The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation
Open accessAbstract
Hsp90 is a highly conserved molecular chaperone that is involved in modulating a multitude of cellular processes. In this study, we identify a function for the chaperone in RNA processing and maintenance. This functionality of Hsp90 involves two recently identified interactors of the chaperone: Tah1 and Pih1/Nop17. Tah1 is a small protein containing tetratricopeptide repeats, whereas Pih1 is found to be an unstable protein. Tah1 and Pih1 bind to the essential helicases Rvb1 and Rvb2 to form the R2TP complex, which we demonstrate is required for the correct accumulation of box C/D small nucleolar ribonucleoproteins. Together with the Tah1 cofactor, Hsp90 functions to stabilize Pih1. As a consequence, the chaperone is shown to affect box C/D accumulation and maintenance, especially under stress conditions. Hsp90 and R2TP proteins are also involved in the proper accumulation of box H/ACA small nucleolar RNAs.
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Cites
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“When both Tah1 and Pih1 were mixed with the Rvb1/2 complex, coelution of Rvb1, Rvb2, Tah1, and Pih1 was observed over several fractions, indicating that the complex might be dynamic ( Fig.”
BackgroundMethodSelf-citationZhao, R., Davey, M., Hsu, Y.-C., Kaplanek, P., Tong, A., Parsons, A. B., Krogan, N., Cagney, G., Mai, D., Greenblatt, J., et al. (2005) · Cell · doi:10.1016/j.cell.2004.12.024 · Cited by 819
Self-citationExploration of Essential Gene Functions via Titratable Promoter Alleles
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“These results show that the R2TP complex can be reconstituted in vitro using purifi ed proteins in the absence (not depicted) or presence ( Fig.”
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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
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
Li, J., Soroka, J., & Buchner, J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.003 · Cited by 498
Structure, Function, and Regulation of the Hsp90 Machinery
Biebl, M. M., & Buchner, J. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a034017 · Cited by 304
Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms
Johnson, J. L., & Brown, C. (2009) · Cell Stress and Chaperones · doi:10.1007/s12192-008-0058-9 · Cited by 119
Metadata
- Authors
- Zhao, R., Kakihara, Y., Gribun, A., Huen, J., Yang, G., Khanna, M., Costanzo, M., Brost, R. L., Boone, C., Hughes, T. R., Yip, C. M., & Houry, W. A.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2008-02-11
- Volume
- 180
- Issue
- 3
- Pages
- 563-578
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2073182827
- Cited by
- 183
- References
- 8
- FWCI
- 6.20
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. https://app.cochat.ai/papers/10.1083/jcb.200709061
- The paper
- Zhao, R., Kakihara, Y., Gribun, A., Huen, J., Yang, G., Khanna, M., Costanzo, M., Brost, R. L., Boone, C., Hughes, T. R., Yip, C. M., & Houry, W. A. (2008). Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. The Journal of Cell Biology. https://doi.org/10.1083/jcb.200709061
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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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