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Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
Open accessAbstract
Dsk2p from Saccharomyces cerevisiae belongs to the class of proteins that contain a ubiquitin-like (UbL) domain at the N terminus together with a ubiquitin-associated (UBA) domain at the C terminus. We show here that the C-terminal UBA domain of Dsk2p binds to K48-linked polyubiquitin chains, and the N-terminal UbL domain of Dsk2p interacts with the proteasome. Overexpression of Dsk2p caused the accumulation of large amounts of polyubiquitin, and extragenic suppressors of the Dsk2p-mediated lethality proved to be temperature-sensitive mutations in two proteasome subunits, rpn1 and pre2. K48-linked ubiquitin-dependent degradation was impaired by disruption of the DSK2 gene. These results indicate that Dsk2p is K48-linked polyubiquitin-binding protein and also interacts with the proteasome. We discuss a possible role of adaptor function of Dsk2p via its UbL and UBA domains in the ubiquitin-proteasome pathway.
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Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872
The N-end rule: functions, mysteries, uses
Varshavsky, A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12142 · Cited by 859
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Hochstrasser, M. (2009) · Nature · doi:10.1038/nature07958 · Cited by 783
Seibenhener, M. L., Babu, J. R., Geetha, T., Wong, H. C., Krishna, N. R., & Wooten, M. W. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.18.8055-8068.2004 · Cited by 710
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Metadata
- Authors
- Funakoshi, M., Sasaki, T., Nishimoto, T., & Kobayashi, H.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2002-01-22
- Volume
- 99
- Issue
- 2
- Pages
- 745-750
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2062636623
- Cited by
- 248
- References
- 2
- FWCI
- 7.88
- Type
- journal article
- Language
- en
- Open access
- green
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