- Title
- CHIP: a co-chaperone for degradation by the proteasome
- Creator
- Edkins, Adrienne L
- Date
- 2015
- Type
- text
- Type
- book
- Identifier
- http://hdl.handle.net/10962/164863
- Identifier
- vital:41179
- Identifier
- ISBN 978-3-319-11730-0
- Identifier
- DOI: 10.1007/978-3-319-11731-7_11
- Description
- Protein homeostasis relies on a balance between protein folding and protein degradation. Molecular chaperones like Hsp70 and Hsp90 fulfil well-defined roles in protein folding and conformational stability via ATP dependent reaction cycles. These folding cycles are controlled by associations with a cohort of non-client protein co-chaperones, such as Hop, p23 and Aha1. Pro-folding co-chaperones facilitate the transit of the client protein through the chaperone mediated folding process. However, chaperones are also involved in ubiquitin-mediated proteasomal degradation of client proteins. Similar to folding complexes, the ability of chaperones to mediate protein degradation is regulated by co-chaperones, such as the C terminal Hsp70 binding protein (CHIP).
- Format
- 24 pages, pdf
- Publisher
- Springer
- Language
- English
- Relation
- Edkins, A.L., 2015. CHIP: a co-chaperone for degradation by the proteasome. In The Networking of Chaperones by Co-chaperones (pp. 219-242). Springer, Cham
- Rights
- Publisher
- Rights
- Use of this resource is governed by the terms and conditions of the SpringerLink Terms of Use Statement ( https://link.springer.com/termsandconditions)
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RU Department of Biochemistry, Microbiology and Bioinformatics
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| Thumbnail | File | Description | Size | Format | |||
|---|---|---|---|---|---|---|---|
| View Details Download | SOURCE1 | CHIP.pdf | 576 KB | Adobe Acrobat PDF | View Details Download |