3    Ohtsuka, K.4    Bensaude, O.5    Kampinga, H.H.6
  • 27
    • 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., Hart F.-U. Regulation of the heat-shock protein 70 reaction cycle by the mammalian dnaJ homolog, hsp40. J. Biol. Chem. 271:(32):1996;19617-19624.
    • (1996) J. Biol. Chem. , vol.271 , Issue.32 , pp. 19617-19624
    • Minami, Y.1    Hohfeld, J.2    Ohtsuka, K.3    Hart, F.-U.4
  • 28
    • 0003720391 scopus 로고
    • R.I. Morimoto, A. Tissiers, & C. Georgopoulos. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press
    • Morimoto R.I., Tissiers A., Georgopoulos C. The Biology of Heat Shock Proteins and Molecular Chaperones. 1994;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones
  • 29
    • 0026526303 scopus 로고
    • Interaction of the immunosuppressant deoxyspergualin with a member of the hsp70 family of heat shock proteins
    • Nadler S.G., Tepper M.A., Schacter B., Mazzucco C.E. Interaction of the immunosuppressant deoxyspergualin with a member of the hsp70 family of heat shock proteins. Science. 258:1992;484-486.
    • (1992) Science , vol.258 , pp. 484-486
    • Nadler, S.G.1    Tepper, M.A.2    Schacter, B.3    Mazzucco, C.E.4
  • 30
    • 0027254681 scopus 로고
    • Human cDNA encoding dnaJ protein homologue
    • Oh S., Iwahori A., Kato S. Human cDNA encoding dnaJ protein homologue. Biochim. Biophys. Acta. 1174:1993;114-116.
    • (1993) Biochim. Biophys. Acta , vol.1174 , pp. 114-116
    • Oh, S.1    Iwahori, A.2    Kato, S.3
  • 31
    • 0023001202 scopus 로고
    • Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product
    • Ohki M., Tamura F., Nishimura S., Uchida H. Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product. J. Biol. Chem. 261:(4):1986;1778-1781.
    • (1986) J. Biol. Chem. , vol.261 , Issue.4 , pp. 1778-1781
    • Ohki, M.1    Tamura, F.2    Nishimura, S.3    Uchida, H.4
  • 32
    • 0027486385 scopus 로고
    • Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial dnaJ
    • Ohtsuka K. Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial dnaJ. Biochem. Biophys. Res. Commun. 197:(1):1993;235-240.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , Issue.1 , pp. 235-240
    • Ohtsuka, K.1
  • 33
    • 0033613957 scopus 로고    scopus 로고
    • Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells
    • Pei L. Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells. J. Biol. Chem. 274:(5):1999;3151-3158.
    • (1999) J. Biol. Chem. , vol.274 , Issue.5 , pp. 3151-3158
    • Pei, L.1
  • 34
    • 0028837979 scopus 로고
    • Interaction between hsp70 and hsp40, eukaryotic homologues of dnaK and dnaJ, in human cells expressing mutant p53
    • Sugito K., Yamane M., Hattori H., Hayashi Y., Tohnai I., Ueda M., Tsuchida N., Ohtsuka K. Interaction between hsp70 and hsp40, eukaryotic homologues of dnaK and dnaJ, in human cells expressing mutant p53. FEBS Lett. 358:1995;161-164.
    • (1995) FEBS Lett. , vol.358 , pp. 161-164
    • Sugito, K.1    Yamane, M.2    Hattori, H.3    Hayashi, Y.4    Tohnai, I.5    Ueda, M.6    Tsuchida, N.7    Ohtsuka, K.8
  • 35
    • 0030830249 scopus 로고    scopus 로고
    • The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding
    • Terada K., Kanazawa M., Bukau B., Mori M. The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding. J. Cell. Biol. 139:(5):1997;1089-1095.
    • (1997) J. Cell. Biol. , vol.139 , Issue.5 , pp. 1089-1095
    • Terada, K.1    Kanazawa, M.2    Bukau, B.3    Mori, M.4
  • 36
    • 0029871766 scopus 로고    scopus 로고
    • A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of hsp70 ATPase activity at a site distinct from substrate binding
    • Tsai J., Douglas M.G. A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of hsp70 ATPase activity at a site distinct from substrate binding. J. Biol. Chem. 271:(16):1996;9347-9354.
    • (1996) J. Biol. Chem. , vol.271 , Issue.16 , pp. 9347-9354
    • Tsai, J.1    Douglas, M.G.2
  • 37
    • 0029257254 scopus 로고
    • Heat-shock proteins hsp104 and hsp70 reactivate mRNA splicing after heat inactivation
    • Vogel J.L., Parsell D.A., Lindquist S. Heat-shock proteins hsp104 and hsp70 reactivate mRNA splicing after heat inactivation. Curr. Biol. 5:(3):1995;306-317.
    • (1995) Curr. Biol. , vol.5 , Issue.3 , pp. 306-317
    • Vogel, J.L.1    Parsell, D.A.2    Lindquist, S.3
  • 39
    • 0024268031 scopus 로고
    • Translation of unspliced transcripts after heat shock
    • Yost H.J., Lindquist S. Translation of unspliced transcripts after heat shock. Science. 242:1988;1544-1548.
    • (1988) Science , vol.242 , pp. 1544-1548
    • Yost, H.J.1    Lindquist, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.