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Volumn 12, Issue 2, 2005, Pages 120-126

Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CYCLOHEXIMIDE; EPIDERMAL GROWTH FACTOR RECEPTOR 2; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; MUTANT PROTEIN; PHOSPHOTRANSFERASE; BENZOQUINONE DERIVATIVE; EPIDERMAL GROWTH FACTOR RECEPTOR; MACROCYCLIC LACTAM; MULTIPROTEIN COMPLEX; QUINONE DERIVATIVE;

EID: 15544372341     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb885     Document Type: Article
Times cited : (134)

References (42)
  • 1
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the Hsp90/Hsp70-based chaperone machinery
    • Pratt, W.B. & Toft, D.O. Regulation of signaling protein function and trafficking by the Hsp90/Hsp70-based chaperone machinery. Exp. Biol. Med. 228, 111-133 (2003).
    • (2003) Exp. Biol. Med. , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 2
    • 0037064023 scopus 로고    scopus 로고
    • The assembly and intermolecular properties of the Hsp70-Hop-Hsp90 molecular chaperone complex
    • Hernandez, M.P., Sullivan, W.P. & Toft, D.O. The assembly and intermolecular properties of the Hsp70-Hop-Hsp90 molecular chaperone complex. J. Biol. Chem. 277, 38294-38304 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 38294-38304
    • Hernandez, M.P.1    Sullivan, W.P.2    Toft, D.O.3
  • 3
    • 0041315908 scopus 로고    scopus 로고
    • Visualization and mechanism of assembly of a glucocorticoid receptor. Hsp70 complex that is primed for subsequent Hsp90-dependent opening of the steroid binding cleft
    • Murphy, P.J. et al. Visualization and mechanism of assembly of a glucocorticoid receptor. Hsp70 complex that is primed for subsequent Hsp90-dependent opening of the steroid binding cleft. J. Biol. Chem. 278, 34764-34773 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 34764-34773
    • Murphy, P.J.1
  • 4
    • 0036303385 scopus 로고    scopus 로고
    • Stimulation of the weak ATPase activity of human Hsp90 by a client protein
    • McLaughlin, S.H., Smith, H.W. & Jackson, S.E. Stimulation of the weak ATPase activity of human Hsp90 by a client protein. J. Mol. Biol. 315, 787-798 (2002).
    • (2002) J. Mol. Biol. , vol.315 , pp. 787-798
    • McLaughlin, S.H.1    Smith, H.W.2    Jackson, S.E.3
  • 5
    • 0036931438 scopus 로고    scopus 로고
    • Activation of the ATPase activity of Hsp90 by the stress-regulated cochaperone aha1
    • Panaretou, B. et al. Activation of the ATPase activity of Hsp90 by the stress-regulated cochaperone aha1. Mol. Cell 10, 1307-1318 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 1307-1318
    • Panaretou, B.1
  • 6
    • 0030863995 scopus 로고    scopus 로고
    • The amino-terminal domain of heat shock protein 90 (Hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates Hsp90 conformation
    • Grenert, J.P. et al. The amino-terminal domain of heat shock protein 90 (Hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates Hsp90 conformation. J. Biol. Chem. 272, 23843-23850 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 23843-23850
    • Grenert, J.P.1
  • 7
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins, C.E. et al. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89, 239-250 (1997).
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1
  • 8
    • 3042598511 scopus 로고    scopus 로고
    • Biochemical and structural studies of the interaction of cdc37 with Hsp90
    • Zhang, W. et al. Biochemical and structural studies of the interaction of cdc37 with Hsp90. J. Mol. Biol. 340, 891-907 (2004).
    • (2004) J. Mol. Biol. , vol.340 , pp. 891-907
    • Zhang, W.1
  • 9
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • Sato, S., Fujita, N. & Tsuruo, T. Modulation of Akt kinase activity by binding to Hsp90. Proc. Natl. Acad. Sci. USA 97, 10832-10837 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 10
    • 0037036458 scopus 로고    scopus 로고
    • Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/ p50cdc37
    • Siligardi, G. et al. Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/ p50cdc37. J. Biol. Chem. 277, 20151-20159 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 20151-20159
    • Siligardi, G.1
  • 11
    • 0242349780 scopus 로고    scopus 로고
    • Functional dissection of cdc37: Characterization of domain structure and amino acid residues critical for protein kinase binding
    • Shao, J., Irwin, A., Hartson, S.D. & Matts, R.L. Functional dissection of cdc37: characterization of domain structure and amino acid residues critical for protein kinase binding. Biochemistry 42, 12577-12588 (2003).
