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Volumn 404, Issue 1, 2007, Pages 159-167

Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions

Author keywords

Heat shock protein; Hop; Molecular chaperone; Tetratricopeptide repeat domain

Indexed keywords

HEAT SHOCK PROTEIN (HSP); MOLECULAR CHAPERONE; MUTANTS; MUTATIONS;

EID: 34249041590     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070084     Document Type: Article
Times cited : (69)

References (45)
  • 1
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell, L. and Lindquist, S. L. (2005) HSP90 and the chaperoning of cancer. Nat. Rev. Cancer 5, 761-772
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 2
    • 20044382800 scopus 로고    scopus 로고
    • Navigating the chaperone network: An integrative map of physical and genetic interactions mediated by the hsp90 chaperone
    • Zhao, R., Davey, M., Hsu, Y. C., Kaplanek, P., Tong, A., Parsons, A. B., Krogan, N., Cagney, G., Mai, D., Greenblatt, J. et al. (2005) Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120, 715-727
    • (2005) Cell , vol.120 , pp. 715-727
    • Zhao, R.1    Davey, M.2    Hsu, Y.C.3    Kaplanek, P.4    Tong, A.5    Parsons, A.B.6    Krogan, N.7    Cagney, G.8    Mai, D.9    Greenblatt, J.10
  • 3
    • 18944365231 scopus 로고    scopus 로고
    • A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p)
    • Millson, S. H., Truman, A. W., King, V., Prodromou, C., Pearl, L. H. and Piper, P. W. (2005) A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p). Eukaryotic Cell 4, 849-860
    • (2005) Eukaryotic Cell , vol.4 , pp. 849-860
    • Millson, S.H.1    Truman, A.W.2    King, V.3    Prodromou, C.4    Pearl, L.H.5    Piper, P.W.6
  • 4
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt, W. B. and Toft, D. O. (2003) Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. 228, 111-133
    • (2003) Exp. Biol. Med , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 5
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the hsp90 molecular chaperone machinery
    • Pearl, L. H. and Prodromou, C. (2006) Structure and mechanism of the hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75, 271-294
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 7
    • 0037023732 scopus 로고    scopus 로고
    • HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor
    • Hernandez, M. P., Chadli, A. and Toft, D. O. (2002) HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor. J. Biol. Chem. 277, 11873-11881
    • (2002) J. Biol. Chem , vol.277 , pp. 11873-11881
    • Hernandez, M.P.1    Chadli, A.2    Toft, D.O.3
  • 8
    • 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. (2002) The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex. J. Biol. Chem. 277, 38294-38304
    • (2002) J. Biol. Chem , vol.277 , pp. 38294-38304
    • Hernandez, M.P.1    Sullivan, W.P.2    Toft, D.O.3
  • 11
    • 0037518202 scopus 로고    scopus 로고
    • Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the ATPase cycle
    • Richter, K., Muschler, P., Hainzl, O., Reinstein, J. and Buchner, J. (2003) Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the ATPase cycle. J. Biol. Chem. 278, 10328-10333
    • (2003) J. Biol. Chem , vol.278 , pp. 10328-10333
    • Richter, K.1    Muschler, P.2    Hainzl, O.3    Reinstein, J.4    Buchner, J.5
  • 12
    • 33846181647 scopus 로고    scopus 로고
    • Nucleotide-dependent interaction of S. cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1
    • Johnson, J. L., Halas, A. and Flom, G. (2007) Nucleotide-dependent interaction of S. cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1. Mol. Cell. Biol. 27, 768-776
    • (2007) Mol. Cell. Biol , vol.27 , pp. 768-776
    • Johnson, J.L.1    Halas, A.2    Flom, G.3
  • 13
    • 0034329452 scopus 로고    scopus 로고
    • Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
    • Young, J. C. and Hartl, F. U. (2000) Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. EMBO J. 19, 5930-5940
    • (2000) EMBO J , vol.19 , pp. 5930-5940
    • Young, J.C.1    Hartl, F.U.2
  • 15
    • 7044240678 scopus 로고    scopus 로고
    • Hop: More than an Hsp70/Hsp90 adaptor protein
    • Odunuga, O. O., Longshaw, V. M. and Blatch, G. L. (2004) Hop: more than an Hsp70/Hsp90 adaptor protein. BioEssays 26, 1058-1068
    • (2004) BioEssays , vol.26 , pp. 1058-1068
    • Odunuga, O.O.1    Longshaw, V.M.2    Blatch, G.L.3
