The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Ubiquitinated Proteins Activate the Proteasome by Binding to Usp14/Ubp6, which Causes 20S Gate Opening
Open accessAbstract
Summary In eukaryotic cells, ubiquitination of proteins leads to their degradation by the 26S proteasome. We tested if the ubiquitin (Ub) chain also regulates the proteasome’s capacity for proteolysis. After incubation with polyubiquitinated proteins, 26S proteasomes hydrolyzed peptides and proteins 2–7 fold faster. Ub conjugates enhanced peptide hydrolysis by stimulating gate opening in the 20S proteasome, since this stimulation was seen when this gate was closed or transiently open, but not maximally open. Gate opening requires conjugate association with Usp14/Ubp6, since it is also mediated by occupancy of the Ubp6 active site with Ub aldehyde. No stimulation was observed with 26S from Ubp6Δ mutants, but was restored by addition of Usp14/Ubp6 or an inactive Ubp6 mutant. The stimulation of gate-opening by Ub conjugates through Usp14/Ubp6 requires nucleotide binding to the gate-regulatory ATPases. This activation enhances the selectivity of the 26S proteasome for ubiquitinated proteins and links their deubiquitination to their degradation.
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Smith, D. M., Chang, S.-C., Park, S., Finley, D., Cheng, Y., & Goldberg, A. L. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.033 · Cited by 521
Self-citationBenaroudj, N., Zwickl, P., Seemüller, E., Baumeister, W., & Goldberg, A. L. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00775-x · Cited by 245
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Cited by
Deubiquitylating enzymes and drug discovery: emerging opportunities
Harrigan, J. A., Jacq, X., Martin, N. M., & Jackson, S. P. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.152 · Cited by 940
The logic of the 26S proteasome.
Collins, G. A., & Goldberg, A. L. (2017) · Cell · doi:10.1016/j.cell.2017.04.023 · Cited by 933
Self-citationEnhancement of proteasome activity by a small-molecule inhibitor of USP14
Lee, B.-H., Lee, M. J., Park, S., Oh, D.-C., Elsasser, S., Chen, P.-C., Gartner, C., Dimova, N., Hanna, J., Gygi, S. P., et al. (2010) · Nature · doi:10.1038/nature09299 · Cited by 893
Structure and Function of the 26S Proteasome
Bard, J. A. M., Goodall, E. A., Greene, E. R., Jonsson, E., Dong, K. C., & Martin, A. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-011931 · Cited by 819
Myeku, N., Clelland, C. L., Emrani, S., Kukushkin, N. V., Yu, W. H., Goldberg, A. L., & Duff, K. E. (2016) · Nature Medicine · doi:10.1038/nm.4011 · Cited by 446
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Metadata
- Authors
- Peth, A., Besche, H. C., & Goldberg, A. L.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2009-12
- Volume
- 36
- Issue
- 5
- Pages
- 794-804
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W1988100248
- Cited by
- 211
- References
- 2
- FWCI
- 4.92
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Peth, A., Besche, H. C., & Goldberg, A. L. (2009). Ubiquitinated Proteins Activate the Proteasome by Binding to Usp14/Ubp6, which Causes 20S Gate Opening. Molecular Cell. https://doi.org/10.1016/j.molcel.2009.11.015
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