The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
A Quantitative Chaperone Interaction Network Reveals the Architecture of Cellular Protein Homeostasis Pathways
Open accessAbstract
Chaperones are abundant cellular proteins that promote the folding and function of their substrate proteins (clients). In vivo, chaperones also associate with a large and diverse set of co-factors (co-chaperones) that regulate their specificity and function. However, how these co-chaperones regulate protein folding and whether they have chaperone-independent biological functions is largely unknown. We have combined mass spectrometry and quantitative high-throughput LUMIER assays to systematically characterize the chaperone/co-chaperone/client interaction network in human cells. We uncover hundreds of novel chaperone clients, delineate their participation in specific co-chaperone complexes, and establish a surprisingly distinct network of protein/protein interactions for co-chaperones. As a salient example of the power of such analysis, we establish that NUDC family co-chaperones specifically associate with structurally related but evolutionarily distinct β-propeller folds. We provide a framework for deciphering the proteostasis network, its regulation in development and disease, and expand the use of chaperones as sensors for drug/target engagement.
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Cites
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“Some ‘‘cochaperones’’ possess intrinsic chaperone activity themselves (Freeman et al., 1996) and others independently regulate cellular processes that are distinct from those of the canonical chaperones (Echtenkamp et al., 2011).”
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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
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In vivo aspects of protein folding and quality control
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Metadata
- Authors
- Taipale, M., Tucker, G., Peng, J., Krykbaeva, I., Lin, Z.-Y., Larsen, B., Choi, H., Berger, B., Gingras, A.-C., & Lindquist, S.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2014-07
- Volume
- 158
- Issue
- 2
- Pages
- 434-448
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2078021348
- Cited by
- 392
- References
- 13
- FWCI
- 14.11
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Taipale, M., Tucker, G., Peng, J., Krykbaeva, I., Lin, Z.-Y., Larsen, B., Choi, H., Berger, B., Gingras, A.-C., & Lindquist, S. (2014). A Quantitative Chaperone Interaction Network Reveals the Architecture of Cellular Protein Homeostasis Pathways. Cell. https://doi.org/10.1016/j.cell.2014.05.039
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