ArticleScience advances2025
Chaperone-mediated heterotypic phase separation regulates liquid-to-solid phase transitions of tau into amyloid fibrils.
Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Beyond the structure-function paradigm: A comprehensive review of intrinsically disordered proteins.Biochemistry and biophysics reports · 2026Review
- Alzheimer's Disease as a Multi-Layer Network Disorder: A Systems Biology Framework Integrating Multi-Omics Mechanisms.Biomedicines · 2026Review
- Redox-Dependent Chaperoning of GBF1 Condensates Regulates Seed Germination in Arabidopsis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Riboregulation: a non-canonical tau function.Molecular neurodegeneration · 2026Review
- Engineering Design of Artificial Phase-Separating Proteins.Biotechnology journal · 2026Review
- Alzheimer's Disease: From Pathogenesis to Emerging Therapeutic Targets.Journal of clinical medicine · 2026Review
- Physiological and pathological roles of ANXA11: a multifunctional regulator in neurodegeneration and other disorders.Cell communication and signaling : CCS · 2026Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biomolecular condensates formed via phase separation of proteins, and nucleic acids regulate crucial cellular processes. However, such liquid-like membraneless bodies can undergo aberrant liquid-to-solid transitions into amyloid-like pathological species, which necessitates their efficient clearance by the cellular protein quality control machinery comprising molecular chaperones. We present a unique case to demonstrate that a heat shock protein 40 (Ydj1) promotes the heterotypic phase separation of intrinsically disordered tau via a multitude of interactions. Using multicolor imaging, time-resolved fluorescence anisotropy, vibrational Raman spectroscopy, and single-molecule Förster resonance energy transfer, we unmask the crucial molecular events associated with heterotypic phase separation of tau. We show that the presence of Ydj1 within condensates abolishes phase transitions into amyloids, unlike tau-only droplets that spontaneously mature into amyloid fibrils. We identify the amyloidogenic hexapeptide motifs located in the hydrophobic microtubule-binding region of tau that interacts with the peptide-binding regions of Ydj1 promoting tau-Ydj1 condensate formation. Our results provide mechanistic underpinnings of condensate-mediated protein homeostasis.
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Registered trials
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