메뉴 건너뛰기




Volumn 9, Issue 5, 2013, Pages 307-312

ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; B RAF KINASE; CYCLIN DEPENDENT KINASE 4; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; ERLOTINIB; HEAT SHOCK PROTEIN 90; LAPATINIB; SORAFENIB; VEMURAFENIB;

EID: 84879098944     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1212     Document Type: Article
Times cited : (119)

References (48)
  • 1
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl, L.H. & Prodromou, C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75, 271-294 (2006).
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 2
    • 12344291243 scopus 로고    scopus 로고
    • Hsp90 and Cdc37-A chaperone cancer conspiracy
    • Pearl, L.H. Hsp90 and Cdc37-a chaperone cancer conspiracy. Curr. Opin. Genet. Dev. 15, 55-61 (2005).
    • (2005) Curr. Opin. Genet. Dev , vol.15 , pp. 55-61
    • Pearl, L.H.1
  • 3
    • 33846651282 scopus 로고    scopus 로고
    • Molecular chaperones and protein kinase quality control
    • Caplan, A.J., Mandal, A.K. & Theodoraki, M.A. Molecular chaperones and protein kinase quality control. Trends Cell Biol. 17, 87-92 (2007).
    • (2007) Trends Cell Biol , vol.17 , pp. 87-92
    • Caplan, A.J.1    Mandal, A.K.2    Theodoraki, M.A.3
  • 4
    • 38449090443 scopus 로고    scopus 로고
    • Cdc37 regulation of the kinome: When to hold 'em and when to fold 'em
    • Karnitz, L.M. & Felts, S.J. Cdc37 regulation of the kinome: when to hold 'em and when to fold 'em. Sci. STKE 2007, pe22 (2007).
    • (2007) Sci. STKE , vol.2007
    • Karnitz, L.M.1    Felts, S.J.2
  • 5
    • 0742269688 scopus 로고    scopus 로고
    • The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)
    • Roe, S.M. et al. The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37). Cell 116, 87-98 (2004).
    • (2004) Cell , vol.116 , pp. 87-98
    • Roe, S.M.1
  • 6
    • 33747878717 scopus 로고    scopus 로고
    • Structure of an Hsp90-Cdc37-Cdk4 complex
    • Vaughan, C.K. et al. Structure of an Hsp90-Cdc37-Cdk4 complex. Mol. Cell 23, 697-707 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 697-707
    • Vaughan, C.K.1
  • 7
    • 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
  • 8
    • 0029963674 scopus 로고    scopus 로고
    • Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90
    • Schneider, C. et al. Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90. Proc. Natl. Acad. Sci. USA 93, 14536-14541 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14536-14541
    • Schneider, C.1
  • 9
    • 34447507818 scopus 로고    scopus 로고
    • Inhibitors of the heat shock response: Biology and pharmacology
    • Powers, M.V. & Workman, P. Inhibitors of the heat shock response: biology and pharmacology. FEBS Lett. 581, 3758-3769 (2007).
    • (2007) FEBS Lett , vol.581 , pp. 3758-3769
    • Powers, M.V.1    Workman, P.2
  • 10
    • 41149111451 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone: An open and shut case for treatment
    • Pearl, L.H., Prodromou, C. & Workman, P. The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem. J. 410, 439-453 (2008).
    • (2008) Biochem. J , vol.410 , pp. 439-453
    • Pearl, L.H.1    Prodromou, C.2    Workman, P.3
  • 11
    • 84857053558 scopus 로고    scopus 로고
    • The role of Hsp90 in protein complex assembly
    • Makhnevych, T. & Houry, W.A. The role of Hsp90 in protein complex assembly. Biochim. Biophys. Acta 1823, 674-682 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 674-682
    • Makhnevych, T.1    Houry, W.A.2
  • 12
    • 0031127737 scopus 로고    scopus 로고
    • Cdc37: A protein kinase chaperone?
    • Hunter, T. & Poon, R.Y.C. Cdc37: A protein kinase chaperone? Trends Cell Biol. 7, 157-161 (1997).
