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Science 2 June 1995:
Vol. 268. no. 5215, pp. 1362 - 1365
DOI: 10.1126/science.7761857
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Articles

Science, Vol 268, Issue 5215, 1362-1365
Copyright © 1995 by American Association for the Advancement of Science

articles

Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways

Y Kimura, I Yahara, and S Lindquist

Department of Molecular Genetics and Cell Biology, University of Chicago, IL 60637, USA.

The substrate-specific protein chaperone Hsp90 (heat shock protein 90) from Saccharomyces cerevisiae functions in diverse signal transduction pathways. A mutation in YDJ1, a member of the DnaJ chaperone family, was recovered in a synthetic-lethal screen with Hsp90 mutants. In an otherwise wild-type background, the ydj1 mutation exerted strong and specific effects on three Hsp90 substrates, derepressing two (the estrogen and glucocorticoid receptors) and reducing the function of the third (the tyrosine kinase p60v-src). Analysis of one of these substrates, the glucocorticoid receptor, indicated that Ydj1 exerts its effects through physical interaction with Hsp90 substrates.


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Cdc37 is a molecular chaperone with specific functions in signal transduction..
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   Abstract »    PDF »
Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones.
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   Abstract »    Full Text »
FLP Recombinase/Estrogen Receptor Fusion Proteins Require the Receptor D Domain for Responsiveness to Antagonists, but not Agonists.
M. Nichols, J. M. J. Rientjes, C. Logie, and A. F. Stewart (1997)
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K. D. Dittmar and W. B. Pratt (1997)
J. Biol. Chem. 272, 13047-13054
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Differential Phosphorylation of Chicken Progesterone Receptor in Hormone-dependent and Ligand-independent Activation.
W. Bai, B. G. Rowan, V. E. Allgood, B. W. O'Malley, and N. L. Weigel (1997)
J. Biol. Chem. 272, 10457-10463
   Abstract »    Full Text »    PDF »
The Yeast CDC37 Gene Interacts with MPS1 and Is Required for Proper Execution of Spindle Pole Body Duplication.
A. R. Schutz, T. H. Giddings Jr., E. Steiner, and M. Winey (1997)
J. Cell Biol. 136, 969-982
   Abstract »    Full Text »    PDF »
The hsp90-binding Antibiotic Geldanamycin Decreases Raf Levels and Epidermal Growth Factor Signaling without Disrupting Formation of Signaling Complexes or Reducing the Specific Enzymatic Activity of Raf Kinase.
L. F. Stancato, A. M. Silverstein, J. K. Owens-Grillo, Y.-H. Chow, R. Jove, and W. B. Pratt (1997)
J. Biol. Chem. 272, 4013-4020
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Characterization of Functional Domains of the Eukaryotic Co-chaperone Hip.
H. Irmer and J. Hohfeld (1997)
J. Biol. Chem. 272, 2230-2235
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The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR.
M. W. Melville, W. J. Hansen, B. C. Freeman, W. J. Welch, and M. G. Katze (1997)
PNAS 94, 97-102
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Molecular chaperones and the cytoskeleton.
P Liang and T. MacRae (1997)
J. Cell Sci. 110, 1431-1440
   Abstract »    PDF »
Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90.
C. Schneider, L. Sepp-Lorenzino, E. Nimmesgern, O. Ouerfelli, S. Danishefsky, N. Rosen, and F. U. Hartl (1996)
PNAS 93, 14536-14541
   Abstract »    Full Text »    PDF »
Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4..
L Stepanova, X Leng, S B Parker, and J W Harper (1996)
Genes & Dev. 10, 1491-1502
   Abstract »    PDF »
Cyclophilin 40 (CyP-40), Mapping of Its hsp90 Binding Domain and Evidence That FKBP52 Competes with CyP-40 for hsp90 Binding.
T. Ratajczak and A. Carrello (1996)
J. Biol. Chem. 271, 2961-2965
   Abstract »    Full Text »    PDF »
Mutational analysis of Hsp90 alpha dimerization and subcellular localization: dimer disruption does not impede ""in vivo' interaction with estrogen receptor.
X Meng, J Devin, W. Sullivan, D Toft, E. Baulieu, and M. Catelli (1996)
J. Cell Sci. 109, 1677-1687
   Abstract »    PDF »
Hsp90 Mutants Disrupt Glucocorticoid Receptor Ligand Binding and Destabilize Aporeceptor Complexes.
S. P. Bohen and S. P. Bohen (1995)
J. Biol. Chem. 270, 29433-29438
   Abstract »    Full Text »    PDF »
Definition of a Minimal Domain of the Dioxin Receptor That Is Associated with Hsp90 and Maintains Wild Type Ligand Binding Affinity and Specificity.
P. Coumailleau, L. Poellinger, J.Åk. Gustafsson, and M. L. Whitelaw (1995)
J. Biol. Chem. 270, 25291-25300
   Abstract »    Full Text »    PDF »
Hold 'em and fold 'em: chaperones and signal transduction.
S. Bohen, A Kralli, and K. Yamamoto (1995)
Science 268, 1303-1304
   PDF »
Functional Interaction of Human Cdc37 with the Androgen Receptor but Not with the Glucocorticoid Receptor.
J. Rao, P. Lee, S. Benzeno, C. Cardozo, J. Albertus, D. M. Robins, and A. J. Caplan (2001)
J. Biol. Chem. 276, 5814-5820
   Abstract »    Full Text »    PDF »


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