Crossref journal-article
Annual Reviews
Annual Review of Pharmacology and Toxicology (22)
Abstract

▪ Abstract  The multicomponent heat-shock protein (hsp) 90–based chaperone system is an ubiquitous protein-folding system in the cytoplasm of eukaryotes. Several signal transduction systems utilize an interaction with hsp90 as an essential component of the signaling pathway. The steroid and dioxin receptors are bound to hsp90 through their hormone-binding domains, and several of them must be bound to hsp90 in order to have a ligand-binding site. The binding of ligands to these receptors promotes their dissociation from hsp90, an event that is the first step in their signaling pathways. Several protein kinases, including the Src and Raf components of the MAP kinase system, are also bound to hsp90. Genetic studies in yeast have demonstrated that hsp90 is required for normal signaling via steroid and dioxin receptors and for the activity of Src in vivo. The hsp90-based chaperone system has been reconstituted from purified components, permitting detailed analysis of the molecular basis of the chaperone's role in signal transduction.

Bibliography

Pratt, W. B. (1997). THE ROLE OF THEhsp90-BASED CHAPERONE SYSTEM IN SIGNAL TRANSDUCTION BY NUCLEAR RECEPTORS AND RECEPTORS SIGNALING VIA MAP KINASE. Annual Review of Pharmacology and Toxicology, 37(1), 297–326.

Authors 1
  1. William B. Pratt (first)
References 183 Referenced 274
  1. {'key': 'b1', 'author': 'Pratt WB', 'year': '1997', 'journal-title': 'Endocrinol. Rev.'} / Endocrinol. Rev. by Pratt WB (1997)
  2. 10.1210/me.7.1.4
  3. 10.1016/S0021-9258(20)80556-0 / J. Biol. Chem. by Pratt WB (1993)
  4. Bohen SP, Yamamoto KR. 1994. Modulation of steroid receptor signal transduction by heat shock proteins. InThe Biology of Heat Shock Proteins and Molecular Chaperones, pp. 313–34. Cold Spring Harbor: Cold Spring Harbor Lab. Press
  5. 10.1146/annurev.ge.27.120193.002253
  6. 10.1128/MCB.14.2.1459
  7. 10.1016/0968-0004(94)90023-X
  8. 10.1073/pnas.55.6.1574
  9. 10.1146/annurev.ph.46.030184.000435
  10. 10.1002/j.1460-2075.1985.tb04055.x
  11. 10.1016/S0021-9258(17)38886-5 / J. Biol. Chem. by Sanchez ER (1985)
  12. 10.1016/S0021-9258(17)38716-1 / J. Biol. Chem. by Schuh S (1985)
  13. 10.1016/S0021-9258(17)35712-5 / J. Biol. Chem. by Mendel DB (1986)
  14. 10.1016/S0021-9258(18)48191-4 / J. Biol. Chem. by Sanchez ER (1987)
  15. 10.1038/333686a0
  16. 10.1016/S0021-9258(18)83301-4 / J. Biol. Chem. by Denis M (1989)
  17. 10.1016/S0021-9258(19)47184-6 / in vitro. J. Biol. Chem. by Dalman FC (1989)
  18. 10.1210/mend-4-11-1704
  19. 10.1016/S0021-9258(18)45746-8 / J. Biol. Chem. by Scherrer LC (1990)
  20. 10.1016/S0021-9258(18)48438-4 / J. Biol. Chem. by Smith DF (1992)
  21. 10.1016/S0021-9258(19)49676-2 / J. Biol. Chem. by Hutchison KA (1992)
  22. 10.1038/365664a0
  23. 10.1128/MCB.9.9.3829