    • (1997) Trends Cell Biol. , vol.7 , pp. 157-161
    • Hunter, T.1    Poon, R.Y.C.2
  • 13
    • 25444501262 scopus 로고    scopus 로고
    • A client-binding site of Cdc37
    • Terasawa, K. & Minami, Y. A client-binding site of Cdc37. FEBS J. 272, 4684-4690 (2005).
    • (2005) FEBS J. , vol.272 , pp. 4684-4690
    • Terasawa, K.1    Minami, Y.2
  • 14
    • 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
  • 15
    • 4544254444 scopus 로고    scopus 로고
    • Definition of protein kinase sequence motifs that trigger high affinity binding of Hsp90 and Cdc37
    • Prince, T. & Matts, R.L. Definition of protein kinase sequence motifs that trigger high affinity binding of Hsp90 and Cdc37. J. Biol. Chem. 279, 39975-39981 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 39975-39981
    • Prince, T.1    Matts, R.L.2
  • 16
    • 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
  • 17
    • 27744551993 scopus 로고    scopus 로고
    • Exposure of protein kinase motifs that trigger binding of Hsp90 and Cdc37
    • Prince, T. & Matts, R.L. Exposure of protein kinase motifs that trigger binding of Hsp90 and Cdc37. Biochem. Biophys. Res. Commun. 338, 1447-1454 (2005).
    • (2005) Biochem. Biophys. Res. Commun , vol.338 , pp. 1447-1454
    • Prince, T.1    Matts, R.L.2
  • 18
    • 15544372341 scopus 로고    scopus 로고
    • Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex
    • Xu, W. et al. Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex. Nat. Struct. Mol. Biol. 12, 120-126 (2005).
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 120-126
    • Xu, W.1
  • 19
    • 28244444919 scopus 로고    scopus 로고
    • Activated B-RAF is an Hsp90 client protein that is targeted by the anticancer drug 17-allylamino-17-demethoxygeldanamycin
    • da Rocha Dias, S. et al. Activated B-RAF is an Hsp90 client protein that is targeted by the anticancer drug 17-allylamino-17-demethoxygeldanamycin. Cancer Res. 65, 10686-10691 (2005).
    • (2005) Cancer Res , vol.65 , pp. 10686-10691
    • Da Rocha Dias, S.1
  • 20
    • 30444441778 scopus 로고    scopus 로고
    • V600E B-Raf requires the Hsp90 chaperone for stability and is degraded in response to Hsp90 inhibitors
    • Grbovic, O.M. et al. V600E B-Raf requires the Hsp90 chaperone for stability and is degraded in response to Hsp90 inhibitors. Proc. Natl. Acad. Sci. USA 103, 57-62 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 57-62
    • Grbovic, O.M.1
  • 21
    • 42949149240 scopus 로고    scopus 로고
    • Discovery of a selective inhibitor of oncogenic B-Raf kinase with potent antimelanoma activity
    • Tsai, J. et al. Discovery of a selective inhibitor of oncogenic B-Raf kinase with potent antimelanoma activity. Proc. Natl. Acad. Sci. USA 105, 3041-3046 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3041-3046
    • Tsai, J.1
  • 22
    • 34248166042 scopus 로고    scopus 로고
    • Inhibition of the heat shock protein 90 molecular chaperone in vitro and in vivo by novel, synthetic, potent resorcinylic pyrazole/isoxazole amide analogues
    • Sharp, S.Y. et al. Inhibition of the heat shock protein 90 molecular chaperone in vitro and in vivo by novel, synthetic, potent resorcinylic pyrazole/isoxazole amide analogues. Mol. Cancer Ther. 6, 1198-1211 (2007).
    • (2007) Mol. Cancer Ther , vol.6 , pp. 1198-1211
    • Sharp, S.Y.1
  • 23
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L.N., Noble, M.E.M. & Owen, D.J. Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158 (1996).
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 24
    • 67649726156 scopus 로고    scopus 로고
    • Protein kinase inhibitors: Contributions from structure to clinical compounds
    • Johnson, L.N. Protein kinase inhibitors: contributions from structure to clinical compounds. Q. Rev. Biophys. 42, 1-40 (2009).
    • (2009) Q. Rev. Biophys , vol.42 , pp. 1-40
    • Johnson, L.N.1
  • 25
    • 33646269303 scopus 로고    scopus 로고
    • Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases
    • Terasawa, K. et al. Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases. Mol. Cell Biol. 26, 3378-3389 (2006).
