메뉴 건너뛰기




Volumn 1783, Issue 6, 2008, Pages 1003-1014

Nuclear translocation of the phosphoprotein Hop (Hsp70/Hsp90 organizing protein) occurs under heat shock, and its proposed nuclear localization signal is involved in Hsp90 binding

Author keywords

Co chaperone; Heat shock protein; Hop; Hsp90; Nuclear localization signal; Phosphorylation

Indexed keywords

CELL EXTRACT; CYCLIN DEPENDENT KINASE 1; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; ISOPROTEIN; LEPTOMYCIN B; PHOSPHATE;

EID: 43549110056     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2008.01.014     Document Type: Article
Times cited : (47)

References (49)
  • 1
    • 0024469206 scopus 로고
    • Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae
    • Nicolet C.M., and Craig E.A. Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae. Mol. Cell. Biol. 9 (1989) 3638-3646
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3638-3646
    • Nicolet, C.M.1    Craig, E.A.2
  • 3
    • 0026640657 scopus 로고
    • Molecular cloning and expression of a transformation-sensitive human protein containing the TRP motif and sharing identity to the stress-inducible yeast protein STI1
    • Honoré B., Leffers H., Madsen P., Rasmussen H.H., Vandekerckhove J., and Celis J.E. Molecular cloning and expression of a transformation-sensitive human protein containing the TRP motif and sharing identity to the stress-inducible yeast protein STI1. J. Biol. Chem. 267 (1992) 8485-8491
    • (1992) J. Biol. Chem. , vol.267 , pp. 8485-8491
    • Honoré, B.1    Leffers, H.2    Madsen, P.3    Rasmussen, H.H.4    Vandekerckhove, J.5    Celis, J.E.6
  • 4
    • 0031036746 scopus 로고    scopus 로고
    • Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases
    • Lässle M., Blatch G.L., Kundra V., Takatori T., and Zetter B.R. Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases. J. Biol. Chem. 272 (1997) 1876-1884
    • (1997) J. Biol. Chem. , vol.272 , pp. 1876-1884
    • Lässle, M.1    Blatch, G.L.2    Kundra, V.3    Takatori, T.4    Zetter, B.R.5
  • 5
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt W.B., and Toft D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr. Rev. 18 (1997) 306-360
    • (1997) Endocr. Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 6
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., Hartl F.U., and Moarefi I. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101 (2000) 199-210
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 7
    • 0343471518 scopus 로고    scopus 로고
    • Isolation of a mouse cDNA encoding mSTI1, a stress-inducible protein containing the TPR motif
    • Blatch G.L., Lässle M., Zetter B.R., and Kundra V. Isolation of a mouse cDNA encoding mSTI1, a stress-inducible protein containing the TPR motif. Gene 194 (1997) 277-282
    • (1997) Gene , vol.194 , pp. 277-282
    • Blatch, G.L.1    Lässle, M.2    Zetter, B.R.3    Kundra, V.4
  • 8
    • 2642689664 scopus 로고    scopus 로고
    • The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors
    • Demand J., Luders J., and Hohfeld J. The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors. Mol. Cell. Biol. 18 (1998) 2023-2028
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2023-2028
    • Demand, J.1    Luders, J.2    Hohfeld, J.3
  • 10
  • 11
    • 0030880862 scopus 로고    scopus 로고
    • Molecular characterization of the heat-inducible LmSTI1 protein of Leishmania major
    • Webb J.R., Campos-Neto A., Skeiky Y.A.W., and Reed S.G. Molecular characterization of the heat-inducible LmSTI1 protein of Leishmania major. Mol. Biochem. Parasitol. 89 (1997) 179-193
    • (1997) Mol. Biochem. Parasitol. , vol.89 , pp. 179-193
    • Webb, J.R.1    Campos-Neto, A.2    Skeiky, Y.A.W.3    Reed, S.G.4
  • 12
    • 0036720897 scopus 로고    scopus 로고
    • Analysis of the complete genome sequence of the Hz-1 virus suggests that it is related to members of the Baculoviridae
