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Structure paper

TitleLocal structural preferences in shaping tau amyloid polymorphism.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 1028, Year 2024
Publish dateFeb 3, 2024
AuthorsNikolaos Louros / Martin Wilkinson / Grigoria Tsaka / Meine Ramakers / Chiara Morelli / Teresa Garcia / Rodrigo Gallardo / Sam D'Haeyer / Vera Goossens / Dominique Audenaert / Dietmar Rudolf Thal / Ian R Mackenzie / Rosa Rademakers / Neil A Ranson / Sheena E Radford / Frederic Rousseau / Joost Schymkowitz /
PubMed AbstractTauopathies encompass a group of neurodegenerative disorders characterised by diverse tau amyloid fibril structures. The persistence of polymorphism across tauopathies suggests that distinct ...Tauopathies encompass a group of neurodegenerative disorders characterised by diverse tau amyloid fibril structures. The persistence of polymorphism across tauopathies suggests that distinct pathological conditions dictate the adopted polymorph for each disease. However, the extent to which intrinsic structural tendencies of tau amyloid cores contribute to fibril polymorphism remains uncertain. Using a combination of experimental approaches, we here identify a new amyloidogenic motif, PAM4 (Polymorphic Amyloid Motif of Repeat 4), as a significant contributor to tau polymorphism. Calculation of per-residue contributions to the stability of the fibril cores of different pathologic tau structures suggests that PAM4 plays a central role in preserving structural integrity across amyloid polymorphs. Consistent with this, cryo-EM structural analysis of fibrils formed from a synthetic PAM4 peptide shows that the sequence adopts alternative structures that closely correspond to distinct disease-associated tau strains. Furthermore, in-cell experiments revealed that PAM4 deletion hampers the cellular seeding efficiency of tau aggregates extracted from Alzheimer's disease, corticobasal degeneration, and progressive supranuclear palsy patients, underscoring PAM4's pivotal role in these tauopathies. Together, our results highlight the importance of the intrinsic structural propensity of amyloid core segments to determine the structure of tau in cells, and in propagating amyloid structures in disease.
External linksNat Commun / PubMed:38310108 / PubMed Central
MethodsEM (helical sym.)
Resolution2.6 - 2.9 Å
Structure data

16876

8oh2

EMDB-16876, PDB-8oh2:
Structure of the Tau-PAM4 Type 1 amyloid fibril
Method: EM (helical sym.) / Resolution: 2.6 Å

16881

8ohi

EMDB-16881, PDB-8ohi:
Structure of the Fmoc-Tau-PAM4 Type 2 amyloid fibril
Method: EM (helical sym.) / Resolution: 2.8 Å

16883

8ohp

EMDB-16883, PDB-8ohp:
Structure of the Fmoc-Tau-PAM4 Type 3 amyloid fibril
Method: EM (helical sym.) / Resolution: 2.7 Å

16886

8oi0

EMDB-16886, PDB-8oi0:
Structure of the Fmoc-Tau-PAM4 Type 4 amyloid fibril
Method: EM (helical sym.) / Resolution: 2.9 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • synthetic construct (others)
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / amyloid / tau / helical / cross-beta / fibril / neurodegeneration / Fmoc

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