    • (2003) Biochemistry , vol.42 , pp. 12577-12588
    • Shao, J.1    Irwin, A.2    Hartson, S.D.3    Matts, R.L.4
  • 12
    • 1842477464 scopus 로고    scopus 로고
    • Identification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4
    • Zhao, Q., Boschelli, F., Caplan, A.J. & Arndt, K.T. Identification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4. J. Biol. Chem. 279, 12560-12564 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 12560-12564
    • Zhao, Q.1    Boschelli, F.2    Caplan, A.J.3    Arndt, K.T.4
  • 13
    • 0029812759 scopus 로고    scopus 로고
    • Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin
    • Mimnaugh, E.G., Chavany, C. & Neckers, L. Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J. Biol. Chem. 271, 22796-22801 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 22796-22801
    • Mimnaugh, E.G.1    Chavany, C.2    Neckers, L.3
  • 14
    • 0034714283 scopus 로고    scopus 로고
    • Geldanamycin induces ErbB-2 degradation by proteolytic fragmentation
    • Tikhomirov, O. & Carpenter, G. Geldanamycin induces ErbB-2 degradation by proteolytic fragmentation. J. Biol. Chem. 275, 26625-26631 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 26625-26631
    • Tikhomirov, O.1    Carpenter, G.2
  • 15
    • 18444404925 scopus 로고    scopus 로고
    • Drug-induced ubiquitylation and degradation of ErbB receptor tyrosine kinases: Implications for cancer therapy
    • Citri, A. et al. Drug-induced ubiquitylation and degradation of ErbB receptor tyrosine kinases: implications for cancer therapy. EMBO J. 21, 2407-2417 (2002).
    • (2002) EMBO J. , vol.21 , pp. 2407-2417
    • Citri, A.1
  • 16
    • 0035793546 scopus 로고    scopus 로고
    • Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90
    • Xu, W. et al. Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J. Biol. Chem. 276, 3702-3708 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 3702-3708
    • Xu, W.1
  • 17
    • 37049183697 scopus 로고
    • Human breast cancer: Correlation of relapse and survival with amplification of the HER-2/neu oncogene
    • Slamon, D.J. et al. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science 235, 177-182 (1987).
    • (1987) Science , vol.235 , pp. 177-182
    • Slamon, D.J.1
  • 18
    • 0032952571 scopus 로고    scopus 로고
    • p53, c-erbB2, and PCNA status in benign, proliferative and malignant ovarian surface epithelial neoplasms: A study of 75 cases
    • Anreder, M.B., Freeman, S.M., Merogi, A., Halabi, S. & Marrogi, A.J. p53, c-erbB2, and PCNA status in benign, proliferative and malignant ovarian surface epithelial neoplasms: a study of 75 cases. Arch. Pathol. Lab. Med. 123, 310-316 (1999).
    • (1999) Arch. Pathol. Lab. Med. , vol.123 , pp. 310-316
    • Anreder, M.B.1    Freeman, S.M.2    Merogi, A.3    Halabi, S.4    Marrogi, A.J.5
  • 19
    • 0025139455 scopus 로고
    • Induction of a variety of tumors by c-erbB2 and clonal nature of lymphomas even with the mutated gene (Val659→Glu659)
    • Suda, Y. et al. Induction of a variety of tumors by c-erbB2 and clonal nature of lymphomas even with the mutated gene (Val659→Glu659). EMBO J. 9, 181-190 (1990).
    • (1990) EMBO J. , vol.9 , pp. 181-190
    • Suda, Y.1
  • 20
    • 0033022342 scopus 로고    scopus 로고
    • A mechanism for hormone-independent prostate cancer through modulation of androgen receptor signaling by the HER-2/neu tyrosine kinase
    • Craft, N., Shostak, Y., Carey, M. & Sawyers, C.L. A mechanism for hormone-independent prostate cancer through modulation of androgen receptor signaling by the HER-2/neu tyrosine kinase. Nat. Med. 5, 280-285 (1999).