  24. 10.1016/S0021-9258(19)39693-0 / J. Biol. Chem. by Smith DF (1990)
  25. 10.1016/S0021-9258(17)30478-7 / J. Biol. Chem. by Sanchez ER (1990)
  26. 10.1146/annurev.bi.62.070193.002025
  27. 10.1016/S0021-9258(17)37651-2 / J. Biol. Chem. by Hutchison KA (1994)
  28. 10.1128/MCB.14.3.1956
  29. 10.1210/me.9.6.670
  30. 10.1016/S0021-9258(17)31487-4 / J. Biol. Chem. by Johnson JL (1994)
  31. 10.1074/jbc.270.31.18543
  32. 10.1210/me.7.11.1418
  33. 10.1128/MCB.13.2.869
  34. 10.1016/S0021-9258(18)42471-4 / J. Biol. Chem. by Honoré B (1992)
  35. 10.1074/jbc.271.22.12833
  36. 10.1126/science.7761857
  37. 10.1074/jbc.270.10.5251
  38. 10.1210/me.10.4.420
  39. 10.1016/0092-8674(95)90099-3
  40. 10.1016/S0021-9258(18)46871-8 / J. Biol. Chem. by Hutchison KA (1994)
  41. 10.1016/S0021-9258(19)78104-6 / J. Biol. Chem. by Czar MJ (1994)
  42. 10.1210/me.10.6.682
  43. 10.1074/jbc.271.23.13468
  44. 10.1021/bi9511649
  45. 10.1021/bi9615349
  46. 10.1038/308850a0
  47. 10.1016/S0021-9258(18)60531-9 / J. Biol. Chem. by Rafstin-Oblin ME (1989)
  48. 10.1016/S0021-9258(18)52316-4 / J. Biol. Chem. by Privalsky ML (1991)
  49. 10.1016/S0021-9258(18)68314-0 / J. Biol. Chem. by Perdew GH (1988)
  50. 10.1016/S0006-291X(88)80566-7
  51. 10.1074/jbc.270.52.31353
  52. 10.1074/jbc.271.25.15084
  53. 10.1073/pnas.93.16.8379
  54. 10.1073/pnas.93.3.1060
  55. 10.1126/science.3283939
  56. 10.1210/me.7.1.12
  57. 10.1016/0092-8674(88)90122-5
  58. 10.1016/0962-8924(93)90057-8
  59. 10.1021/bi00071a013
  60. 10.1126/science.7761857
  61. 10.1016/S0021-9258(19)57388-4 / J. Biol. Chem. by Pratt WB (1988)
  62. 10.1016/S0021-9258(19)81389-3 / J. Biol. Chem. by Denis M (1988)
  63. 10.1016/S0021-9258(19)67821-X / J. Biol. Chem. by Dalman FC (1991)
  64. 10.1016/0006-291X(91)90433-8
  65. 10.1016/S0021-9258(19)67673-8 / J. Biol. Chem. by Cadepond F (1991)
  66. 10.1016/S0021-9258(18)54835-3 / J. Biol. Chem. by Schowalter DB (1991)
  67. Gehring U. 1995. Structure of the nonactivated glucocorticoid receptor and activation to binding. InGlucocorticoid Receptor Structure and Leukemic Cell Responses, ed. B. Gametchu, pp. 35–56. Austin: RG Landis Co.
  68. 10.1016/S0021-9258(18)83689-4 / J. Biol. Chem. by Bresnick EH (1989)
  69. 10.1210/en.130.5.3074
  70. 10.1074/jbc.271.15.8831
  71. 10.1016/S0021-9258(19)50135-1 / J. Biol. Chem. by Rexin M (1992)
  72. 10.1111/j.1432-1033.1992.tb16607.x
  73. 10.1038/348166a0
  74. 10.1128/MCB.15.7.3917
  75. 10.1073/pnas.90.23.11424
  76. 10.1083/jcb.114.4.609
  77. 10.1016/S0021-9258(17)36953-3 / J. Biol. Chem. by Cyr DM (1994)
  78. 10.1002/bies.950141209
  79. 10.1016/0022-4731(72)90103-3
  80. 10.1210/er.13.1.105
  81. 10.1016/S0021-9258(17)37410-0 / J. Biol. Chem. by Hu LM (1994)
  82. 10.1002/j.1460-2075.1991.tb04954.x
  83. 10.1210/me.6.5.837
  84. 10.1073/pnas.90.8.3588
  85. 10.1242/jcs.106.4.1377 / J. Cell Sci. by Dauvois S (1993)
  86. 10.1016/S0083-6729(08)61043-2