  • 16
    • 3543037605 scopus 로고    scopus 로고
    • Tetratricopeptide repeat cochaperones in steroid receptor complexes
    • Smith, D. F. (2004) Tetratricopeptide repeat cochaperones in steroid receptor complexes. Cell Stress Chaperones 9, 109-121
    • (2004) Cell Stress Chaperones , vol.9 , pp. 109-121
    • Smith, D.F.1
  • 17
    • 0032541163 scopus 로고    scopus 로고
    • Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90
    • Young, J. C., Obermann, W. M. and Hartl, F. U. (1998) Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90. J. Biol. Chem. 273, 18007-18010
    • (1998) J. Biol. Chem , vol.273 , pp. 18007-18010
    • Young, J.C.1    Obermann, W.M.2    Hartl, F.U.3
  • 18
    • 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. (1998) The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors. Mol. Cell. Biol. 18, 2023-2028
    • (1998) Mol. Cell. Biol , vol.18 , pp. 2023-2028
    • Demand, J.1    Luders, J.2    Hohfeld, J.3
  • 19
    • 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. (2000) Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101, 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
  • 22
  • 23
    • 0032567434 scopus 로고    scopus 로고
    • Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
    • Chen, S. and Smith, D. F. (1998) Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery. J. Biol. Chem. 273, 35194-35200
    • (1998) J. Biol. Chem , vol.273 , pp. 35194-35200
    • Chen, S.1    Smith, D.F.2
  • 24
    • 0031013723 scopus 로고    scopus 로고
    • In vivo analysis of the Hsp90 cochaperone Sti1 (p60)
    • Chang, H. C., Nathan, D. F. and Lindquist, S. (1997) In vivo analysis of the Hsp90 cochaperone Sti1 (p60). Mol. Cell. Biol. 17, 318-325
    • (1997) Mol. Cell. Biol , vol.17 , pp. 318-325
    • Chang, H.C.1    Nathan, D.F.2    Lindquist, S.3
  • 25
    • 33644746255 scopus 로고    scopus 로고
    • Effect of mutation of the tetratricopeptide repeat and aspartate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae
    • Flom, G., Weekes, J., Williams, J. J. and Johnson, J. L. (2006) Effect of mutation of the tetratricopeptide repeat and aspartate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae. Genetics 172, 41-51
    • (2006) Genetics , vol.172 , pp. 41-51
    • Flom, G.1    Weekes, J.2    Williams, J.J.3    Johnson, J.L.4
  • 26
    • 26644453716 scopus 로고    scopus 로고
    • Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1)
    • Song, Y. and Masison, D. C. (2005) Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1). J. Biol. Chem. 280, 34178-34185
    • (2005) J. Biol. Chem , vol.280 , pp. 34178-34185
    • Song, Y.1    Masison, D.C.2
  • 27
    • 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, B., Pugh, D. J. and Blatch, G. L. (2003) Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity. J. Biol. Chem. 278, 6896-6904
    • (2003) J. Biol. Chem , vol.278 , pp. 6896-6904
    • Odunuga, O.O.1    Hornby, J.A.2    Bies, C.3    Zimmermann, B.4    Pugh, D.J.5    Blatch, G.L.6
  • 29
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure
    • Gietz, R. D., Schiestl, R. H., Willems, A. R. and Woods, R. A. (1995) Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 11, 355-360
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4
  • 30
    • 0024469206 scopus 로고
    • Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae
    • Nicolet, C. M. and Craig, E. A. (1989) Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae. Mol. Cell. Biol. 9, 3638-3646
    • (1989) Mol. Cell. Biol , vol.9 , pp. 3638-3646
    • Nicolet, C.M.1    Craig, E.A.2
  • 31
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S. and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 32
    • 0028953840 scopus 로고
    • Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
    • Mumberg, D., Muller, R. and Funk, M. (1995) Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene 156, 119-122
    • (1995) Gene , vol.156 , pp. 119-122
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 33
    • 18844400606 scopus 로고    scopus 로고
    • In vivo bipartite interaction between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae
    • Aron, R., Lopez, N., Walter, W., Craig, E. A. and Johnson, J. (2005) In vivo bipartite interaction between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae. Genetics 169, 1873-1882
    • (2005) Genetics , vol.169 , pp. 1873-1882