    • (2006) Mol. Cell Biol , vol.26 , pp. 3378-3389
    • Terasawa, K.1
  • 26
    • 44649110104 scopus 로고    scopus 로고
    • Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding
    • Polier, S., Dragovic, Z., Hartl, F.U. & Bracher, A. Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 133, 1068-1079 (2008).
    • (2008) Cell , vol.133 , pp. 1068-1079
    • Polier, S.1    Dragovic, Z.2    Hartl, F.U.3    Bracher, A.4
  • 27
    • 0033815252 scopus 로고    scopus 로고
    • Insights into nucleotide binding in protein kinase A using fluorescent adenosine derivatives
    • Ni, Q., Shaffer, J. & Adams, J.A. Insights into nucleotide binding in protein kinase A using fluorescent adenosine derivatives. Protein Sci. 9, 1818-1827 (2000).
    • (2000) Protein Sci , vol.9 , pp. 1818-1827
    • Ni, Q.1    Shaffer, J.2    Adams, J.A.3
  • 28
    • 77949685981 scopus 로고    scopus 로고
    • RAF inhibitors prime wild-type RAF to activate the MAPK pathway and enhance growth
    • Hatzivassiliou, G. et al. RAF inhibitors prime wild-type RAF to activate the MAPK pathway and enhance growth. Nature 464, 431-435 (2010).
    • (2010) Nature , vol.464 , pp. 431-435
    • Hatzivassiliou, G.1
  • 29
    • 77957089182 scopus 로고    scopus 로고
    • The RAF inhibitor PLX4032 inhibits ERK signaling and tumor cell proliferation in a V600E BRAF-selective manner
    • Joseph, E.W. et al. The RAF inhibitor PLX4032 inhibits ERK signaling and tumor cell proliferation in a V600E BRAF-selective manner. Proc. Natl. Acad. Sci. USA 107, 14903-14908 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 14903-14908
    • Joseph, E.W.1
  • 30
    • 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
  • 31
    • 0034675919 scopus 로고    scopus 로고
    • Activation of B-Raf kinase requires phosphorylation of the conserved residues Thr598 and Ser601
    • Zhang, B.H. & Guan, K.L. Activation of B-Raf kinase requires phosphorylation of the conserved residues Thr598 and Ser601. EMBO J. 19, 5429-5439 (2000).
    • (2000) EMBO J. , vol.19 , pp. 5429-5439
    • Zhang, B.H.1    Guan, K.L.2
  • 32
    • 12144289677 scopus 로고    scopus 로고
    • Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF
    • Wan, P.T. et al. Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF. Cell 116, 855-867 (2004).
    • (2004) Cell , vol.116 , pp. 855-867
    • Wan, P.T.1
  • 33
    • 33845730781 scopus 로고    scopus 로고
    • Demonstration of a genetic therapeutic index for tumors expressing oncogenic BRAF by the kinase inhibitor SB-590885
    • King, A.J. et al. Demonstration of a genetic therapeutic index for tumors expressing oncogenic BRAF by the kinase inhibitor SB-590885. Cancer Res. 66, 11100-11105 (2006).
    • (2006) Cancer Res , vol.66 , pp. 11100-11105
    • King, A.J.1
  • 34
    • 0033974108 scopus 로고    scopus 로고
    • Cdc37 promotes the stability of protein kinases Cdc28 and Cak1
    • Farrell, A. & Morgan, D.O. Cdc37 promotes the stability of protein kinases Cdc28 and Cak1. Mol. Cell Biol. 20, 749-754 (2000).
    • (2000) Mol. Cell Biol , vol.20 , pp. 749-754
    • Farrell, A.1    Morgan, D.O.2
  • 35
    • 52249108496 scopus 로고    scopus 로고
    • Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37
    • Vaughan, C.K. et al. Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37. Mol. Cell 31, 886-895 (2008).
    • (2008) Mol. Cell , vol.31 , pp. 886-895
    • Vaughan, C.K.1
  • 36
    • 58249112898 scopus 로고    scopus 로고
    • Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitors
    • Smith, J.R., Clarke, P.A., de Billy, E. & Workman, P. Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitors. Oncogene 28, 157-169 (2009).
