메뉴 건너뛰기




Volumn 272, Issue 18, 2005, Pages 4684-4690

A client-binding site of Cdc37

Author keywords

Cdc37; Hsp90; Protein kinase; Raf 1

Indexed keywords

AMINO ACID; AURORA B KINASE; BINDING PROTEIN; CELL CYCLE PROTEIN 37; CHAPERONE; CHAPERONIN; CYCLIN DEPENDENT KINASE 1; CYCLIN DEPENDENT KINASE 2; CYCLIN DEPENDENT KINASE 4; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; MUTANT PROTEIN; PROTEIN KINASE; PROTEIN KINASE B; PROTEIN P50; RAF PROTEIN; UNCLASSIFIED DRUG;

EID: 25444501262     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04884.x     Document Type: Article
Times cited : (24)

References (43)
  • 1
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hatl FU & Hayer-Hartl M (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hatl, F.U.1    Hayer-Hartl, M.2
  • 2
    • 0033951278 scopus 로고    scopus 로고
    • Structure and in vivo function of Hsp90
    • Pearl LH & Prodromou C (2000) Structure and in vivo function of Hsp90. Curr Opin Struct Biol 10, 46-51.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 46-51
    • Pearl, L.H.1    Prodromou, C.2
  • 3
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • Young JC, Moarefi I & Hartl FU (2001) Hsp90: a specialized but essential protein-folding tool. J Cell Biol 154, 267-273.
    • (2001) J Cell Biol , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 4
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • Picard D (2002) Heat-shock protein 90, a chaperone for folding and regulation. Cell Mol Life Sci 59, 1640-1648.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 5
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt WB & Toft DO (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
  • 7
    • 20444371377 scopus 로고    scopus 로고
    • Constantly updated knowledge of Hsp90
    • Terasawa K, Minami M & Minami Y (2005) Constantly updated knowledge of Hsp90. J Biochem 137, 443-447.
    • (2005) J Biochem , vol.137 , pp. 443-447
    • Terasawa, K.1    Minami, M.2    Minami, Y.3
  • 8
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B & Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 10
    • 0031127737 scopus 로고    scopus 로고
    • Cdc37: A protein kinase chaperone?
    • Hunter T & Poon RYC (1997) Cdc37: a protein kinase chaperone? Trends Cell Biol 7, 157-161.
    • (1997) Trends Cell Biol , vol.7 , pp. 157-161
    • Hunter, T.1    Poon, R.Y.C.2
  • 11
    • 0042527167 scopus 로고    scopus 로고
    • Cdc37 goes beyond Hps90 and kinases
    • MacLean M & Picard D (2003) Cdc37 goes beyond Hps90 and kinases. Cell Stress Chaperones 8, 114-119.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 114-119
    • MacLean, M.1    Picard, D.2
  • 12
    • 12344291243 scopus 로고    scopus 로고
    • Hsp90 and Cdc37 - A chaperone cancer conspiracy
    • Pearl LH (2005) Hsp90 and Cdc37 - a chaperone cancer conspiracy. Curr Opin Genet Dev 15, 55-61.
    • (2005) Curr Opin Genet Dev , vol.15 , pp. 55-61
    • Pearl, L.H.1
  • 13
    • 0022574582 scopus 로고
    • Interaction of the Rous sarcoma virus protein pp60src with the cellular proteins pp50 and pp90
    • Brugge JS (1986) Interaction of the Rous sarcoma virus protein pp60src with the cellular proteins pp50 and pp90. Curr Top Microbiol Immunol 123, 1-22.
    • (1986) Curr Top Microbiol Immunol , vol.123 , pp. 1-22
    • Brugge, J.S.1
  • 14
    • 0027433644 scopus 로고
    • Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system
    • Stancato LF, Chow YH, Hutchison KA, Perdew GH, Jove R & Pratt WB (1993) Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system. J Biol Chem 268, 21711-21716.
    • (1993) J Biol Chem , vol.268 , pp. 21711-21716
    • Stancato, L.F.1    Chow, Y.H.2    Hutchison, K.A.3    Perdew, G.H.4    Jove, R.5    Pratt, W.B.6
