The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress
Open accessAbstract
The heat-shock response is a complex cellular program that induces major changes in protein translation, folding and degradation to alleviate toxicity caused by protein misfolding. Although heat shock has been widely used to study proteostasis, it remained unclear how misfolded proteins are targeted for proteolysis in these conditions. We found that Rsp5 and its mammalian homologue Nedd4 are important E3 ligases responsible for the increased ubiquitylation induced by heat stress. We determined that Rsp5 ubiquitylates mainly cytosolic misfolded proteins upon heat shock for proteasome degradation. We found that ubiquitylation of heat-induced substrates requires the Hsp40 co-chaperone Ydj1 that is further associated with Rsp5 upon heat shock. In addition, ubiquitylation is also promoted by PY Rsp5-binding motifs found primarily in the structured regions of stress-induced substrates, which can act as heat-induced degrons. Our results support a bipartite recognition mechanism combining direct and chaperone-dependent ubiquitylation of misfolded cytosolic proteins by Rsp5.
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Cites
Global analysis of protein localization in budding yeast
Huh, W.-K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., & O'Shea, E. K. (2003) · Nature · doi:10.1038/nature02026 · Cited by 4,248
Global analysis of protein expression in yeast
Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750
Exploration of Essential Gene Functions via Titratable Promoter Alleles
Mnaimneh, S., Davierwala, A. P., Haynes, J., Moffat, J., Peng, W.-T., Zhang, W., Yang, X., Pootoolal, J., Chua, G., Lopez, A., et al. (2004) · Cell · doi:10.1016/j.cell.2004.06.013 · Cited by 604
Cited by
Protein aggregation as a mechanism of adaptive cellular responses
Saarikangas, J., & Barral, Y. (2016) · Current Genetics · doi:10.1007/s00294-016-0596-0 · Cited by 67
Cuinat, S., Bézieau, S., Deb, W., Mercier, S., Vignard, V., Isidor, B., Küry, S., & Ebstein, F. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2023.101130 · Cited by 10
Metadata
- Authors
- Fang, N. N., Chan, G. T., Zhu, M., Comyn, S. A., Persaud, A., Deshaies, R. J., Rotin, D., Gsponer, J., & Mayor, T.
- Venue
- Nature Cell Biology
- Published
- 2014-10-26
- Volume
- 16
- Issue
- 12
- Pages
- 1227-1237
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2028380145
- Cited by
- 182
- References
- 3
- FWCI
- 7.30
- Type
- journal article
- Language
- en
- Open access
- green
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- Fang, N. N., Chan, G. T., Zhu, M., Comyn, S. A., Persaud, A., Deshaies, R. J., Rotin, D., Gsponer, J., & Mayor, T. (2014). Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress. Nature Cell Biology. https://doi.org/10.1038/ncb3054
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