    • (1999) Nat. Med. , vol.5 , pp. 280-285
    • Craft, N.1    Shostak, Y.2    Carey, M.3    Sawyers, C.L.4
  • 21
    • 0025940263 scopus 로고
    • Expression of activated rat neu oncogene is sufficient to induce experimental metastasis in 3T3 cells
    • Yu, D.H. & Hung, M.C. Expression of activated rat neu oncogene is sufficient to induce experimental metastasis in 3T3 cells. Oncogene 6, 1991-1996 (1991).
    • (1991) Oncogene , vol.6 , pp. 1991-1996
    • Yu, D.H.1    Hung, M.C.2
  • 22
    • 0035174126 scopus 로고    scopus 로고
    • The role of HER2 in angiogenesis
    • Kumar, R. & Yarmand-Bagheri, R. The role of HER2 in angiogenesis. Semin. Oncol. 28, 27-32 (2001).
    • (2001) Semin. Oncol. , vol.28 , pp. 27-32
    • Kumar, R.1    Yarmand-Bagheri, R.2
  • 23
    • 0037133672 scopus 로고    scopus 로고
    • Genetic instability favoring transversions associated with ErbB2-induced mammary tumorigenesis
    • Liu, S. et al. Genetic instability favoring transversions associated with ErbB2-induced mammary tumorigenesis. Proc. Natl. Acad. Sci. USA 99, 3770-3775 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3770-3775
    • Liu, S.1
  • 24
    • 0034794636 scopus 로고    scopus 로고
    • Overexpression of HER-2 as a resistance mechanism to hormonal therapy for breast cancer
    • Dowsett, M. Overexpression of HER-2 as a resistance mechanism to hormonal therapy for breast cancer. Endocr. Relat. Cancer 8, 191-195 (2001).
    • (2001) Endocr. Relat. Cancer , vol.8 , pp. 191-195
    • Dowsett, M.1
  • 25
    • 0032860819 scopus 로고    scopus 로고
    • Controlled dimerization of ErbB receptors provides evidence for differential signaling by homo- and heterodimers
    • Muthuswamy, S.K., Gilman, M. & Brugge, J.S. Controlled dimerization of ErbB receptors provides evidence for differential signaling by homo- and heterodimers. Mol. Cell. Biol. 19, 6845-6857 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6845-6857
    • Muthuswamy, S.K.1    Gilman, M.2    Brugge, J.S.3
  • 26
    • 0028233833 scopus 로고
    • Depletion of the erbB-2 gene product p185 by benzoquinoid ansamycins
    • Miller, P. et al. Depletion of the erbB-2 gene product p185 by benzoquinoid ansamycins. Cancer Res. 54, 2724-2730 (1994).
    • (1994) Cancer Res. , vol.54 , pp. 2724-2730
    • Miller, P.1
  • 27
    • 0033863883 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome
    • An, W.G., Schulte, T.W. & Neckers, L.M. The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome. Cell Growth Differ. 11, 355-360 (2000).
    • (2000) Cell Growth Differ. , vol.11 , pp. 355-360
    • An, W.G.1    Schulte, T.W.2    Neckers, L.M.3
  • 28
    • 0037224231 scopus 로고    scopus 로고
    • Identification of ErbB-2 kinase domain motifs required for geldanamycin-induced degradation
    • Tikhomirov, O. & Carpenter, G. Identification of ErbB-2 kinase domain motifs required for geldanamycin-induced degradation. Cancer Res. 63, 39-43 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 39-43
    • Tikhomirov, O.1    Carpenter, G.2
  • 30
    • 0141599428 scopus 로고    scopus 로고
    • Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor
    • Stamos, J., Sliwkowski, M.X. & Eigenbrot, C. Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. J. Biol. Chem. 277, 46265-46272 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 46265-46272
    • Stamos, J.1    Sliwkowski, M.X.2    Eigenbrot, C.3
  • 31
    • 0036461584 scopus 로고    scopus 로고
    • Hsp90, not Grp94, regulates the intracellular trafficking and stability of nascent ErbB2
    • Xu, W., Mimnaugh, E.G., Kim, J.S., Trepel, J.B. & Neckers, L.M. Hsp90, not Grp94, regulates the intracellular trafficking and stability of nascent ErbB2. Cell Stress Chaperones 7, 91-96 (2002).