    • (2009) Oncogene , vol.28 , pp. 157-169
    • Smith, J.R.1    Clarke, P.A.2    De Billy, E.3    Workman, P.4
  • 37
    • 84864910544 scopus 로고    scopus 로고
    • Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50CDC37-AHA1 chaperone machine
    • Xu, W. et al. Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50CDC37-AHA1 chaperone machine. Mol. Cell 47, 434-443 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 434-443
    • Xu, W.1
  • 38
    • 84865695733 scopus 로고    scopus 로고
    • Quantitative analysis of hsp90-client interactions reveals principles of substrate recognition
    • Taipale, M. et al. Quantitative analysis of hsp90-client interactions reveals principles of substrate recognition. Cell 150, 987-1001 (2012).
    • (2012) Cell , vol.150 , pp. 987-1001
    • Taipale, M.1
  • 39
    • 15844382550 scopus 로고    scopus 로고
    • STI571 (Glivec) inhibits the interaction between c-KIT and heat shock protein 90 of the gastrointestinal stromal tumor cell line, GIST-T1
    • Nakatani, H. et al. STI571 (Glivec) inhibits the interaction between c-KIT and heat shock protein 90 of the gastrointestinal stromal tumor cell line, GIST-T1. Cancer Sci. 96, 116-119 (2005).
    • (2005) Cancer Sci , vol.96 , pp. 116-119
    • Nakatani, H.1
  • 40
    • 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
  • 41
    • 84873728334 scopus 로고    scopus 로고
    • Modelling vemurafenib resistance in melanoma reveals a strategy to forestall drug resistance
    • Das Thakur, M. et al. Modelling vemurafenib resistance in melanoma reveals a strategy to forestall drug resistance. Nature 494, 251-255 (2013).
    • (2013) Nature , vol.494 , pp. 251-255
    • Das Thakur, M.1
  • 42
    • 77956030786 scopus 로고    scopus 로고
    • Inhibition of mutated, activated BRAF in metastatic melanoma
    • Flaherty, K.T. et al. Inhibition of mutated, activated BRAF in metastatic melanoma. N. Engl. J. Med. 363, 809-819 (2010).
    • (2010) N. Engl. J. Med , vol.363 , pp. 809-819
    • Flaherty, K.T.1
  • 43
    • 77956513286 scopus 로고    scopus 로고
    • Clinical efficacy of a RAF inhibitor needs broad target blockade in BRAF-mutant melanoma
    • Bollag, G. et al. Clinical efficacy of a RAF inhibitor needs broad target blockade in BRAF-mutant melanoma. Nature 467, 596-599 (2010).
    • (2010) Nature , vol.467 , pp. 596-599
    • Bollag, G.1
  • 45
    • 84857030102 scopus 로고    scopus 로고
    • Engineering human MEK-1 for structural studies: A case study of combinatorial domain hunting
    • Meier, C. et al. Engineering human MEK-1 for structural studies: a case study of combinatorial domain hunting. J. Struct. Biol. 177, 329-334 (2012).
    • (2012) J. Struct. Biol , vol.177 , pp. 329-334
    • Meier, C.1
  • 46
    • 57649215437 scopus 로고    scopus 로고
    • A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s
    • Vaughan, C.K., Piper, P.W., Pearl, L.H. & Prodromou, C. A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s. FEBS J. 276, 199-209 (2009).
    • (2009) FEBS J. , vol.276 , pp. 199-209
    • Vaughan, C.K.1    Piper, P.W.2    Pearl, L.H.3    Prodromou, C.4
  • 48
    • 0031962973 scopus 로고    scopus 로고
    • In vitro circumvention of cisplatin resistance by the novel sterically hindered platinum complex AMD473
    • Holford, J., Sharp, S.Y., Murrer, B.A., Abrams, M. & Kelland, L.R. in vitro circumvention of cisplatin resistance by the novel sterically hindered platinum complex AMD473. Br. J. Cancer 77, 366-373 (1998).
    • (1998) Br. J. Cancer , vol.77 , pp. 366-373
    • Holford, J.1    Sharp, S.Y.2    Murrer, B.A.3    Abrams, M.4    Kelland, L.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.