  87. 10.1210/mend-3-2-251
  88. 10.1073/pnas.91.1.340
  89. 10.1210/me.10.1.3
  90. 10.1083/jcb.102.4.1191
  91. 10.1016/0165-6147(92)90076-I
  92. {'key': 'b92', 'first-page': '428', 'volume': '45', 'author': 'Polenz RS', 'year': '1994', 'journal-title': 'Mol. Pharmacol.'} / Mol. Pharmacol. by Polenz RS (1994)
  93. 10.1016/1043-2760(94)P3082-I
  94. 10.1002/j.1460-2075.1993.tb06101.x
  95. 10.1016/S0021-9258(18)42274-0 / J. Biol. Chem. by Pongratz I (1992)
  96. 10.1074/jbc.270.52.31353
  97. 10.1128/MCB.13.4.2504
  98. 10.1128/MCB.15.2.756
  99. Carver LA, Jackiw V, Bradfield CA. 1994. The 90-kDa heat shock protein is essential for Ah receptor signaling in a yeast expression system. 269:30109–12 (10.1016/S0021-9258(18)43782-9)
  100. 10.1128/MCB.12.11.5059
  101. 10.1016/S0021-9258(17)42001-1 / J. Biol. Chem. by Shue G (1992)
  102. 10.1126/science.1702904
  103. 10.1016/S0021-9258(18)42176-X / J. Biol. Chem. by Walsh CT (1992)
  104. 10.1146/annurev.bb.22.060193.001011
  105. 10.1016/S0021-9258(19)36676-1 / J. Biol. Chem. by Wiederrecht G (1992)
  106. 10.1073/pnas.89.14.6270
  107. 10.1016/0092-8674(90)90745-Z
  108. 10.1021/bi00366a043
  109. 10.1016/S0021-9258(18)45667-0 / J. Biol. Chem. by Sanchez ER (1990)
  110. 10.1016/S0021-9258(19)50664-0 / J. Biol. Chem. by Yem AW (1992)
  111. 10.1126/science.1376003
  112. 10.1016/S0021-9258(18)42827-X / J. Biol. Chem. by Lebeau MC (1992)
  113. 10.1073/pnas.89.22.10974
  114. 10.1016/0378-1119(93)90206-I
  115. 10.1016/S0021-9258(17)46853-0 / J. Biol. Chem. by Smith DF (1993)
  116. 10.1016/S0021-9258(20)80520-1 / J. Biol. Chem. by Smith DF (1993)
  117. 10.1128/MCB.15.8.4395
  118. 10.1210/me.9.7.838
  119. 10.1016/0022-4731(90)90197-Z
  120. 10.1016/S0021-9258(19)38636-3 / J. Biol. Chem. by Ratajczak T (1993)
  121. 10.1016/S0021-9258(18)42795-0 / J. Biol. Chem. by Kieffer LJ (1992)
  122. 10.1016/S0021-9258(18)31389-9 / J. Biol. Chem. by Kieffer LJ (1993)
  123. 10.1021/bi00473a021
  124. 10.1016/S0021-9258(20)89556-8 / J. Biol. Chem. by Perdew GH (1991)
  125. 10.1074/jbc.270.35.20479
  126. 10.1074/jbc.271.6.2961
  127. 10.1073/pnas.91.23.11197
  128. 10.1042/bj3070005
  129. 10.1073/pnas.92.11.4977
  130. 10.1021/bi00066a015
  131. 10.1016/0960-0760(94)90256-9
  132. 10.1016/S0021-9258(18)53220-8 / J. Biol. Chem. by Ning YM (1993)
  133. 10.1083/jcb.44.1.103
  134. 10.1210/me.7.7.840
  135. 10.1073/pnas.92.10.4701
  136. 10.1016/S0021-9258(18)53221-X / J. Biol. Chem. by Saeki T (1993)
  137. 10.1074/jbc.271.29.17152
  138. 10.1016/0960-0760(93)90216-J
  139. 10.1210/me.9.11.1549
  140. 10.1210/me.8.12.1731
  141. 10.1016/0092-8674(81)90055-6
  142. 10.1073/pnas.78.2.1067
  143. 10.1016/S0021-9258(19)50671-8 / J. Biol. Chem. by Hutchison KA (1992)
  144. 10.1128/MCB.2.7.875
  145. 10.1021/bi00196a008
  146. 10.1002/j.1460-2075.1994.tb06956.x
  147. 10.1016/S0021-9258(20)80600-0 / J. Biol. Chem. by Stancato LF (1993)
