메뉴 건너뛰기




Volumn 17, Issue 2, 2007, Pages 87-92

Molecular chaperones and protein kinase quality control

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN 37; CHAPERONE; ENZYME INHIBITOR; PROTEIN KINASE;

EID: 33846651282     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2006.12.002     Document Type: Review
Times cited : (161)

References (47)
  • 1
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: the role of molecular chaperones
    • Frydman J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70 (2001) 603-647
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 2
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L., and Lindquist S.L. HSP90 and the chaperoning of cancer. Nat. Rev. Cancer 5 (2005) 761-772
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 3
    • 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. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. (Maywood) 228 (2003) 111-133
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 4
    • 33646371494 scopus 로고    scopus 로고
    • Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones
    • Arlander S.J., et al. Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones. J. Biol. Chem. 281 (2006) 2989-2998
    • (2006) J. Biol. Chem. , vol.281 , pp. 2989-2998
    • Arlander, S.J.1
  • 5
    • 1642505452 scopus 로고    scopus 로고
    • Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase
    • Lee P., et al. Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase. Mol. Biol. Cell 15 (2004) 1785-1792
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1785-1792
    • Lee, P.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 (2006) 697-707
    • (2006) Mol. Cell , vol.23 , pp. 697-707
    • Vaughan, C.K.1
  • 7
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machine
    • Pearl L.H., and Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machine. Ann. Rev. Biochem. 75 (2006) 271-294
    • (2006) Ann. Rev. Biochem. , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 8
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • Manning G., et al. The protein kinase complement of the human genome. Science 298 (2002) 1912-1934
    • (2002) Science , vol.298 , pp. 1912-1934
    • Manning, G.1
  • 9
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; controlling activity through activation segment conformation
    • Nolen B., et al. Regulation of protein kinases; controlling activity through activation segment conformation. Mol. Cell 15 (2004) 661-675
    • (2004) Mol. Cell , vol.15 , pp. 661-675
    • Nolen, B.1
  • 10
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M., and Kuriyan J. The conformational plasticity of protein kinases. Cell 109 (2002) 275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 11
    • 0037436388 scopus 로고    scopus 로고
    • Dynamic features of cAMP-dependent protein kinase revealed by apoenzyme crystal structure
    • Akamine P., et al. Dynamic features of cAMP-dependent protein kinase revealed by apoenzyme crystal structure. J. Mol. Biol. 327 (2003) 159-171
    • (2003) J. Mol. Biol. , vol.327 , pp. 159-171
    • Akamine, P.1
  • 12
    • 0031578579 scopus 로고    scopus 로고
    • The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions
    • Williams J.C., et al. The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions. J. Mol. Biol. 274 (1997) 757-775
    • (1997) J. Mol. Biol. , vol.274 , pp. 757-775
    • Williams, J.C.1
  • 13
    • 1842477464 scopus 로고    scopus 로고
    • Identification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4
    • Zhao Q., et al. Identification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4. J. Biol. Chem. 279 (2004) 12560-12564
    • (2004) J. Biol. Chem. , vol.279 , pp. 12560-12564
    • Zhao, Q.1
  • 14
    • 4544254444 scopus 로고    scopus 로고
    • Definition of protein kinase sequence motifs that trigger high affinity binding of Hsp90 and Cdc37
    • Prince T., and Matts R.L. Definition of protein kinase sequence motifs that trigger high affinity binding of Hsp90 and Cdc37. J. Biol. Chem. 279 (2004) 39975-39981
    • (2004) J. Biol. Chem. , vol.279 , pp. 39975-39981
    • Prince, T.1    Matts, R.L.2
  • 15
    • 27744562164 scopus 로고    scopus 로고
    • Cdk2: a genuine protein kinase client of Hsp90 and Cdc37
    • Prince T., et al. Cdk2: a genuine protein kinase client of Hsp90 and Cdc37. Biochemistry 44 (2005) 15287-15295
    • (2005) Biochemistry , vol.44 , pp. 15287-15295
    • Prince, T.1
  • 16
    • 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 (2006) 3378-3389
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3378-3389
    • Terasawa, K.1
  • 17
