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000275936 041__ $$aEnglish
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000275936 1001_ $$0P:(DE-2719)2812532$$aChakraborty, Pijush$$b0$$udzne
000275936 245__ $$aInterplay of p23 with FKBP51 and their chaperone complex in regulating tau aggregation.
000275936 260__ $$a[London]$$bSpringer Nature$$c2025
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000275936 520__ $$aThe pathological deposition of tau and amyloid-beta into insoluble amyloid fibrils are pathological hallmarks of Alzheimer's disease. Molecular chaperones are important cellular factors contributing to the regulation of tau misfolding and aggregation. Here we reveal an Hsp90-independent mechanism by which the co-chaperone p23 as well as a molecular complex formed by two co-chaperones, p23 and FKBP51, modulates tau aggregation. Integrating NMR spectroscopy, SAXS, molecular docking, and site-directed mutagenesis we reveal the structural basis of the p23-FKBP51 complex. We show that p23 specifically recognizes the TPR domain of FKBP51 and interacts with tau through its C-terminal disordered tail. We further show that the p23-FKBP51 complex binds tau to form a dynamic p23-FKBP51-tau trimeric complex that delays tau aggregation and thus may counteract Hsp90-FKBP51 mediated toxicity. Taken together, our findings reveal a co-chaperone mediated Hsp90-independent chaperoning of tau protein.
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000275936 650_7 $$2NLM Chemicals$$atau Proteins
000275936 650_7 $$0EC 5.2.1.-$$2NLM Chemicals$$aTacrolimus Binding Proteins
000275936 650_7 $$0EC 5.2.1.8$$2NLM Chemicals$$atacrolimus binding protein 5
000275936 650_7 $$2NLM Chemicals$$aMolecular Chaperones
000275936 650_7 $$2NLM Chemicals$$aHSP90 Heat-Shock Proteins
000275936 650_7 $$0EC 5.3.99.3$$2NLM Chemicals$$aProstaglandin-E Synthases
000275936 650_7 $$2NLM Chemicals$$aMAPT protein, human
000275936 650_7 $$2NLM Chemicals$$aDNAJA1 protein, human
000275936 650_7 $$2NLM Chemicals$$aProtein Aggregates
000275936 650_7 $$2NLM Chemicals$$aHSP40 Heat-Shock Proteins
000275936 650_2 $$2MeSH$$atau Proteins: metabolism
000275936 650_2 $$2MeSH$$atau Proteins: chemistry
000275936 650_2 $$2MeSH$$atau Proteins: genetics
000275936 650_2 $$2MeSH$$aTacrolimus Binding Proteins: metabolism
000275936 650_2 $$2MeSH$$aTacrolimus Binding Proteins: genetics
000275936 650_2 $$2MeSH$$aHumans
000275936 650_2 $$2MeSH$$aMolecular Chaperones: metabolism
000275936 650_2 $$2MeSH$$aHSP90 Heat-Shock Proteins: metabolism
000275936 650_2 $$2MeSH$$aHSP90 Heat-Shock Proteins: genetics
000275936 650_2 $$2MeSH$$aProstaglandin-E Synthases: metabolism
000275936 650_2 $$2MeSH$$aProstaglandin-E Synthases: genetics
000275936 650_2 $$2MeSH$$aProtein Binding
000275936 650_2 $$2MeSH$$aMolecular Docking Simulation
000275936 650_2 $$2MeSH$$aAlzheimer Disease: metabolism
000275936 650_2 $$2MeSH$$aAlzheimer Disease: genetics
000275936 650_2 $$2MeSH$$aAlzheimer Disease: pathology
000275936 650_2 $$2MeSH$$aProtein Aggregates
000275936 650_2 $$2MeSH$$aProtein Aggregation, Pathological: metabolism
000275936 650_2 $$2MeSH$$aScattering, Small Angle
000275936 650_2 $$2MeSH$$aHSP40 Heat-Shock Proteins
000275936 7001_ $$0P:(DE-2719)2810591$$aZweckstetter, Markus$$b1$$eLast author
000275936 773__ $$0PERI:(DE-600)2553671-0$$a10.1038/s41467-025-56028-0$$gVol. 16, no. 1, p. 669$$n1$$p669$$tNature Communications$$v16$$x2041-1723$$y2025
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