The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
The Ubiquitin-related BAG-1 Provides a Link between the Molecular Chaperones Hsc70/Hsp70 and the Proteasome
Open accessAbstract
The BAG-1 protein modulates the chaperone activity of Hsc70 and Hsp70 in the mammalian cytosol and nucleus. Remarkably, BAG-1 possesses a ubiquitin-like domain at its amino terminus, suggesting a link to the ubiquitin/proteasome system. Here we show that BAG-1 is indeed associated with the 26 S proteasome in HeLa cells. Binding of the chaperone cofactor to the proteolytic complex is regulated by ATP hydrolysis and is not mediated by Hsc70 and Hsp70. The presented findings reveal a role of BAG-1 as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. In fact, targeting of BAG-1 to the proteasome promotes an association of the chaperones with the proteolytic complex in vitro and in vivo. A regulatory function of the chaperone cofactor at the interface between protein folding and protein degradation is thus indicated.
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Cites
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Cited by
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Self-citationProtein quality control during aging involves recruitment of the macroautophagy pathway by BAG3
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Metadata
- Authors
- Lüders, J., Demand, J., & Höhfeld, J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-02
- Volume
- 275
- Issue
- 7
- Pages
- 4613-4617
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2073991273
- Cited by
- 489
- References
- 46
- FWCI
- 11.38
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Lüders, J., Demand, J., & Höhfeld, J. (2000). The Ubiquitin-related BAG-1 Provides a Link between the Molecular Chaperones Hsc70/Hsp70 and the Proteasome. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.275.7.4613
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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