Structure and in vivo function of Hsp90

Current Opinion in Structural Biology - Tập 10 - Trang 46-51 - 2000
Laurence H Pearl1, Chrisostomos Prodromou1
1Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK

Tài liệu tham khảo

Pratt, 1998, The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors, Proc Soc Exp Biol Med, 217, 420, 10.3181/00379727-217-44252 Prodromou, 1997, Identification and structural characterisation of the ATP/ADP binding site in the Hsp90 molecular chaperone, Cell, 90, 65, 10.1016/S0092-8674(00)80314-1 Grenert, 1997, 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, 10.1074/jbc.272.38.23843 Panaretou, 1998, ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo, EMBO J, 17, 4829, 10.1093/emboj/17.16.4829 Obermann, 1998, In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis, J Cell Biol, 143, 901, 10.1083/jcb.143.4.901 Grenert, 1999, The importance of ATP binding and hydrolysis by Hsp90 in formation and function of protein heterocomplexes, J Biol Chem, 274, 17525, 10.1074/jbc.274.25.17525 Prodromou, 1997, A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone, Nat Struct Biol, 4, 477, 10.1038/nsb0697-477 Roe, 1999, The structural basis for inhibition of the Hsp90 molecular chaperone, by the anti-tumour antibiotics radicicol and geldanamycin, J Med Chem, 42, 260, 10.1021/jm980403y Stebbins, 1997, Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent, Cell, 89, 239, 10.1016/S0092-8674(00)80203-2 Ban, 1998, Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis, Cell, 95, 541, 10.1016/S0092-8674(00)81621-9 Ban, 1999, Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair, Cell, 97, 85, 10.1016/S0092-8674(00)80717-5 Bilwes, 1999, Structure of CheA, a signal-transducing histidine kinase, Cell, 96, 131, 10.1016/S0092-8674(00)80966-6 Maruya, 1999, Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies, J Mol Biol, 285, 903, 10.1006/jmbi.1998.2349 Kampranis, 1999, A model for the mechanism of strand passage by DNA gyrase, Proc Natl Acad Sci USA, 96, 8414, 10.1073/pnas.96.15.8414 Dittmar, 1997, Folding of the glucocorticoid receptor by the reconstituted hsp90-based chaperone machinery, J Biol Chem, 272, 13047, 10.1074/jbc.272.20.13047 Kosano, 1998, The assembly of progesterone receptor-hsp90 complexes using purified proteins, J Biol Chem, 273, 32973, 10.1074/jbc.273.49.32973 Das, 1998, The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions, EMBO J, 17, 1192, 10.1093/emboj/17.5.1192 Russell, 1999, Identification of conserved residues required for the binding of a tetratricopeptide repeat domain to heat shock protein 90, J Biol Chem, 274, 20060, 10.1074/jbc.274.29.20060 Carrello, 1999, The common tetratricopeptide repeat acceptor site for steroid receptor associated immunophilins and hop is located in the dimerization domain of Hsp90, J Biol Chem, 274, 2682, 10.1074/jbc.274.5.2682 Chen, 1998, Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants, Cell Stress Chaperones, 3, 118, 10.1379/1466-1268(1998)003<0118:DIOPAT>2.3.CO;2 Young, 1998, Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90, J Biol Chem, 273, 18007, 10.1074/jbc.273.29.18007 Prodromou, 1999, Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones, EMBO J, 18, 754, 10.1093/emboj/18.3.754 Marsh, 1998, Cns1 is an essential protein associated with the Hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Δ cells, Mol Cell Biol, 18, 7353, 10.1128/MCB.18.12.7353 Dolinski, 1998, CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90, Mol Cell Biol, 18, 7344, 10.1128/MCB.18.12.7344 Grammatikakis, 1999, p50cdc37 acting in concert with Hsp90 is required for Raf-1 function, Mol Cell Biol, 19, 1661, 10.1128/MCB.19.3.1661 Silverstein, 1998, P50(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, 