The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity.
Open accessAbstract
We found that a preparation of the 90-kDa heat shock protein, HSP90, purified to apparent homogeneity, contains a serine/threonine kinase which phosphorylates HSP90. The protein kinase was identified as casein kinase II (CKII) according to its properties. The protein kinase was separable from HSP90 by adsorption to heparin-Sepharose or phosphocellulose. CKII was coimmunoprecipitated with HSP90 by anti-HSP90 antibodies from cell extracts. Sucrose density gradient centrifugation analysis revealed that an addition of anti-HSP90 antibodies to cell extracts induces a shift of the sedimentation peak of CKII toward the bottom of a centrifuge tube. These results suggest that CKII is associated with HSP90 in cell lysates at low salt conditions. Furthermore, the CKII.HSP90 complex was reconstituted from purified HSP90-free CKII and CKII-free HSP90. In a buffer at low ionic strength, CKII forms large aggregates, but HSP90 dissociates the aggregates. Finally, we found that HSP90 activates CKII; an addition of HSP90 to CKII dramatically increased phosphorylation of exogenous substrates as well as the CKII beta subunit. Taken altogether, these observations suggest that CKII is structurally and functionally active when it forms a complex with HSP90.
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Casein kinase 2: An ‘eminence grise’ in cellular regulation?
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Reduced levels of hsp90 compromise steroid receptor action in vivo
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Association of the Ah receptor with the 90-kDa heat shock protein.
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Cited by
Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones*
Pratt, W. B., & Toft, D. O. (1997) · Endocrine Reviews · doi:10.1210/edrv.18.3.0303 · Cited by 1,791
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The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
Hoter, A., El-Sabban, M. E., & Naim, H. Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092560 · Cited by 693
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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
Metadata
- Authors
- Miyata, Y., & Yahara, I.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-04
- Volume
- 267
- Issue
- 10
- Pages
- 7042-7047
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1516006437
- Cited by
- 311
- References
- 40
- FWCI
- 8.53
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Miyata, Y., & Yahara, I. (1992). The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)50533-6
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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