ArticleThe Journal of biological chemistry2011
Ordered assembly of heat shock proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Ferguson Plot Analysis of Chaperone ClpB from Moderate Halophile.The protein journal · 2025Article
- Inhibitors and chemical probes for molecular chaperone networks.The Journal of biological chemistry · 2019Review
- Synthesis and evaluation of esterified Hsp70 agonists in cellular models of protein aggregation and folding.Bioorganic & medicinal chemistry · 2019Article
- The Ubiquitination, Disaggregation and Proteasomal Degradation Machineries in Polyglutamine Disease.Frontiers in molecular neuroscience · 2017Review
- The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation.Prion · 2016Article
- Multiple discrete soluble aggregates influence polyglutamine toxicity in a Huntington's disease model system.Scientific reports · 2016Article
- Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity.Disease models & mechanisms · 2016Review
- Dynamic droplets: the role of cytoplasmic inclusions in stress, function, and disease.Cellular and molecular life sciences : CMLS · 2015Review
- Direct and Propagated Effects of Small Molecules on Protein-Protein Interaction Networks.Frontiers in bioengineering and biotechnology · 2015Review
- High-throughput screen of natural product extracts in a yeast model of polyglutamine proteotoxicity.Chemical biology & drug design · 2014Article
- Membrane trafficking in neuronal maintenance and degeneration.Cellular and molecular life sciences : CMLS · 2013Review
- Opportunities and challenges for molecular chaperone modulation to treat protein-conformational brain diseases.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2013Review
- Synthesis and initial evaluation of YM-08, a blood-brain barrier permeable derivative of the heat shock protein 70 (Hsp70) inhibitor MKT-077, which reduces tau levels.ACS chemical neuroscience · 2013Article
- Chaperone-dependent Neurodegeneration: A Molecular Perspective on Therapeutic Intervention.Journal of Alzheimer's disease & Parkinsonism · 2013Article
- Hsp70 protein complexes as drug targets.Current pharmaceutical design · 2013Review
- Pharmacological tuning of heat shock protein 70 modulates polyglutamine toxicity and aggregation.ACS chemical biology · 2012Article
- Article
- Contribution of yeast models to neurodegeneration research.Journal of biomedicine & biotechnology · 2012Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
In Saccharomyces cerevisae, expanded polyglutamine (polyQ) fragments are assembled into discrete cytosolic aggregates in a process regulated by the molecular chaperones Hsp26, Hsp70, Hsp90, and Hsp104. To better understand how the different chaperones might cooperate during polyQ aggregation, we used sequential immunoprecipitations and mass spectrometry to identify proteins associated with either soluble (Q25) or aggregation-prone (Q103) fragments at both early and later times after induction of their expression. We found that Hsp26, Hsp70, Hsp90, and other chaperones interact with Q103, but not Q25, within the first 2 h. Further, Hsp70 and Hsp90 appear to be partially released from Q103 prior to the maturation of the aggregates and before the recruitment of Hsp104. To test the importance of this seemingly ordered process, we used a chemical probe to artificially enhance Hsp70 binding to Q103. This treatment retained both Hsp70 and Hsp90 on the polyQ fragment and, interestingly, limited subsequent exchange for Hsp26 and Hsp104, resulting in incomplete aggregation. Together, these results suggest that partial release of Hsp70 may be an essential step in the continued processing of expanded polyQ fragments in yeast.
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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.