    • Cheng C.H., Liu S.M., Chow T.Y., Hsiao Y.Y., Wang D.P., Huang J.J., and Chen H.H. Analysis of the complete genome sequence of the Hz-1 virus suggests that it is related to members of the Baculoviridae. J. Virol. 76 (2002) 9024-9034
    • (2002) J. Virol. , vol.76 , pp. 9024-9034
    • Cheng, C.H.1    Liu, S.M.2    Chow, T.Y.3    Hsiao, Y.Y.4    Wang, D.P.5    Huang, J.J.6    Chen, H.H.7
  • 13
    • 0034141290 scopus 로고    scopus 로고
    • Heat shock cognate protein 70 chaperone-binding site in the co-chaperone murine stress-inducible protein 1 maps to within three consecutive tetratricopeptide repeat motifs
    • van der Spuy J., Kana B.D., Dirr H.W., and Blatch G.L. Heat shock cognate protein 70 chaperone-binding site in the co-chaperone murine stress-inducible protein 1 maps to within three consecutive tetratricopeptide repeat motifs. Biochem. J. 345 (2000) 645-651
    • (2000) Biochem. J. , vol.345 , pp. 645-651
    • van der Spuy, J.1    Kana, B.D.2    Dirr, H.W.3    Blatch, G.L.4
  • 14
    • 0029885423 scopus 로고    scopus 로고
    • Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins Hsp90 and Hsp70
    • Chen S., Prapapanich V., Rimerman R.A., Honore B., and Smith D.F. Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins Hsp90 and Hsp70. Mol. Endocrinol. 10 (1996) 682-693
    • (1996) Mol. Endocrinol. , vol.10 , pp. 682-693
    • Chen, S.1    Prapapanich, V.2    Rimerman, R.A.3    Honore, B.4    Smith, D.F.5
  • 15
    • 0037470073 scopus 로고    scopus 로고
    • Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity
    • Odunuga O.O., Hornby J.A., Bies C., Zimmermann R., Pugh D.J., and Blatch G.L. Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity. J. Biol. Chem. 278 (2003) 6896-6904
    • (2003) J. Biol. Chem. , vol.278 , pp. 6896-6904
    • Odunuga, O.O.1    Hornby, J.A.2    Bies, C.3    Zimmermann, R.4    Pugh, D.J.5    Blatch, G.L.6
  • 17
    • 34249041590 scopus 로고    scopus 로고
    • Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions
    • Flom G., Behal R.H., Rosen L., Cole D.G., and Johnson J.L. Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions. Biochem. J. 404 (2007) 158-167
    • (2007) Biochem. J. , vol.404 , pp. 158-167
    • Flom, G.1    Behal, R.H.2    Rosen, L.3    Cole, D.G.4    Johnson, J.L.5
  • 18
    • 33644746255 scopus 로고    scopus 로고
    • Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae
    • Flom G., Weekes J., Williams J.J., and Johnson J.L. Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae. Genetics 172 (2006) 41-51
    • (2006) Genetics , vol.172 , pp. 41-51
    • Flom, G.1    Weekes, J.2    Williams, J.J.3    Johnson, J.L.4
  • 19
    • 15744373611 scopus 로고    scopus 로고
    • Functional comparison of human and drosophila Hop reveals novel role in steroid receptor maturation
    • Carrigan P.E., Riggs D.L., Chinkers M., and Smith D.F. Functional comparison of human and drosophila Hop reveals novel role in steroid receptor maturation. J. Biol. Chem. 280 (2005) 8906-8911
    • (2005) J. Biol. Chem. , vol.280 , pp. 8906-8911
    • Carrigan, P.E.1    Riggs, D.L.2    Chinkers, M.3    Smith, D.F.4
  • 22
    • 1342283935 scopus 로고    scopus 로고
    • Nuclear translocation of the Hsp70/Hsp90 organizing protein mSTI1 is regulated by cell cycle kinases
    • Longshaw V.M., Chapple J.P., Balda M.S., Cheetham M.E., and Blatch G.L. Nuclear translocation of the Hsp70/Hsp90 organizing protein mSTI1 is regulated by cell cycle kinases. J. Cell. Sci. 117 (2004) 701-710
    • (2004) J. Cell. Sci. , vol.117 , pp. 701-710
    • Longshaw, V.M.1    Chapple, J.P.2    Balda, M.S.3    Cheetham, M.E.4    Blatch, G.L.5
  • 23
    • 0034535451 scopus 로고    scopus 로고
    • The in vitro phosphorylation of the co-chaperone mSTI1 by cell cycle kinases substantiates a predicted casein kinase II-p34cdc2-NLS (CcN) motif
    • Longshaw V.M., Dirr H.W., Blatch G.L., and Lässle M. The in vitro phosphorylation of the co-chaperone mSTI1 by cell cycle kinases substantiates a predicted casein kinase II-p34cdc2-NLS (CcN) motif. Biol. Chem. 381 (2000) 1133-1138
