The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Biological and Structural Basis for Aha1 Regulation of Hsp90 ATPase Activity in Maintaining Proteostasis in the Human Disease Cystic Fibrosis
Open accessAbstract
The activator of Hsp90 ATPase 1, Aha1, has been shown to participate in the Hsp90 chaperone cycle by stimulating the low intrinsic ATPase activity of Hsp90. To elucidate the structural basis for ATPase stimulation of human Hsp90 by human Aha1, we have developed novel mass spectrometry approaches that demonstrate that the N- and C-terminal domains of Aha1 cooperatively bind across the dimer interface of Hsp90 to modulate the ATP hydrolysis cycle and client activity in vivo. Mutations in both the N- and C-terminal domains of Aha1 impair its ability to bind Hsp90 and stimulate its ATPase activity in vitro and impair in vivo the ability of the Hsp90 system to modulate the folding and trafficking of wild-type and variant (ΔF508) cystic fibrosis transmembrane conductance regulator (CFTR) responsible for the inherited disease cystic fibrosis (CF). We now propose a general model for the role of Aha1 in the Hsp90 ATPase cycle in proteostasis whereby Aha1 regulates the dwell time of Hsp90 with client. We suggest that Aha1 activity integrates chaperone function with client folding energetics by modulating ATPase sensitive N-terminal dimer structural transitions, thereby protecting transient folding intermediates in vivo that could contribute to protein misfolding systems disorders such as CF when destabilized.
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Cites
Biological and Chemical Approaches to Diseases of Proteostasis Deficiency
Powers, E. T., Morimoto, R. I., Dillin, A., Kelly, J. W., & Balch, W. E. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.114844 · Cited by 1,149
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The Hsp90 molecular chaperone: an open and shut case for treatment
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“…and structural studies currently support the view that the Hsp90 conformational cycle is coupled to the hydrolysis of ATP (Pearl and Prodromou, 2006; Krukenberg et al ., 2008; Richter et al ., 2008; Hessling et al ., 2009; Mickler et al ., 2009; Neckers et al ., 2009; Vaughan et al ., 2009).”
InfluentialAn Adaptable Standard for Protein Export from the Endoplasmic Reticulum
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Self-citationProtein Homeostasis and Aging: Taking Care of Proteins From the Cradle to the Grave
Morimoto, R. I., & Cuervo, A. M. (2009) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/gln071 · Cited by 151
Cited by
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
Mollapour, M., Tsutsumi, S., Truman, A. W., Xu, W., Vaughan, C. K., Beebe, K., Konstantinova, A., Vourganti, S., Panaretou, B., Piper, P. W., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.011 · Cited by 165
Mixed Hsp90–cochaperone complexes are important for the progression of the reaction cycle
Li, J., Richter, K., & Buchner, J. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1965 · Cited by 155
Conformational Switching of the Molecular Chaperone Hsp90 via Regulated Phosphorylation
Soroka, J., Wandinger, S. K., Mäusbacher, N., Schreiber, T., Richter, K., Daub, H., & Buchner, J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2011.12.031 · Cited by 139
Metadata
- Authors
- Koulov, A. V., LaPointe, P., Lu, B., Razvi, A., Coppinger, J., Dong, M.-Q., Matteson, J., Laister, R., Arrowsmith, C., Yates, J. R., & Balch, W. E.
- Venue
- Molecular Biology of the Cell
- Published
- 2010-03-15
- Volume
- 21
- Issue
- 6
- Pages
- 871-884
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2140457152
- Cited by
- 172
- References
- 6
- FWCI
- 6.62
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Biological and Structural Basis for Aha1 Regulation of Hsp90 ATPase Activity in Maintaining Proteostasis in the Human Disease Cystic Fibrosis. https://app.cochat.ai/papers/10.1091/mbc.e09-12-1017
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- Koulov, A. V., LaPointe, P., Lu, B., Razvi, A., Coppinger, J., Dong, M.-Q., Matteson, J., Laister, R., Arrowsmith, C., Yates, J. R., & Balch, W. E. (2010). Biological and Structural Basis for Aha1 Regulation of Hsp90 ATPase Activity in Maintaining Proteostasis in the Human Disease Cystic Fibrosis. Molecular Biology of the Cell. https://doi.org/10.1091/mbc.e09-12-1017
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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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