    • (2002) Cell Stress Chaperones , vol.7 , pp. 91-96
    • Xu, W.1    Mimnaugh, E.G.2    Kim, J.S.3    Trepel, J.B.4    Neckers, L.M.5
  • 32
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • Isaacs, J.S., Xu, W. & Neckers, L. Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell 3, 213-217 (2003).
    • (2003) Cancer Cell , vol.3 , pp. 213-217
    • Isaacs, J.S.1    Xu, W.2    Neckers, L.3
  • 33
    • 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. et al. 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).
    • (2003) Mol. Cell , vol.11 , pp. 647-658
    • Meyer, P.1
  • 34
    • 0242318392 scopus 로고    scopus 로고
    • High affinity binding of Hsp90 is triggered by multiple discrete segments of its kinase clients
    • Scroggins, B.T. et al. High affinity binding of Hsp90 is triggered by multiple discrete segments of its kinase clients. Biochemistry 42, 12550-12561 (2003).
    • (2003) Biochemistry , vol.42 , pp. 12550-12561
    • Scroggins, B.T.1
  • 35
    • 1942486312 scopus 로고    scopus 로고
    • CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37
    • Miyata, Y. & Nishida, E. CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37. Mol. Cell. Biol. 24, 4065-4074 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4065-4074
    • Miyata, Y.1    Nishida, E.2
  • 36
    • 0141755381 scopus 로고    scopus 로고
    • Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37
    • Shao, J., Prince, T., Hartson, S.D. & Matts, R.L. Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37. J. Biol. Chem. 278, 38117-38120 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 38117-38120
    • Shao, J.1    Prince, T.2    Hartson, S.D.3    Matts, R.L.4
  • 37
    • 0029670034 scopus 로고    scopus 로고
    • p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/ GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2
    • Chavany, C. et al. p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/ GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2. J. Biol. Chem. 271, 4974-4977 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 4974-4977
    • Chavany, C.1
  • 38
    • 0344873345 scopus 로고    scopus 로고
    • On the role of structural information in remote homology detection and sequence alignment: New methods using hybrid sequence profiles
    • Tang, C.L. et al. On the role of structural information in remote homology detection and sequence alignment: new methods using hybrid sequence profiles. J. Mol. Biol. 334, 1043-1062 (2003).
    • (2003) J. Mol. Biol. , vol.334 , pp. 1043-1062
    • Tang, C.L.1
  • 39
    • 0035838974 scopus 로고    scopus 로고
    • Extending the accuracy limits of prediction for side-chain conformations
    • Xiang, Z. & Honig, B. Extending the accuracy limits of prediction for side-chain conformations. J. Mol. Biol. 311, 421-430 (2001).
    • (2001) J. Mol. Biol. , vol.311 , pp. 421-430
    • Xiang, Z.1    Honig, B.2
  • 40
    • 0037188507 scopus 로고    scopus 로고
    • Evaluating conformational free energies: The colony energy and its application to the problem of loop prediction
    • Xiang, Z., Soto, C.S. & Honig, B. Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction. Proc. Natl. Acad. Sci. USA 99, 7432-7437 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7432-7437
    • Xiang, Z.1    Soto, C.S.2    Honig, B.3
  • 41
    • 0034682851 scopus 로고    scopus 로고
    • An integrated approach to the analysis and modeling of protein sequences and structures. III. A comparative study of sequence conservation in protein structural families using multiple structural alignments
    • Yang, A.S. & Honig, B. An integrated approach to the analysis and modeling of protein sequences and structures. III. A comparative study of sequence conservation in protein structural families using multiple structural alignments. J. Mol. Biol. 301, 691-711 (2000).
    • (2000) J. Mol. Biol. , vol.301 , pp. 691-711
    • Yang, A.S.1    Honig, B.2
  • 42
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296 (1991).
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


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