    • (2000) Biol. Chem. , vol.381 , pp. 1133-1138
    • Longshaw, V.M.1    Dirr, H.W.2    Blatch, G.L.3    Lässle, M.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 27
    • 0023872192 scopus 로고
    • Establishment of mouse cells which constitutively secrete large quantities of interleukin 2, 3, 4, or 5, using modified cDNA expression vectors
    • Karasuyama H., and Melchers F. Establishment of mouse cells which constitutively secrete large quantities of interleukin 2, 3, 4, or 5, using modified cDNA expression vectors. Eur. J. Immunol. 18 (1988) 97-104
    • (1988) Eur. J. Immunol. , vol.18 , pp. 97-104
    • Karasuyama, H.1    Melchers, F.2
  • 28
    • 0034653375 scopus 로고    scopus 로고
    • Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha
    • Conti E., and Kuriyan J. Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha. Structure 8 (2000) 329-338
    • (2000) Structure , vol.8 , pp. 329-338
    • Conti, E.1    Kuriyan, J.2
  • 29
    • 0034646565 scopus 로고    scopus 로고
    • Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha
    • Fontes M.R., The T., and Kobe B. Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha. J. Mol. Biol. 297 (2000) 1183-1194
    • (2000) J. Mol. Biol. , vol.297 , pp. 1183-1194
    • Fontes, M.R.1    The, T.2    Kobe, B.3
  • 30
    • 33845196953 scopus 로고    scopus 로고
    • Nuclear localization signal and protein context mediate importin a specificity of nuclear import substrates
    • Friedrich B., Quensel C., Sommer T., Hartmann E., and Köhler M. Nuclear localization signal and protein context mediate importin a specificity of nuclear import substrates. Mol. Cell. Biol. 26 (2006) 8697-8709
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8697-8709
    • Friedrich, B.1    Quensel, C.2    Sommer, T.3    Hartmann, E.4    Köhler, M.5
  • 31
    • 0026550804 scopus 로고
    • The KKRKK Sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, Cofilin
    • Iida K., Matsumoto S., and Yahara I. The KKRKK Sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, Cofilin. Cell Struct. Funct. 17 (1992) 39-46
    • (1992) Cell Struct. Funct. , vol.17 , pp. 39-46
    • Iida, K.1    Matsumoto, S.2    Yahara, I.3
  • 32
    • 0032536820 scopus 로고    scopus 로고
    • Nuclear export of actin: a novel mechanism regulating the subcellular localization of a major cytoskeletal protein
    • Wada A., Fukuda M., Mishima M., and Nishida E. Nuclear export of actin: a novel mechanism regulating the subcellular localization of a major cytoskeletal protein. EMBO J. 17 (1998) 1635-1641
    • (1998) EMBO J. , vol.17 , pp. 1635-1641
    • Wada, A.1    Fukuda, M.2    Mishima, M.3    Nishida, E.4
  • 33
    • 0021398211 scopus 로고
    • Hsp70: nuclear concentration during environmental stress and cytoplasmic storage during recovery
    • Velazquez J.M., and Lindquist S. Hsp70: nuclear concentration during environmental stress and cytoplasmic storage during recovery. Cell 36 (1984) 655-662
    • (1984) Cell , vol.36 , pp. 655-662
    • Velazquez, J.M.1    Lindquist, S.2
  • 35
    • 0030601988 scopus 로고    scopus 로고
    • Localization of heat shock proteins in mouse male germ cells: an immunoelectron microscopical study
    • Biggiogera M., Tanguay R.M., Marin R., Wu Y., Martin T.E., and Fakan S. Localization of heat shock proteins in mouse male germ cells: an immunoelectron microscopical study. Exp. Cell Res. 229 (1996) 77-85
    • (1996) Exp. Cell Res. , vol.229 , pp. 77-85
    • Biggiogera, M.1    Tanguay, R.M.2    Marin, R.3    Wu, Y.4    Martin, T.E.5    Fakan, S.6
  • 36
    • 0037258854 scopus 로고    scopus 로고
    • Intracellular localization of the 90 kDA heat shock protein (HSP90alpha) determined by expression of a EGFP-HSP90alpha-fusion protein in unstressed and heat stressed 3T3 cells
    • Langer T., Rosmus S., and Fasold H. Intracellular localization of the 90 kDA heat shock protein (HSP90alpha) determined by expression of a EGFP-HSP90alpha-fusion protein in unstressed and heat stressed 3T3 cells. Cell Biol. Int. 27 (2003) 47-52