    • 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 A.D., et al. 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 (2002) 39858-39866
    • (2002) J. Biol. Chem. , vol.277 , pp. 39858-39866
    • Basso, A.D.1
  • 18
    • 33244484848 scopus 로고    scopus 로고
    • Targeting chaperones in transformed systems-a focus on Hsp90 and cancer
    • Chiosis G. Targeting chaperones in transformed systems-a focus on Hsp90 and cancer. Expert Opin. Ther. Targets 10 (2006) 37-50
    • (2006) Expert Opin. Ther. Targets , vol.10 , pp. 37-50
    • Chiosis, G.1
  • 19
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal A., et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 425 (2003) 407-410
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1
  • 20
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal A., et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 425 (2003) 407-410
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1
  • 21
    • 33646725129 scopus 로고    scopus 로고
    • A biochemical rationale for the anticancer effects of Hsp90 inhibitors: Slow, tight binding inhibition by geldanamycin and its analogues
    • Gooljarsingh L.T., et al. A biochemical rationale for the anticancer effects of Hsp90 inhibitors: Slow, tight binding inhibition by geldanamycin and its analogues. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 7625-7630
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 7625-7630
    • Gooljarsingh, L.T.1
  • 22
    • 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 (2001) 3702-3708
    • (2001) J. Biol. Chem. , vol.276 , pp. 3702-3708
    • Xu, W.1
  • 23
    • 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 (2005) 120-126
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 120-126
    • Xu, W.1
  • 24
    • 0037224231 scopus 로고    scopus 로고
    • Identification of ErbB-2 kinase domain motifs required for geldanamycin-induced degradation
    • Tikhomirov O., and Carpenter G. Identification of ErbB-2 kinase domain motifs required for geldanamycin-induced degradation. Cancer Res. 63 (2003) 39-43
    • (2003) Cancer Res. , vol.63 , pp. 39-43
    • Tikhomirov, O.1    Carpenter, G.2
  • 25
    • 33744931946 scopus 로고    scopus 로고
    • Hsp90 recognizes a common surface on client kinases
    • Citri A., et al. Hsp90 recognizes a common surface on client kinases. J. Biol. Chem. 281 (2006) 14361-14369
    • (2006) J. Biol. Chem. , vol.281 , pp. 14361-14369
    • Citri, A.1
  • 26
    • 0037474219 scopus 로고    scopus 로고
    • A positive feedback loop between protein kinase CKII and Cdc37 promotes the activity of multiple protein kinases
    • Bandhakavi S., et al. A positive feedback loop between protein kinase CKII and Cdc37 promotes the activity of multiple protein kinases. J. Biol. Chem. 278 (2003) 2829-2836
    • (2003) J. Biol. Chem. , vol.278 , pp. 2829-2836
    • Bandhakavi, S.1
  • 27
    • 0141755381 scopus 로고    scopus 로고
    • Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37
    • Shao J., et al. Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37. J. Biol. Chem. 278 (2003) 38117-38120
    • (2003) J. Biol. Chem. , vol.278 , pp. 38117-38120
    • Shao, J.1
  • 28
    • 1942486312 scopus 로고    scopus 로고
    • CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37
    • Miyata Y., and Nishida E. CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37. Mol. Cell. Biol. 24 (2004) 4065-4074
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4065-4074
    • Miyata, Y.1    Nishida, E.2
  • 29
    • 0032897474 scopus 로고    scopus 로고
    • Benzoquinoid ansamycins (herbimycin A and geldanamycin) interfere with the maturation of growth factor receptor tyrosine kinases
    • Sakagami M., et al. Benzoquinoid ansamycins (herbimycin A and geldanamycin) interfere with the maturation of growth factor receptor tyrosine kinases. Cell Stress Chaperones 4 (1999) 19-28
    • (1999) Cell Stress Chaperones , vol.4 , pp. 19-28
    • Sakagami, M.1
  • 30
    • 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 (2005) 10686-10691
    • (2005) Cancer Res. , vol.65 , pp. 10686-10691
    • da Rocha Dias, S.1
  • 31
    • 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. U. S. A. 103 (2006) 57-62
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 57-62
    • Grbovic, O.M.1
  • 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 (2004) 855-867
    • (2004) Cell , vol.116 , pp. 855-867
    • Wan, P.T.1
  • 33
    • 2942744500 scopus 로고    scopus 로고
    • Regulation of the Src family kinase Lck by Hsp90 and ubiquitination
    • Giannini A., and Bijlmakers M.J. Regulation of the Src family kinase Lck by Hsp90 and ubiquitination. Mol. Cell. Biol. 24 (2004) 5667-5676