  • 15
    • 0029838168 scopus 로고    scopus 로고
    • Physical interaction of mammalian CDC37 with CDK4
    • Dai K, Kobayashi R & Beach D (1996) Physical interaction of mammalian CDC37 with CDK4. J Biol Chem 271, 22030-22034.
    • (1996) J Biol Chem , vol.271 , pp. 22030-22034
    • Dai, K.1    Kobayashi, R.2    Beach, D.3
  • 16
    • 0029665779 scopus 로고    scopus 로고
    • Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
    • Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes Dev 10, 1491-1502.
    • (1996) Genes Dev , vol.10 , pp. 1491-1502
    • Stepanova, L.1    Leng, X.2    Parker, S.B.3    Harper, J.W.4
  • 17
    • 0032493624 scopus 로고    scopus 로고
    • cdc37 binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site
    • cdc37 binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site. J Biol Chem 273, 20090-20095.
    • (1998) J Biol Chem , vol.273 , pp. 20090-20095
    • Silverstein, A.M.1    Grammatikakis, N.2    Cochran, B.H.3    Chinkers, M.4    Pratt, W.B.5
  • 23
    • 0037164751 scopus 로고    scopus 로고
    • The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability
    • Lee P, Rao J, Fliss A, Yang E, Garrett S & Caplan AJ (2002) The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability. J Cell Biol 159, 1051-1059.
    • (2002) J Cell Biol , vol.159 , pp. 1051-1059
    • Lee, P.1    Rao, J.2    Fliss, A.3    Yang, E.4    Garrett, S.5    Caplan, A.J.6
  • 24
    • 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 SD & Matts RL (2003) Functional dissection of Cdc37: characterization of domain structure and amino acid residues critical for protein kinase binding. Biochemistry 42, 12577-12588.
    • (2003) Biochemistry , vol.42 , pp. 12577-12588
    • Shao, J.1    Irwin, A.2    Hartson, S.D.3    Matts, R.L.4
  • 25
    • 0036095375 scopus 로고    scopus 로고
    • Physical interaction of Cdc28 with Cdc37 in Saccharomyces cerevisiae
    • Mort-Bontemps-Soret M, Facca C & Paye G (2002) Physical interaction of Cdc28 with Cdc37 in Saccharomyces cerevisiae. Mol Genet Genomics 267, 447-458.
    • (2002) Mol Genet Genomics , vol.267 , pp. 447-458
    • Mort-Bontemps-Soret, M.1    Facca, C.2    Paye, G.3
  • 27
    • 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 AJ & Arndt KT (2004) Identification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4. J Biol Chem 279, 12560-12564.
    • (2004) J Biol Chem , vol.279 , pp. 12560-12564
    • Zhao, Q.1    Boschelli, F.2    Caplan, A.J.3    Arndt, K.T.4
  • 28
    • 4544254444 scopus 로고    scopus 로고
    • Definition of protein kinase sequence motifs that trigger high affinity binding of Hsp90 and Cdc37
    • Prince T & Matts RL (2004) Definition of protein kinase sequence motifs that trigger high affinity binding of Hsp90 and Cdc37. J Biol Chem 279, 39975-39981.
    • (2004) J Biol Chem , vol.279 , pp. 39975-39981
    • Prince, T.1    Matts, R.L.2
  • 30
    • 0035937187 scopus 로고    scopus 로고
    • Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor
    • Rao J, Lee P, Benzeno S, Cardozo C, Albertus J, Robins DM & Caplan AJ (2001) Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor. J Biol Chem 276, 5814-5820.
    • (2001) J Biol Chem , vol.276 , pp. 5814-5820
    • Rao, J.1    Lee, P.2    Benzeno, S.3    Cardozo, C.4    Albertus, J.5    Robins, D.M.6    Caplan, A.J.7
  • 31
    • 0042092020 scopus 로고    scopus 로고
    • Identification of Cdc37 as a novel regulator of the stress-responsive mitogen-activated protein kinase
    • Tatebe H & Shiozaki K (2003) Identification of Cdc37 as a novel regulator of the stress-responsive mitogen-activated protein kinase. Mol Cell Biol 23, 5132-5142.
    • (2003) Mol Cell Biol , vol.23 , pp. 5132-5142
    • Tatebe, H.1    Shiozaki, K.2
  • 32
