ArticleThe Journal of biological chemistry2010
Hsc70 rapidly engages tau after microtubule destabilization.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 98 citations in OpenAlex.
- Implications of virus-induced stress granules in tauopathies.Translational neurodegeneration · 2026Review
- Are neurodegenerative diseases late-onset neurodevelopmental disorders? Tracing the developmental origins of neuronal vulnerability.Frontiers in neuroscience · 2026Review
- Article
- Intermediate Filament Protein BFSP2 Controls Spindle Formation via HSC70-Mediated Stabilization of CLTC During Oocyte meiosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Phosphorylation enables progressive microtubule-associated protein proteolysis and functionalisation during neural development.bioRxiv : the preprint server for biology · 2025Article
- Exploring Protein Misfolding in Amyotrophic Lateral Sclerosis: Structural and Functional Insights.Biomedicines · 2025Review
- TBG096 Ameliorates Memory Deficiency in AD Mouse Model via Promoting Neurogenesis and Regulation of Hsc70/HK2/PKM2/LAMP2A Signaling Pathway.International journal of molecular sciences · 2025Article
- Probe-dependent Proximity Profiling (ProPPr) Uncovers Similarities and Differences in Phospho-Tau-Associated Proteomes Between Tauopathies.Molecular neurodegeneration · 2025Article
- DnaJs are enriched in tau regulators.International journal of biological macromolecules · 2023Article
- Identification of gene networks mediating regional resistance to tauopathy in late-onset Alzheimer's disease.PLoS genetics · 2023Article
- Deletion of UCP1 in Tg2576 Mice Increases Body Temperature and Exacerbates Alzheimer's Disease-Related Pathologies.International journal of molecular sciences · 2023Article
- Review
- Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities.MedComm · 2022Review
- Sustained high body temperature exacerbates cognitive function and Alzheimer's disease-related pathologies.Scientific reports · 2022Article
- Structural basis for the inhibition of IAPP fibril formation by the co-chaperonin prefoldin.Nature communications · 2022Article
- Inhibitors of heat shock protein 70 (Hsp70) with enhanced metabolic stability reduce tau levels.Bioorganic & medicinal chemistry letters · 2021Article
- Hsp90 co-chaperones, FKBP52 and Aha1, promote tau pathogenesis in aged wild-type mice.Acta neuropathologica communications · 2021Article
- Tau protein- induced sequestration of the eukaryotic ribosome: Implications in neurodegenerative disease.Scientific reports · 2020Article
- Tau protein aggregates inhibit the protein-folding and vesicular trafficking arms of the cellular proteostasis network.The Journal of biological chemistry · 2019Article
- Changes in proteome solubility indicate widespread proteostatic disruption in mouse models of neurodegenerative disease.Acta neuropathologica · 2018Article
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 1 country.
Funding
Abstract
The microtubule-associated protein Tau plays a crucial role in regulating the dynamic stability of microtubules during neuronal development and synaptic transmission. In a group of neurodegenerative diseases, such as Alzheimer disease and other tauopathies, conformational changes in Tau are associated with the initial stages of disease pathology. Folding of Tau into the MC1 conformation, where the amino acids at residues 7-9 interact with residues 312-342, is one of the earliest pathological alterations of Tau in Alzheimer disease. The mechanism of this conformational change in Tau and the subsequent effect on function and association to microtubules is largely unknown. Recent work by our group and others suggests that members of the Hsp70 family play a significant role in Tau regulation. Our new findings suggest that heat shock cognate (Hsc) 70 facilitates Tau-mediated microtubule polymerization. The association of Hsc70 with Tau was rapidly enhanced following treatment with microtubule-destabilizing agents. The fate of Tau released from the microtubule was found to be dependent on ATPase activity of Hsc70. Microtubule destabilization also rapidly increased the MC1 folded conformation of Tau. An in vitro assay suggests that Hsc70 facilitates formation of MC1 Tau. However, in a hyperphosphorylating environment, the formation of MC1 was abrogated, but Hsc70 binding to Tau was enhanced. Thus, under normal circumstances, MC1 formation may be a protective conformation facilitated by Hsc70. However, in a diseased environment, Hsc70 may preserve Tau in a more unstructured state, perhaps facilitating its pathogenicity.
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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.