The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
The Charged Linker Region Is an Important Regulator of Hsp90 Function
Open accessAbstract
Hsp90 is an ATP-dependent molecular chaperone which assists the maturation of a large set of target proteins. Members of the highly conserved Hsp90 family are found from bacteria to higher eukaryotes, with homologues in different organelles. The core architecture of Hsp90 is defined by the N-terminal ATP binding domain followed by the middle domain and the C-terminal dimerization domain. A long, highly charged linker between the N-terminal domain and the middle domain is a feature characteristic for Hsp90s of eukaryotic organisms. We set out to clarify the function of this linker by studying the effects of deletions in this region in vivo and in vitro. Here we show that increasing deletions in the charged linker region lead to defects ranging from mild temperature sensitivity to a lethal phenotype. The lethal deletion variants investigated in this study still exhibit ATPase activity. Deletion of the charged linker ultimately causes a loss of Hsp90 regulation by co-chaperones, as the sensitivity for Aha1-mediated ATPase acceleration declines, and binding of p23/Sba1 is lost in non-viable deletion constructs. In vivo client assays additionally demonstrated that the deletion of the linker had a pronounced effect on the ability of Hsp90 to facilitate client activation. A partial reconstruction of the linker sequence showed that the supplementation by artificial sequences can rescue the functionality of Hsp90 and restore the conformational flexibility of the protein, required for the processing of client proteins.
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Cites
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Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
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Reduced levels of hsp90 compromise steroid receptor action in vivo
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Mutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase
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Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle
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The Co-chaperone p23 Arrests the Hsp90 ATPase Cycle to Trap Client Proteins
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Self-citation
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
Schopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540
Lu, H., Zhou, Q., He, J., Jiang, Z., Peng, C., Tong, R., & Shi, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00315-3 · Cited by 891
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
Verghese, J., Abrams, J., Wang, Y., & Morano, K. A. (2012) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.05018-11 · Cited by 575
Metadata
- Authors
- Hainzl, O., Lapina, M. C., Buchner, J., & Richter, K.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-08
- Volume
- 284
- Issue
- 34
- Pages
- 22559-22567
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2063992197
- Cited by
- 162
- References
- 9
- FWCI
- 4.56
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Hainzl, O., Lapina, M. C., Buchner, J., & Richter, K. (2009). The Charged Linker Region Is an Important Regulator of Hsp90 Function. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m109.031658
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