    • Aron, R.1    Lopez, N.2    Walter, W.3    Craig, E.A.4    Johnson, J.5
  • 34
    • 0024421221 scopus 로고
    • hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
    • Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J. and Lindquist, S. (1989) hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol. Cell. Biol. 9, 3919-3930
    • (1989) Mol. Cell. Biol , vol.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farrelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 35
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • Guan, K. L. and Dixon, J. E. (1991) Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal. Biochem. 192, 262-267
    • (1991) Anal. Biochem , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 36
    • 0029872081 scopus 로고    scopus 로고
    • The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes
    • Johnson, J., Corbisier, R., Stensgard, B. and Toft, D. (1996) The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes. J. Steroid Biochem. Mol. Biol. 56, 31-37
    • (1996) J. Steroid Biochem. Mol. Biol , vol.56 , pp. 31-37
    • Johnson, J.1    Corbisier, R.2    Stensgard, B.3    Toft, D.4
  • 37
    • 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. (1996) Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70. Mol. Endocrinol. 10, 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
  • 38
    • 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. (2005) Functional comparison of human and Drosophila Hop reveals novel role in steroid receptor maturation. J. Biol. Chem. 280, 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
  • 39
    • 10644265069 scopus 로고    scopus 로고
    • Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle
    • Siligardi, G., Hu, B., Panaretou, B., Piper, P. W., Pearl, L. H. and Prodromou, C. (2004) Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle. J. Biol. Chem. 279, 51989-51998
    • (2004) J. Biol. Chem , vol.279 , pp. 51989-51998
    • Siligardi, G.1    Hu, B.2    Panaretou, B.3    Piper, P.W.4    Pearl, L.H.5    Prodromou, C.6
  • 40
    • 0034769599 scopus 로고    scopus 로고
    • Hsp104 interacts with Hsp90 cochaperones in respiring yeast
    • Abbas-Terki, T., Donze, O., Briand, P. A. and Picard, D. (2001) Hsp104 interacts with Hsp90 cochaperones in respiring yeast. Mol. Cell. Biol. 21, 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
  • 41
    • 0030462612 scopus 로고    scopus 로고
    • Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast
    • Louvion, J. F., Warth, R. and Picard, D. (1996) Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast. Proc. Natl. Acad. Sci. U.S.A. 93, 13937-13942
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 13937-13942
    • Louvion, J.F.1    Warth, R.2    Picard, D.3
  • 42
    • 0037352446 scopus 로고    scopus 로고
    • Structural and functional analysis of the middle segment of hsp90. Implications for ATP hydrolysis and client protein and cochaperone interactions
    • Meyer, P., Prodromou, C., Hu, B., Vaughan, C., Roe, S. M., Panaretou, B., Piper, P. W. and Pearl, L. H. (2003) Structural and functional analysis of the middle segment of hsp90. Implications for ATP hydrolysis and client protein and cochaperone interactions. Mol. Cell 11, 647-658
    • (2003) Mol. Cell , vol.11 , pp. 647-658
    • Meyer, P.1    Prodromou, C.2    Hu, B.3    Vaughan, C.4    Roe, S.M.5    Panaretou, B.6    Piper, P.W.7    Pearl, L.H.8
  • 44
    • 0031846768 scopus 로고    scopus 로고
    • Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants
    • Chen, S., Sullivan, W. P., Toft, D. O. and Smith, D. F. (1998) Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants. Cell Stress Chaperones 3, 118-129
    • (1998) Cell Stress Chaperones , vol.3 , pp. 118-129
    • Chen, S.1    Sullivan, W.P.2    Toft, D.O.3    Smith, D.F.4
  • 45
    • 33644500163 scopus 로고    scopus 로고
    • Domain-domain interactions within Hop, the Hsp70/Hsp90 organizing protein, are required for protein stability and structure
    • Carrigan, P. E., Sikkink, L. A., Smith, D. F. and Ramirez-Alvarado, M. (2006) Domain-domain interactions within Hop, the Hsp70/Hsp90 organizing protein, are required for protein stability and structure. Protein Sci. 15, 522-532
    • (2006) Protein Sci , vol.15 , pp. 522-532
    • Carrigan, P.E.1    Sikkink, L.A.2    Smith, D.F.3    Ramirez-Alvarado, M.4


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