Hsp70-mediated quality control: should I stay or should I go?
Abstract: Chaperones of the 70 kDa heat shock protein (Hsp70) superfamily are key components of the cellular proteostasis system. Together with its co-chaperones, Hsp70 forms proteostasis subsystems that antagonize protein damage during physiological and stress conditions. This function stems from highly regulated binding and release cycles of protein substrates, which results in a flow of unfolded, partially folded and misfolded species through the Hsp70 subsystem. Specific factors control how Hsp70 makes decisions regarding folding and degradation fates of the substrate proteins. In this review, we summarize how the flow of Hsp70 substrates is controlled in the cell with special emphasis on recent advances regarding substrate release mechanisms.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Hsp70-mediated quality control: should I stay or should I go? ; volume:401 ; number:11 ; year:2020 ; pages:1233-1248 ; extent:16
Biological chemistry ; 401, Heft 11 (2020), 1233-1248 (gesamt 16)
- Creator
- DOI
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10.1515/hsz-2020-0187
- URN
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urn:nbn:de:101:1-2408061611501.972512849787
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:58 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Kohler, Verena
- Andréasson, Claes
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