ArticleProceedings of the National Academy of Sciences of the United States of America2013
Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
72 citing papers in PubMed, 110 citations in OpenAlex.
- HAX1 drives assembly and activation of the mitochondrial intermembrane space chaperone CLPB.bioRxiv : the preprint server for biology · 2026Article
- When mitochondria lose their fold: matrix proteostasis and stress signaling.Frontiers in physiology · 2026Review
- HSP104 and HSP20-L Are Required by Aspergillus nidulans in Response to Attack by Fungivorous Springtail Sinella curviseta.Environmental microbiology reports · 2025Article
- Hsp90, DnaK, and ClpB collaborate in protein reactivation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Thermotolerant yeasts promoting climate-resilient bioproduction.FEMS yeast research · 2025Review
- Design principles to tailor Hsp104 therapeutics.Cell reports · 2024Article
- The middle domain of Hsp104 can ensure substrates are functional after processing.PLoS genetics · 2024Article
- Design principles to tailor Hsp104 therapeutics.bioRxiv : the preprint server for biology · 2024Article
- The yeast guanine nucleotide exchange factor Sec7 is a bottleneck in spatial protein quality control and detoxifies neurological disease proteins.Scientific reports · 2023Article
- Structural basis of impaired disaggregase function in the oxidation-sensitive SKD3 mutant causing 3-methylglutaconic aciduria.Nature communications · 2023Article
- Hsp70 Binding to the N-terminal Domain of Hsp104 Regulates [Molecular and cellular biology · 2023Article
- Deciphering the mechanism and function of Hsp100 unfoldases from protein structure.Biochemical Society transactions · 2022Article
- Hsp104 N-terminal domain interaction with substrates plays a regulatory role in protein disaggregation.The FEBS journal · 2022Article
- Molecular mechanisms of amyloid disaggregation.Journal of advanced research · 2022Review
- Class-specific interactions between Sis1 J-domain protein and Hsp70 chaperone potentiate disaggregation of misfolded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex.Nature communications · 2021Article
- Differential role of cytosolic Hsp70s in longevity assurance and protein quality control.PLoS genetics · 2021Article
- Resisting the Heat: Bacterial Disaggregases Rescue Cells From Devastating Protein Aggregation.Frontiers in molecular biosciences · 2021Review
- Article
- Growth-Regulated Hsp70 Phosphorylation Regulates Stress Responses and Prion Maintenance.Molecular and cellular biology · 2020Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Heat shock protein (Hsp) 104 is a ring-forming, protein-remodeling machine that harnesses the energy of ATP binding and hydrolysis to drive protein disaggregation. Although Hsp104 is an active ATPase, the recovery of functional protein requires the species-specific cooperation of the Hsp70 system. However, like Hsp104, Hsp70 is an active ATPase, which recognizes aggregated and aggregation-prone proteins, making it difficult to differentiate the mechanistic roles of Hsp104 and Hsp70 during protein disaggregation. Mapping the Hsp70-binding sites in yeast Hsp104 using peptide array technology and photo-cross-linking revealed a striking conservation of the primary Hsp70-binding motifs on the Hsp104 middle-domain across species, despite lack of sequence identity. Remarkably, inserting a Strep-Tactin binding motif at the spatially conserved Hsp70-binding site elicits the Hsp104 protein disaggregating activity that now depends on Strep-Tactin but no longer requires Hsp70/40. Consistent with a Strep-Tactin-dependent activation step, we found that full-length Hsp70 on its own could activate the Hsp104 hexamer by promoting intersubunit coordination, suggesting that Hsp70 is an activator of the Hsp104 motor.
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Registered trials
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.