    • (2003) Cell Biol. Int. , vol.27 , pp. 47-52
    • Langer, T.1    Rosmus, S.2    Fasold, H.3
  • 37
    • 0025148825 scopus 로고
    • Protein phosphorylation and kinase activities in tumour cells after hyperthermia
    • Bagi G., and Hidvegi E.J. Protein phosphorylation and kinase activities in tumour cells after hyperthermia. Int. J. Radiat. Biol. 58 (1990) 633-650
    • (1990) Int. J. Radiat. Biol. , vol.58 , pp. 633-650
    • Bagi, G.1    Hidvegi, E.J.2
  • 38
    • 0028949615 scopus 로고
    • Proteins and temperature
    • Somero G.N. Proteins and temperature. Annu. Rev. Physiol. 57 (1995) 43-68
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 43-68
    • Somero, G.N.1
  • 39
    • 0028022750 scopus 로고
    • A novel kinase cascade triggered by chemical stress and heat shock which stimulates MAP kinase-activated protein kinase-2 and phosphorylation of the small heat shock proteins
    • Rouse J., Cohen P., Trigon S., Morange M., and Alonso-Llamazares A. A novel kinase cascade triggered by chemical stress and heat shock which stimulates MAP kinase-activated protein kinase-2 and phosphorylation of the small heat shock proteins. Cell 78 (1994) 1027-1037
    • (1994) Cell , vol.78 , pp. 1027-1037
    • Rouse, J.1    Cohen, P.2    Trigon, S.3    Morange, M.4    Alonso-Llamazares, A.5
  • 40
    • 0029619815 scopus 로고
    • Activation of mitogen-activated protein kinase by heat shock treatment in Drosophila
    • Chen F., Torres M., and Duncan R.F. Activation of mitogen-activated protein kinase by heat shock treatment in Drosophila. Biochem. J. 312 (1995) 341-349
    • (1995) Biochem. J. , vol.312 , pp. 341-349
    • Chen, F.1    Torres, M.2    Duncan, R.F.3
  • 41
    • 0028878242 scopus 로고
    • Heat treatment induces dephosphorylation of pRb and dissociation of T-antigen pRb complex during transforming infection with SV40
    • Khandijan E.W. Heat treatment induces dephosphorylation of pRb and dissociation of T-antigen pRb complex during transforming infection with SV40. Oncogene 10 (1995) 359-367
    • (1995) Oncogene , vol.10 , pp. 359-367
    • Khandijan, E.W.1
  • 44
    • 0031013723 scopus 로고    scopus 로고
    • In vivo analysis of the hsp90 cochaperone sti1 (p60)
    • Chang H.C.J., Nathan D.F., and Lindquist S. In vivo analysis of the hsp90 cochaperone sti1 (p60). Mol. Cell. Biol. 17 (1997) 318-325
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 318-325
    • Chang, H.C.J.1    Nathan, D.F.2    Lindquist, S.3
  • 45
    • 0037064023 scopus 로고    scopus 로고
    • The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex
    • Hernandez M.P., Sullivan W.P., and Toft D.O. The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex. J. Biol. Chem. 277 (2002) 38294-38304
    • (2002) J. Biol. Chem. , vol.277 , pp. 38294-38304
    • Hernandez, M.P.1    Sullivan, W.P.2    Toft, D.O.3
  • 46
    • 0034769599 scopus 로고    scopus 로고
    • Hsp104 interacts with Hsp90 cochaperones in respiring yeast
    • Abbas-Terki T., Donze O., Briand P.A., and Picard D. Hsp104 interacts with Hsp90 cochaperones in respiring yeast. Mol. Cell. Biol. 21 (2001) 7569-7575
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7569-7575
    • Abbas-Terki, T.1    Donze, O.2    Briand, P.A.3    Picard, D.4
  • 47
    • 0032491412 scopus 로고    scopus 로고
    • The chaperone cofactor hop/p60 interacts with the cytosolic chaperonin-containing TCP-1 and affects its nucleotide exchange and protein folding activities
    • Gebauer M., Melki R., and Gehring U. The chaperone cofactor hop/p60 interacts with the cytosolic chaperonin-containing TCP-1 and affects its nucleotide exchange and protein folding activities. J. Biol. Chem. 273 (1998) 29475-29480
    • (1998) J. Biol. Chem. , vol.273 , pp. 29475-29480
    • Gebauer, M.1    Melki, R.2    Gehring, U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.