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TitleWater-directed pinning is key to tau prion formation.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 18, Page e2421391122, Year 2025
Publish dateMay 6, 2025
AuthorsMichael P Vigers / Samuel Lobo / Saeed Najafi / Austin Dubose / Karen Tsay / Pritam Ganguly / Andrew P Longhini / Yingying Jin / Steven K Buratto / Kenneth S Kosik / M Scott Shell / Joan-Emma Shea / Songi Han /
PubMed AbstractTau forms fibrillar aggregates that are pathological hallmarks of a family of neurodegenerative diseases known as tauopathies. The synthetic replication of disease-specific fibril structures is a ...Tau forms fibrillar aggregates that are pathological hallmarks of a family of neurodegenerative diseases known as tauopathies. The synthetic replication of disease-specific fibril structures is a critical gap for developing diagnostic and therapeutic tools. This study debuts a strategy of identifying a critical and minimal folding motif in fibrils characteristic of tauopathies and generating seeding-competent fibrils from the isolated tau peptides. The 19-residue jR2R3 peptide (295 to 313) which spans the R2/R3 splice junction of tau, and includes the P301L mutation, is one such peptide that forms prion-competent fibrils. This tau fragment contains the hydrophobic VQIVYK hexapeptide that is part of the core of all known pathological tau fibril structures and an intramolecular counterstrand that stabilizes the strand-loop-strand (SLS) motif observed in 4R tauopathy fibrils. This study shows that P301L exhibits a duality of effects: it lowers the barrier for the peptide to adopt aggregation-prone conformations and enhances the local structuring of water around the mutation site to facilitate site-directed pinning and dewetting around sites 300-301 to achieve in-register stacking of tau to cross β-sheets. We solved a 3 Å cryo-EM structure of jR2R3-P301L fibrils in which each protofilament layer contains two jR2R3-P301L copies, of which one adopts a SLS fold found in 4R tauopathies and the other wraps around the SLS fold to stabilize it, reminiscent of the three- and fourfold structures observed in 4R tauopathies. These jR2R3-P301L fibrils are competent to template full-length 4R tau in a prion-like manner.
External linksProc Natl Acad Sci U S A / PubMed:40294272 / PubMed Central
MethodsEM (helical sym.)
Resolution3.0 Å
Structure data

42886

8v1n

EMDB-42886, PDB-8v1n:
Cryo-EM structure of tau filaments made from jR2R3-P301L peptides induced with heparin
Method: EM (helical sym.) / Resolution: 3.0 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / tau / amyloid / filament / P301L

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