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5667-5676
    • Giannini, A.1    Bijlmakers, M.J.2
  • 34
    • 27744551993 scopus 로고    scopus 로고
    • Exposure of protein kinase motifs that trigger binding of Hsp90 and Cdc37
    • Prince T., and Matts R.L. Exposure of protein kinase motifs that trigger binding of Hsp90 and Cdc37. Biochem. Biophys. Res. Commun. 338 (2005) 1447-1454
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 1447-1454
    • Prince, T.1    Matts, R.L.2
  • 35
    • 18744373865 scopus 로고    scopus 로고
    • Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP
    • Yang J., et al. Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP. Nat. Struct. Biol. 9 (2002) 940-944
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 940-944
    • Yang, J.1
  • 36
    • 0029665779 scopus 로고    scopus 로고
    • Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
    • Stepanova L., et al. Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes Dev. 10 (1996) 1491-1502
    • (1996) Genes Dev. , vol.10 , pp. 1491-1502
    • Stepanova, L.1
  • 37
    • 0029029617 scopus 로고
    • Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
    • Jeffrey P.D., et al. Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376 (1995) 313-320
    • (1995) Nature , vol.376 , pp. 313-320
    • Jeffrey, P.D.1
  • 38
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
    • Yang J., et al. Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. Mol. Cell 9 (2002) 1227-1240
    • (2002) Mol. Cell , vol.9 , pp. 1227-1240
    • Yang, J.1
  • 39
    • 1542269006 scopus 로고    scopus 로고
    • PKA: a portrait of protein kinase dynamics
    • Taylor S.S., et al. PKA: a portrait of protein kinase dynamics. Biochim. Biophys. Acta 1697 (2004) 259-269
    • (2004) Biochim. Biophys. Acta , vol.1697 , pp. 259-269
    • Taylor, S.S.1
  • 40
    • 27144551963 scopus 로고    scopus 로고
    • ZAP-70 is a novel conditional heat shock protein 90 (Hsp90) client: inhibition of Hsp90 leads to ZAP-70 degradation, apoptosis, and impaired signaling in chronic lymphocytic leukemia
    • Castro J.E., et al. ZAP-70 is a novel conditional heat shock protein 90 (Hsp90) client: inhibition of Hsp90 leads to ZAP-70 degradation, apoptosis, and impaired signaling in chronic lymphocytic leukemia. Blood 106 (2005) 2506-2512
    • (2005) Blood , vol.106 , pp. 2506-2512
    • Castro, J.E.1
  • 41
    • 20444413061 scopus 로고    scopus 로고
    • Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways
    • McClellan A.J., et al. Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell 121 (2005) 739-748
    • (2005) Cell , vol.121 , pp. 739-748
    • McClellan, A.J.1
  • 42
    • 0035816574 scopus 로고    scopus 로고
    • Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70
    • Gusarova V., et al. Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70. J. Biol. Chem. 276 (2001) 24891-24900
    • (2001) J. Biol. Chem. , vol.276 , pp. 24891-24900
    • Gusarova, V.1
  • 43
    • 0034661466 scopus 로고    scopus 로고
    • CYP2E1 degradation by in vitro reconstituted systems: role of the molecular chaperone hsp90
    • Goasduff T., and Cederbaum A.I. CYP2E1 degradation by in vitro reconstituted systems: role of the molecular chaperone hsp90. Arch. Biochem. Biophys. 379 (2000) 321-330
    • (2000) Arch. Biochem. Biophys. , vol.379 , pp. 321-330
    • Goasduff, T.1    Cederbaum, A.I.2
  • 44
    • 0036789884 scopus 로고    scopus 로고
    • Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu
    • Xu W., et al. Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 12847-12852
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12847-12852
    • Xu, W.1
  • 45
    • 0034720255 scopus 로고    scopus 로고
    • Induction of human Cdc37 in prostate cancer correlates with the ability of targeted Cdc37 expression to promote prostatic hyperplasia
    • Stepanova L., et al. Induction of human Cdc37 in prostate cancer correlates with the ability of targeted Cdc37 expression to promote prostatic hyperplasia. Oncogene 19 (2000) 2186-2193
    • (2000) Oncogene , vol.19 , pp. 2186-2193
    • Stepanova, L.1
  • 46
    • 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., et al. 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 (2000) 355-360
    • (2000) Cell Growth Differ. , vol.11 , pp. 355-360
    • An, W.G.1
  • 47
    • 0028828273 scopus 로고
    • Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent
    • Smith D.F., et al. Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent. Mol. Cell. Biol. 15 (1995) 6804-6812
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6804-6812
    • Smith, D.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.