The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Characterization of Celastrol to Inhibit Hsp90 and Cdc37 Interaction
Open accessAbstract
The molecular chaperone heat shock protein 90 (Hsp90) is required for the stabilization and conformational maturation of various oncogenic proteins in cancer. The loading of protein kinases to Hsp90 is actively mediated by the cochaperone Cdc37. The crucial role of the Hsp90-Cdc37 complex has made it an exciting target for cancer treatment. In this study, we characterize Hsp90 and Cdc37 interaction and drug disruption using a reconstituted protein system. The GST pull-down assay and ELISA assay show that Cdc37 binds to ADP-bound/nucleotide-free Hsp90 but not ATP-bound Hsp90. Celastrol disrupts Hsp90-Cdc37 complex formation, whereas the classical Hsp90 inhibitors (e.g. geldanamycin) have no effect. Celastrol inhibits Hsp90 ATPase activity without blocking ATP binding. Proteolytic fingerprinting indicates celastrol binds to Hsp90 C-terminal domain to protect it from trypsin digestion. These data suggest that celastrol may represent a new class of Hsp90 inhibitor by modifying Hsp90 C terminus to allosterically regulate its chaperone activity and disrupt Hsp90-Cdc37 complex.
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Cites
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., & Neckers, L. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8324 · Cited by 1,444
Dual Targeting of HSC70 and HSP72 Inhibits HSP90 Function and Induces Tumor-Specific Apoptosis
Powers, M. V., Clarke, P. A., & Workman, P. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.08.002 · Cited by 307
The Middle Domain of Hsp90 Acts as a Discriminator between Different Types of Client Proteins
Hawle, P., Siepmann, M., Harst, A., Siderius, M., Reusch, H. P., & Obermann, W. M. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02188-05 · Cited by 127
The Influence of ATP and p23 on the Conformation of hsp90
Sullivan, W. P., Owen, B. A. L., & Toft, D. O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207754200 · Cited by 111
Cited by
Hsp90 Molecular Chaperone Inhibitors: Are We There Yet?
Neckers, L., & Workman, P. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-1000 · Cited by 891
Targeting inflammatory pathways by triterpenoids for prevention and treatment of cancer.
Yadav, V. R., Prasad, S., Sung, B., Kannappan, R., & Aggarwal, B. B. (2010) · Toxins · doi:10.3390/toxins2102428 · Cited by 320
Smith, M. C., & Gestwicki, J. E. (2012) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2012.10 · Cited by 286
HSP90AB1: Helping the good and the bad
Haase, M., & Fitze, G. (2016) · Gene · doi:10.1016/j.gene.2015.08.063 · Cited by 179
Small-molecule inhibitor targeting the Hsp90-Cdc37 protein-protein interaction in colorectal cancer
Wang, L., Zhang, L., Li, L., Jiang, J., Zheng, Z., Shang, J., Wang, C., Chen, W., Bao, Q., Xu, X., et al. (2019) · Science Advances · doi:10.1126/sciadv.aax2277 · Cited by 110
Metadata
- Authors
- Zhang, T., Li, Y., Yu, Y., Zou, P., Jiang, Y., & Sun, D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-12
- Volume
- 284
- Issue
- 51
- Pages
- 35381-35389
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1993549724
- Cited by
- 199
- References
- 5
- FWCI
- 5.40
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Zhang, T., Li, Y., Yu, Y., Zou, P., Jiang, Y., & Sun, D. (2009). Characterization of Celastrol to Inhibit Hsp90 and Cdc37 Interaction. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m109.051532
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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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