The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis
Open accessAbstract
The pathways that distinguish transport of folded and misfolded cargo through the exocytic (secretory) pathway of eukaryotic cells remain unknown. Using proteomics to assess global cystic fibrosis (CF) transmembrane conductance regulator (CFTR) protein interactions (the CFTR interactome), we show that Hsp90 cochaperones modulate Hsp90-dependent stability of CFTR protein folding in the endoplasmic reticulum (ER). Cell-surface rescue of the most common disease variant that is restricted to the ER, DeltaF508, can be initiated by partial siRNA silencing of the Hsp90 cochaperone ATPase regulator Aha1. We propose that failure of DeltaF508 to achieve an energetically favorable fold in response to the steady-state dynamics of the chaperone folding environment (the "chaperome") is responsible for the pathophysiology of CF. The activity of cargo-associated chaperome components may be a common mechanism regulating folding for ER exit, providing a general framework for correction of misfolding disease.
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Cites
Large-scale analysis of the yeast proteome by multidimensional protein identification technology
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Self-citationTHE MAMMALIAN UNFOLDED PROTEIN RESPONSE
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The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
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BI-DIRECTIONAL PROTEIN TRANSPORT BETWEEN THE ER AND GOLGI
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Regulation of Longevity in Caenorhabditis elegans by Heat Shock Factor and Molecular Chaperones
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Progressive disruption of cellular protein folding in models of polyglutamine diseases
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Hsp70 and Hsp90—a relay team for protein folding
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Activation of the ATPase Activity of Hsp90 by the Stress-Regulated Cochaperone Aha1
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Cited by
Adapting Proteostasis for Disease Intervention
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Self-citationHSP90 at the hub of protein homeostasis: emerging mechanistic insights
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Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
Morimoto, R. I. (2008) · Genes & Development · doi:10.1101/gad.1657108 · Cited by 872
Metadata
- Authors
- Wang, X., Venable, J., LaPointe, P., Hutt, D. M., Koulov, A. V., Coppinger, J., Gurkan, C., Kellner, W., Matteson, J., Plutner, H., Riordan, J. R., Kelly, J. W., Yates, J. R., & Balch, W. E.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2006-11
- Volume
- 127
- Issue
- 4
- Pages
- 803-815
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2159997339
- Cited by
- 601
- References
- 38
- FWCI
- 13.75
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis. https://app.cochat.ai/papers/10.1016/j.cell.2006.09.043
- The paper
- Wang, X., Venable, J., LaPointe, P., Hutt, D. M., Koulov, A. V., Coppinger, J., Gurkan, C., Kellner, W., Matteson, J., Plutner, H., Riordan, J. R., Kelly, J. W., Yates, J. R., & Balch, W. E. (2006). Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis. Cell. https://doi.org/10.1016/j.cell.2006.09.043
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