  148. 10.1016/S0021-9258(17)37431-8 / J. Biol. Chem. by Wartmann M (1994)
  149. 10.1016/0014-5793(94)80598-9
  150. 10.1074/jbc.272.7.4013
  151. 10.1021/bi00395a003
  152. 10.1016/S0021-9258(19)84864-0 / J. Biol. Chem. by Matts RL (1989)
  153. 10.1016/0014-5793(94)00676-8
  154. 10.1021/bi00025a019
  155. 10.1016/0092-8674(93)90411-I
  156. 10.1073/pnas.89.7.2922
  157. 10.1128/MCB.15.1.398
  158. 10.1146/annurev.cb.03.110187.000335
  159. 10.1073/pnas.79.23.7117
  160. 10.1128/MCB.3.1.9
  161. {'key': 'b161', 'first-page': '1', 'volume': '123', 'author': 'Brugge JS', 'year': '1986', 'journal-title': 'Curr. Top. Microbiol. Immunol.'} / Curr. Top. Microbiol. Immunol. by Brugge JS (1986)
  162. 10.1016/S0021-9258(19)49662-2 / J. Biol. Chem. by Hutchison KA (1992)
  163. 10.1128/jvi.60.3.849-857.1986 / J. Virol. by Jove R (1986)
  164. 10.1073/pnas.90.15.7074
  165. 10.1016/S0021-9258(18)55318-7 / J. Biol. Chem. by Whitelaw ML (1991)
  166. 10.1128/MCB.6.6.2198
  167. 10.1016/0042-6822(88)90649-6
  168. {'key': 'b168', 'first-page': '1721', 'volume': '52', 'author': 'Whitesell L', 'year': '1992', 'journal-title': 'Cancer Res.'} / Cancer Res. by Whitesell L (1992)
  169. 10.1073/pnas.91.18.8324
  170. {'key': 'b170', 'first-page': '780', 'volume': '49', 'author': 'Uehara Y', 'year': '1989', 'journal-title': 'Cancer Res.'} / Cancer Res. by Uehara Y (1989)
  171. 10.1074/jbc.270.41.24585
  172. 10.1128/MCB.15.12.6804
  173. 10.1210/me.10.6.705
  174. {'key': 'b174', 'first-page': '933', 'volume': '11', 'author': 'Blagosklonny MV', 'year': '1995', 'journal-title': 'Oncogene'} / Oncogene by Blagosklonny MV (1995)
  175. 10.1074/jbc.271.37.22796
  176. 10.1073/pnas.87.19.7722
  177. 10.1074/jbc.270.1.1
  178. 10.1093/oxfordjournals.jbchem.a124363
  179. 10.1016/S0021-9258(19)67601-5 / J. Biol. Chem. by Simonds WF (1991)
  180. 10.1016/S0021-9258(18)50106-X / J. Biol. Chem. by Iniguez-Lluhi JA (1992)
  181. 10.1016/S0021-9258(17)37077-1 / J. Biol. Chem. by Higgins JB (1994)
  182. 10.1016/S0021-9258(20)64356-3 / J. Biol. Chem. by Schmidt CJ (1991)
  183. 10.1074/jbc.270.26.15892
Dates
Type When
Created 23 years ago (July 27, 2002, 7:45 a.m.)
Deposited 3 years, 10 months ago (Oct. 16, 2021, 3:09 a.m.)
Indexed 2 months, 4 weeks ago (May 27, 2025, 5:06 p.m.)
Issued 28 years, 4 months ago (April 1, 1997)
Published 28 years, 4 months ago (April 1, 1997)
Published Print 28 years, 4 months ago (April 1, 1997)
Funders 0

None

@article{Pratt_1997, title={THE ROLE OF THEhsp90-BASED CHAPERONE SYSTEM IN SIGNAL TRANSDUCTION BY NUCLEAR RECEPTORS AND RECEPTORS SIGNALING VIA MAP KINASE}, volume={37}, ISSN={1545-4304}, url={http://dx.doi.org/10.1146/annurev.pharmtox.37.1.297}, DOI={10.1146/annurev.pharmtox.37.1.297}, number={1}, journal={Annual Review of Pharmacology and Toxicology}, publisher={Annual Reviews}, author={Pratt, William B.}, year={1997}, month=apr, pages={297–326} }