    • 0030659844 scopus 로고    scopus 로고
    • Differential in vivo regulation of steroid hormone receptor activation by Cdc37
    • Fliss AE, Fang Y, Boschelli F & Caplan AJ (1997) Differential in vivo regulation of steroid hormone receptor activation by Cdc37. Mol Biol Cell 8, 2501-2509.
    • (1997) Mol Biol Cell , vol.8 , pp. 2501-2509
    • Fliss, A.E.1    Fang, Y.2    Boschelli, F.3    Caplan, A.J.4
  • 33
    • 0037025366 scopus 로고    scopus 로고
    • Role of p50/CDC37 is hepadnavirus assembly and replication
    • Wang X, Grammatikakis N & Hu J (2002) Role of p50/CDC37 is hepadnavirus assembly and replication. J Biol Chem 277, 24361-24367.
    • (2002) J Biol Chem , vol.277 , pp. 24361-24367
    • Wang, X.1    Grammatikakis, N.2    Hu, J.3
  • 34
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function
    • Basso AD, Solit DB, Chiosis G, Giri B, Tsichlis P & Rosen N (2002) Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J Biol Chem 277, 39858-39866.
    • (2002) J Biol Chem , vol.277 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 35
    • 0037107454 scopus 로고    scopus 로고
    • Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes
    • Lange BMH, Rebollo E, Herold A & Gonzalez C (2002) Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes. EMBO J 21, 5364-5374.
    • (2002) EMBO J , vol.21 , pp. 5364-5374
    • Lange, B.M.H.1    Rebollo, E.2    Herold, A.3    Gonzalez, C.4
  • 36
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks SK & Hunter T (1995) The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J 9, 576-596.
    • (1995) FASEB J , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 38
    • 0033974108 scopus 로고    scopus 로고
    • Cdc37 promotes the stability of protein kinases Cdc28 and Cak1
    • Farrell A & Morgan DO (2000) Cdc37 promotes the stability of protein kinases Cdc28 and Cak1. Mol Cell Biol 20, 749-754.
    • (2000) Mol Cell Biol , vol.20 , pp. 749-754
    • Farrell, A.1    Morgan, D.O.2
  • 39
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases: Controlling activity through activation segment conformation
    • Nolen B, Taylor S & Ghosh G (2004) Regulation of protein kinases: controlling activity through activation segment conformation. Mol Cell 15, 661-675.
    • (2004) Mol Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 40
    • 0028363670 scopus 로고
    • Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila
    • Cutforth T & Rubin GM (1994) Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. Cell 77, 1027-1036.
    • (1994) Cell , vol.77 , pp. 1027-1036
    • Cutforth, T.1    Rubin, G.M.2
  • 41
    • 0037474219 scopus 로고    scopus 로고
    • A positive feedback loop between protein kinase CKII and Cdc37 promotes the activity of multiple protein kinases
    • Bandhakavi S, McCann RO, Hanna DE & Glover CVC (2003) A positive feedback loop between protein kinase CKII and Cdc37 promotes the activity of multiple protein kinases. J Biol Chem 278, 2829-2836.
    • (2003) J Biol Chem , vol.278 , pp. 2829-2836
    • Bandhakavi, S.1    McCann, R.O.2    Hanna, D.E.3    Glover, C.V.C.4
  • 42
    • 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 SD & Matts RL (2003) Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37. J Biol Chem 278, 38117-38120.
    • (2003) J Biol Chem , vol.278 , pp. 38117-38120
    • Shao, J.1    Prince, T.2    Hartson, S.D.3    Matts, R.L.4
  • 43
    • 1942486312 scopus 로고    scopus 로고
    • CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37
    • Miyata Y & Nishida E (2004) CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37. Mol Cell Biol 24, 4065-4074.
    • (2004) Mol Cell Biol , vol.24 , pp. 4065-4074
    • Miyata, Y.1    Nishida, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.