10.1074/jbc.273.32.20090 Chen, 1998, Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery, J Biol Chem, 273, 35194, 10.1074/jbc.273.52.35194 Johnson, 1998, Hop modulates hsp70/hsp90 interactions in protein folding, J Biol Chem, 273, 3679, 10.1074/jbc.273.6.3679 Fang, 1998, SBA1 encodes a yeast Hsp90 cochaperone that is homologous to vertebrate p23 proteins, Mol Cell Biol, 18, 3727, 10.1128/MCB.18.7.3727 Nathan, 1999, Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation, Proc Natl Acad Sci USA, 96, 1409, 10.1073/pnas.96.4.1409 Duina, 1998, The peptidyl-prolyl isomerase domain of the Cyp-40 cyclophilin homolog Cpr7 is not required to support growth or glucocorticoid receptor activity in Saccharomyces cerevisiae, J Biol Chem, 273, 10819, 10.1074/jbc.273.18.10819 Pratt, 1998, Studies with purified chaperones advance the understanding of the mechanism of glucocorticoid receptor hsp90 heterocomplex assembly, Trends Endocrinol Metabol, 9, 244, 10.1016/S1043-2760(98)00059-9 Caamano, 1998, A conserved proline in the hsp90 binding region of the glucocorticoid receptor is required for hsp90 heterocomplex stabilization and receptor signalling, J Biol Chem, 273, 20473, 10.1074/jbc.273.32.20473 Xu, 1998, Binding of hsp90 to the glucocorticoid receptor requires a specific 7-amino acid sequence at the amino terminus of the hormone-binding domain, J Biol Chem, 273, 13918, 10.1074/jbc.273.22.13918 Xu, 1999, Maturation of the tyrosine kinase c Src as a kinase and as a substrate depends on the molecular chaperone Hsp90, Proc Natl Acad Sci USA, 96, 109, 10.1073/pnas.96.1.109 Hartson, 1998, Modular folding and evidence for phosphorylation-induced stabilization of an Hsp90-dependent kinase, J Biol Chem, 273, 8475, 10.1074/jbc.273.14.8475 Loo, 1998, Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteosome, EMBO J, 17, 6879, 10.1093/emboj/17.23.6879 Garcia-Cardena, 1998, Dynamic activation of endothelial nitric oxide synthase by Hsp90, Nature, 392, 821, 10.1038/33934 Holt, 1999, Functional requirement of p23 and Hsp90 in telomerase complexes, Genes Dev, 13, 817, 10.1101/gad.13.7.817 Hoshino, 1998, Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression, Blood, 91, 4379, 10.1182/blood.V91.11.4379 Zou, 1998, Repression of heat shock transcription factor HSF1 activation by Hsp90 (Hsp90 complex) that forms a stress-sensitive complex with HSF1, Cell, 94, 471, 10.1016/S0092-8674(00)81588-3 Ali, 1998, Hsp90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes, Mol Cell Biol, 18, 4949, 10.1128/MCB.18.9.4949 Duina, 1998, Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response, J Biol Chem, 273, 18974, 10.1074/jbc.273.30.18974 Rutherford, 1998, Hsp90 as a capacitor for morphological evolution, Nature, 396, 336, 10.1038/24550 Whitesell, 1994, Inhibition of heat-shock protein Hsp90-Pp60(V-Src) heteroprotein complex-formation by benzoquinone ansamycins — essential role for stress proteins in oncogenic transformation, Proc Natl Acad Sci USA, 91, 8324, 10.1073/pnas.91.18.8324 Sharma, 1998, Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol, Oncogene, 16, 2639, 10.1038/sj.onc.1201790 Soga, 1998, Radicicol leads to selective depletion of Raf kinase and disrupts K-Ras-activated aberrant signaling pathway, J Biol Chem, 273, 822, 10.1074/jbc.273.2.822 Whitesell, 1998, The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent, Mol Cell Biol, 18, 1517, 10.1128/MCB.18.3.1517 Schulte, 1998, Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin, Cell Stress Chaperones, 3, 100, 10.1379/1466-1268(1998)003<0100:ARBTTN>2.3.CO;2 Scheibel, 1998, Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence, Proc Natl Acad Sci USA, 95, 1495, 10.1073/pnas.95.4.1495