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TitleStructure-based classification of tauopathies.
Journal, issue, pagesNature, Vol. 598, Issue 7880, Page 359-363, Year 2021
Publish dateSep 29, 2021
AuthorsYang Shi / Wenjuan Zhang / Yang Yang / Alexey G Murzin / Benjamin Falcon / Abhay Kotecha / Mike van Beers / Airi Tarutani / Fuyuki Kametani / Holly J Garringer / Ruben Vidal / Grace I Hallinan / Tammaryn Lashley / Yuko Saito / Shigeo Murayama / Mari Yoshida / Hidetomo Tanaka / Akiyoshi Kakita / Takeshi Ikeuchi / Andrew C Robinson / David M A Mann / Gabor G Kovacs / Tamas Revesz / Bernardino Ghetti / Masato Hasegawa / Michel Goedert / Sjors H W Scheres /
PubMed AbstractThe ordered assembly of tau protein into filaments characterizes several neurodegenerative diseases, which are called tauopathies. It was previously reported that, by cryo-electron microscopy, the ...The ordered assembly of tau protein into filaments characterizes several neurodegenerative diseases, which are called tauopathies. It was previously reported that, by cryo-electron microscopy, the structures of tau filaments from Alzheimer's disease, Pick's disease, chronic traumatic encephalopathy and corticobasal degeneration are distinct. Here we show that the structures of tau filaments from progressive supranuclear palsy (PSP) define a new three-layered fold. Moreover, the structures of tau filaments from globular glial tauopathy are similar to those from PSP. The tau filament fold of argyrophilic grain disease (AGD) differs, instead resembling the four-layered fold of corticobasal degeneration. The AGD fold is also observed in ageing-related tau astrogliopathy. Tau protofilament structures from inherited cases of mutations at positions +3 or +16 in intron 10 of MAPT (the microtubule-associated protein tau gene) are also identical to those from AGD, suggesting that relative overproduction of four-repeat tau can give rise to the AGD fold. Finally, the structures of tau filaments from cases of familial British dementia and familial Danish dementia are the same as those from cases of Alzheimer's disease and primary age-related tauopathy. These findings suggest a hierarchical classification of tauopathies on the basis of their filament folds, which complements clinical diagnosis and neuropathology and also allows the identification of new entities-as we show for a case diagnosed as PSP, but with filament structures that are intermediate between those of globular glial tauopathy and PSP.
External linksNature / PubMed:34588692 / PubMed Central
MethodsEM (helical sym.)
Resolution1.9 - 3.4 Å
Structure data

13218

7p65

EMDB-13218, PDB-7p65:
Progressive supranuclear palsy tau filament
Method: EM (helical sym.) / Resolution: 2.7 Å

13219

7p66

EMDB-13219, PDB-7p66:
Globular glial tauopathy type 1 tau filament
Method: EM (helical sym.) / Resolution: 3.0 Å

13220

7p67

EMDB-13220, PDB-7p67:
Globular glial tauopathy type 2 tau filament
Method: EM (helical sym.) / Resolution: 3.1 Å

13221

7p68

EMDB-13221, PDB-7p68:
Globular glial tauopathy type 3 tau filament
Method: EM (helical sym.) / Resolution: 2.9 Å

13223

7p6a

EMDB-13223, PDB-7p6a:
Limbic-predominant neuronal inclusion body 4R tauopathy type 1a tau filament
Method: EM (helical sym.) / Resolution: 1.9 Å

13224

7p6b

EMDB-13224, PDB-7p6b:
Limbic-predominant neuronal inclusion body 4R tauopathy type 1b tau filament
Method: EM (helical sym.) / Resolution: 2.2 Å

13225

7p6c

EMDB-13225, PDB-7p6c:
Limbic-predominant neuronal inclusion body 4R tauopathy type 2 tau filament
Method: EM (helical sym.) / Resolution: 2.5 Å

13226

7p6d

EMDB-13226, PDB-7p6d:
Argyrophilic grain disease type 1 tau filament
Method: EM (helical sym.) / Resolution: 3.3 Å

13227

7p6e

EMDB-13227, PDB-7p6e:
Argyrophilic grain disease type 2 tau filament
Method: EM (helical sym.) / Resolution: 3.4 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • Human (human)
KeywordsPROTEIN FIBRIL / Amyloid fibril

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