The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Nucleotides and Two Functional States of hsp90
Open accessAbstract
Previous studies have demonstrated the ATP-dependent formation of a complex containing the heat shock protein hsp90, the unique hsp90 binding protein p23, and one of three high molecular weight immunophilins. In the present study, hsp90 and p23 are shown to form a complex that requires elevated temperature and ATP/Mg2+. Complex formation is strongly promoted by molybdate and by the nonionic detergent Nonidet P-40. ADP and the benzoquinone ansamycin, geldanamycin, are potent inhibitors of complex formation. The ATP-dependent process alters the state of hsp90, not p23, and influences the ability of hsp90 to bind to phenyl-Sepharose. Conversion of hsp90 to the ATP-bound state lowers its affinity for phenyl-Sepharose. These results show that hsp90 can exist in at least two functional states, one able to bind p23 and the other with a high affinity for hydrophobic resins. A model is presented where these states are dictated by the binding of either ATP or ADP.
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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
Borkovich, 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
Freeman, B. C., Toft, D. O., & Morimoto, R. I. (1996) · Science · doi:10.1126/science.274.5293.1718 · Cited by 370
Self-citationBinding of p23 and hsp90 during assembly with the progesterone receptor.
Johnson, J. L., & Toft, D. O. (1995) · Molecular Endocrinology · doi:10.1210/mend.9.6.8592513 · Cited by 233
Self-citationATP induces a conformational change of the 90-kDa heat shock protein (hsp90).
Csermely, P., Kajtár, J., Hollósi, M., Jalsovszky, G., Holly, S., Kahn, C. R., Gergely, P., Söti, C., Mihály, K., & Somogyi, J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53939-9 · Cited by 133
Cited by
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818
Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
Ali, M. M. U., Roe, S. M., Vaughan, C. K., Meyer, P., Panaretou, B., Piper, P. W., Prodromou, C., & Pearl, L. H. (2006) · Nature · doi:10.1038/nature04716 · Cited by 962
ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
Panaretou, B., Prodromou, C., Roe, S. M., O'Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.16.4829 · Cited by 735
Tanioka, T., Nakatani, Y., Semmyo, N., Murakami, M., & Kudo, I. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003504200 · Cited by 708
Prodromou, C., Panaretou, B., Chohan, S., Siligardi, G., O'Brien, R., Ladbury, J. E., Roe, S. M., Piper, P. W., & Pearl, L. H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.16.4383 · Cited by 492
Metadata
- Authors
- Sullivan, W., Stensgard, B., Caucutt, G., Bartha, B., McMahon, N., Alnemri, E. S., Litwack, G., & Toft, D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-03
- Volume
- 272
- Issue
- 12
- Pages
- 8007-8012
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2046699174
- Cited by
- 238
- References
- 5
- FWCI
- 7.76
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Sullivan, W., Stensgard, B., Caucutt, G., Bartha, B., McMahon, N., Alnemri, E. S., Litwack, G., & Toft, D. (1997). Nucleotides and Two Functional States of hsp90. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.272.12.8007
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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).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
