Academic Journal
Early steps of protein disaggregation by Hsp70 chaperone and class B J-domain proteins are shaped by Hsp110
| العنوان: | Early steps of protein disaggregation by Hsp70 chaperone and class B J-domain proteins are shaped by Hsp110 |
|---|---|
| المؤلفون: | Wiktoria Sztangierska, Hubert Wyszkowski, Maria Pokornowska, Klaudia Kochanowicz, Michal Rychłowski, Krzysztof Liberek, Agnieszka Kłosowska |
| المصدر: | eLife, Vol 13 (2024) |
| بيانات النشر: | eLife Sciences Publications Ltd, 2024. |
| سنة النشر: | 2024 |
| المجموعة: | LCC:Medicine LCC:Science LCC:Biology (General) |
| مصطلحات موضوعية: | protein aggregation, stress, protein quality control, heat shock protein, protein folding, Medicine, Science, Biology (General), QH301-705.5 |
| الوصف: | Hsp70 is a key cellular system counteracting protein misfolding and aggregation, associated with stress, ageing, and disease. Hsp70 solubilises aggregates and aids protein refolding through substrate binding and release cycles regulated by co-chaperones: J-domain proteins (JDPs) and nucleotide exchange factors (NEFs). Here, we elucidate the collaborative impact of Hsp110 NEFs and different JDP classes throughout Hsp70-dependent aggregate processing. We show that Hsp110 plays a major role at initial stages of disaggregation, determining its final efficacy. The NEF catalyses the recruitment of thick Hsp70 assemblies onto aggregate surface, which modifies aggregates into smaller species more readily processed by chaperones. Hsp70 stimulation by Hsp110 is much stronger with class B than class A JDPs and requires the auxiliary interaction between class B JDP and the Hsp70 EEVD motif. Furthermore, we demonstrate for the first time that Hsp110 disrupts the JDP-Hsp70 interaction. Such destabilisation of chaperone complexes at the aggregate surface might improve disaggregation, but also lead to the inhibition above the sub-stoichiometric Hsp110 optimum. Thus, balanced interplay between the co-chaperones and Hsp70 is critical to unlock its disaggregating potential. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 2050-084X |
| Relation: | https://elifesciences.org/articles/94795; https://doaj.org/toc/2050-084X |
| DOI: | 10.7554/eLife.94795 |
| URL الوصول: | https://doaj.org/article/f21c38e791d7464183add8aeaab0c303 |
| رقم الانضمام: | edsdoj.f21c38e791d7464183add8aeaab0c303 |
| قاعدة البيانات: | Directory of Open Access Journals |
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