ArticleeLife2016
Adenosine diphosphate restricts the protein remodeling activity of the Hsp104 chaperone to Hsp70 assisted disaggregation.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3.Cell reports · 2022Article
- Hsp104 N-terminal domain interaction with substrates plays a regulatory role in protein disaggregation.The FEBS journal · 2022Article
- Chaperones directly and efficiently disperse stress-triggered biomolecular condensates.Molecular cell · 2022Article
- Reduced ATP-dependent proteolysis of functional proteins during nutrient limitation speeds the return of microbes to a growth state.Science signaling · 2021Article
- Resisting the Heat: Bacterial Disaggregases Rescue Cells From Devastating Protein Aggregation.Frontiers in molecular biosciences · 2021Review
- ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo.Nature communications · 2020Article
- Mitochondria orchestrate proteostatic and metabolic stress responses.EMBO reports · 2019Review
- Hsp104 and Potentiated Variants Can Operate as Distinct Nonprocessive Translocases.Biophysical journal · 2019Article
- The amino-terminal domain ofFEBS open bio · 2018Article
- Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.Journal of molecular biology · 2017Article
- The growing world of small heat shock proteins: from structure to functions.Cell stress & chaperones · 2017Review
- Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.Biochemistry · 2017Article
- Crystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for the function of Hsp104 in dissolving prions.Acta crystallographica. Section D, Structural biology · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hsp104 disaggregase provides thermotolerance in yeast by recovering proteins from aggregates in cooperation with the Hsp70 chaperone. Protein disaggregation involves polypeptide extraction from aggregates and its translocation through the central channel of the Hsp104 hexamer. This process relies on adenosine triphosphate (ATP) hydrolysis. Considering that Hsp104 is characterized by low affinity towards ATP and is strongly inhibited by adenosine diphosphate (ADP), we asked how Hsp104 functions at the physiological levels of adenine nucleotides. We demonstrate that physiological levels of ADP highly limit Hsp104 activity. This inhibition, however, is moderated by the Hsp70 chaperone, which allows efficient disaggregation by supporting Hsp104 binding to aggregates but not to non-aggregated, disordered protein substrates. Our results point to an additional level of Hsp104 regulation by Hsp70, which restricts the potentially toxic protein unfolding activity of Hsp104 to the disaggregation process, providing the yeast protein-recovery system with substrate specificity and efficiency in ATP consumption.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.