The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Cdc37 is a molecular chaperone with specific functions in signal transduction.
Open accessAbstract
Cdc37 is required for cyclin-dependent kinase activation and is genetically linked with the activity of several other kinases, including oncogenic v-Src, casein kinase II, MPS-1 kinase, and sevenless. Strikingly, many pathways involving Cdc37 also involve the protein chaperone Hsp90. The identification of Cdc37 as the 50-kD protein in several Hsp90-kinase complexes, together with other data, led to the recent suggestion that Cdc37 is a kinase-targeting "subunit" of Hsp90. We directly examined the effect of Cdc37 on Hsp90 functions. Rather than simply acting as an accessory factor for Hsp90, Cdc37 is itself a protein chaperone with properties remarkably similar to those of Hsp90. In vitro, Cdc37 maintains denatured beta-galactosidase in an activation-competent state without reactivating it and stabilizes mature, but unstable, casein kinase II. In vivo, Cdc37 overexpression can compensate for decreased Hsp90 function, but the proteins are not interchangeable. Cdc37 can compensate for Hsp90 in maintaining the activity of v-Src kinase but does not maintain the activity of the glucocorticoid receptor. Thus, the very similar chaperone activities of the two proteins, uncovered through in vitro analysis, diverge in vivo in specific signal transduction pathways.
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Cites
Reduced levels of hsp90 compromise steroid receptor action in vivo
Picard, D., Khursheed, B., Garabedian, M. J., Fortin, M. G., Lindquist, S., & Yamamoto, K. R. (1990) · Nature · doi:10.1038/348166a0 · Cited by 787 · cited 1×
“The Hsp90 chaperone pathway is highly conserved, and when these heterologous target proteins are expressed in yeast their activity depends on Hsp90 (Picard et al. 1990; Xu and Lindquist 1993; Bohen and Yamamoto 1994; Nathan and Lindquist 1995).”
BackgroundSelf-citationBorkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., & Lindquist, S. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3919 · Cited by 641
Self-citationMammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
Stepanova, L., Leng, X., Parker, S. B., & Harper, J. W. (1996) · Genes & Development · doi:10.1101/gad.10.12.1491 · Cited by 483
Mutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase
Nathan, D. F., & Lindquist, S. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3917 · Cited by 423
Self-citationHeat-shock protein hsp90 governs the activity of pp60v-src kinase.
Xu, Y., & Lindquist, S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.7074 · Cited by 416
Self-citationFreeman, B. C., Toft, D. O., & Morimoto, R. I. (1996) · Science · doi:10.1126/science.274.5293.1718 · Cited by 370
Self-citationSmith, D. F. (1993) · Molecular Endocrinology · doi:10.1210/me.7.11.1418 · Cited by 300
Cited by
Mendenhall, M. D., & Hodge, A. E. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.4.1191-1243.1998 · Cited by 429
In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
Nathan, D. F., Vos, M. H., & Lindquist, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.12949 · Cited by 364
Self-citationMiyata, Y., Chambraud, B., Radanyi, C., Leclerc, J., Lebeau, M.-C., Renoir, J.-M., Shirai, R., Catelli, M.-G., Yahara, I., & Baulieu, E.-E. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14500 · Cited by 121
Self-citationHsp90: A New Player in DNA Repair?
Pennisi, R., Ascenzi, P., & Di Masi, A. (2015) · Biomolecules · doi:10.3390/biom5042589 · Cited by 112
Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs
Leach, M. D., Klipp, E., Cowen, L. E., & Brown, A. J. P. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2875 · Cited by 107
Metadata
- Authors
- Kimura, Y., Rutherford, S. L., Miyata, Y., Yahara, I., Freeman, B. C., Yue, L., Morimoto, R. I., & Lindquist, S.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1997-07-15
- Volume
- 11
- Issue
- 14
- Pages
- 1775-1785
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2148779817
- Cited by
- 206
- References
- 7
- Type
- posted content
- Language
- en
- Open access
- diamond
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- Kimura, Y., Rutherford, S. L., Miyata, Y., Yahara, I., Freeman, B. C., Yue, L., Morimoto, R. I., & Lindquist, S. (1997). Cdc37 is a molecular chaperone with specific functions in signal transduction. Genes & Development. https://doi.org/10.1101/gad.11.14.1775
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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