Interaction of radicicol with members of the heat shock protein 90 family of molecular chaperones

Molecular Endocrinology

Volumn 13, Issue 9, 1999, Pages 1435-1448

  Schulte, Theodor W ^a   Akinaga, Shiro ^b   Murakata, T ^b   Agatsuma, Tsutomu ^b   Sugimoto, Seiji ^b   Nakano, Hirofumi ^b   Lee, Yong S ^c   Simen, Birgitte B ^d   Argon, Yair ^d   Felts, Sara ^e   Toft, David O ^e   Neckers, Leonard M ^a   Sharma, Sreenath V ^f  

^a NATIONAL CANCER INSTITUTE   (United States)

^b KYOWA HAKKO KOGYO CO LTD   (Japan)

^c NATIONAL EYE INSTITUTE   (United States)

^d UNIVERSITY OF CHICAGO   (United States)

^e MAYO CLINIC   (United States)

^f UNIVERSITY OF TENNESSEE HEALTH SCIENCE CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID; ANSAMYCIN DERIVATIVE; CHAPERONE; DRUG DERIVATIVE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; RADICICOL; TUMOR NECROSIS FACTOR RECEPTOR;

ANIMAL CELL; ARTICLE; BINDING SITE; BIOTINYLATION; DRUG PROTEIN BINDING; ESCHERICHIA COLI; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN INTERACTION; YEAST;

ANIMALIA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MAMMALIA;

EID: 0033305209     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/mend.13.9.0339     Document Type: Article

References (57)

1. The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review
2. Mutational analysis of hsp90 function: Interactions with a steroid receptor and a protein kinase
3. The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes
4. Molecular chaperoning of steroid hormone receptors
5. Association of the dioxin receptor with the Mr 90,000 heat shock protein: A structural kinship with the glucocorticoid receptor
6. Association of the Ah receptor with the 90-kDa heat shock protein
7. Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84)
8. Geldanamycin selectively destabilizes and conformationally alters mutated p53
9. Functional interference between hypoxia and dioxin signal transduction pathways: Competition for recruitment of the Arnt transcription factor
10. Interaction between the Rous sarcoma virus transforming protein and two cellular phosphoproteins: Analysis of the turnover and distribution of this complex
11. Interaction of the Rous sarcoma virus protein pp60 src with the cellular proteins pp50 and pp90
12. Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function
13. Hsp90-mediated folding of the lymphoid cell kinase p56(lck)
14. Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system
15. The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex
16. Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
17. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
18. Crystal structure of an HSP90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
19. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation
20. Herbimycin A induces the 20 S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases
21. Geldanamycin-induced destabilization of Raf-1 involves the proteasome
22. Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96
23. Geldanamycin, an hsp90/GRP94-binding drug, induces increased transcription of endoplasmic reticulum (ER) chaperones via the ER stress pathway
24. Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor
25. A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock
26. A new antifungal substance of fungal origin
27. The constitution of radicicol
28. Radicicol, a microbial cell differentiation modulator, inhibits in vivo angiogenesis
29. Potent and specific inhibition of p60v-src protein kinase both in vivo and in vitro by radicicol
30. Suppression of RAS and MOS transformation by radicicol
31. Morphology of ras-transformed cells becomes apparently normal again with tyrosine kinase inhibitors without a decrease in the ras-GTP complex
32. Radicicol leads to selective depletion of Raf kinase and disrupts K-Ras-activated aberrant signaling pathway
33. Suppression of morphological transformation by radicicol is accompanied by enhanced gelsolin expression
34. Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
35. Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol
36. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
37. CHARMM: A program for macromolecular energy minimizations and molecular dynamics calculations
38. An atypical topoisomerase II from Archaea with implications for meiotic recombination
39. Positionally cloned human disease genes: Patterns of evolutionary conservation and functional motifs [see comments]
40. Crystal structure and ATPase activity of MutL: Implications for DNA repair and mutagenesis
41. A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90
42. The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity
43. Interaction of the Calcium and calmodulin regulated eEF-2 kinase with heat shock protein 90
44. The Hsp90 chaperone family
45. CDC37-a protein kinase chaperone
46. Steroid receptor interactions with heat shock protein and immunophilin chaperones
47. The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase
48. The Hsp90 complex-a super-chaperone machine as a novel drug target
49. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
50. Identifying the catalytic residue of the ATPase reaction of DNA gyrase
51. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
52. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis
53. Crystal structure of an N-terminal fragment of the DNA gyrase B protein
54. Dominant negative mutator mutations in the mutL gene of Escherichia coli
55. ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94)
56. Cleavage of structural proteins during the assembly of the head of bacteriophage T4
57. Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association