Dataset Information

Single particle cryo-EM dataset of sarkosyl-insoluble fraction from the frontal cortex of an individual with Type I globular glial tauopathy

ABSTRACT:

SUBMITTER: Yang Shi

PROVIDER: EMPIAR-10766 | biostudies-other |

REPOSITORIES: biostudies-other

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Publications

Structure-based classification of tauopathies.

Shi Yang Y Zhang Wenjuan W Yang Yang Y Murzin Alexey G AG Falcon Benjamin B Kotecha Abhay A van Beers Mike M Tarutani Airi A Kametani Fuyuki F Garringer Holly J HJ Vidal Ruben R Hallinan Grace I GI Lashley Tammaryn T Saito Yuko Y Murayama Shigeo S Yoshida Mari M Tanaka Hidetomo H Kakita Akiyoshi A Ikeuchi Takeshi T Robinson Andrew C AC Mann David M A DMA Kovacs Gabor G GG Revesz Tamas T Ghetti Bernardino B Hasegawa Masato M Goedert Michel M Scheres Sjors H W SHW

Nature 20210929 7880

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 disease1,2, Pick's disease3, chronic traumatic encephalopathy4 and corticobasal degeneration5 are distinct. Here we show that the structures of tau filaments from progressive supranuclear palsy (PSP) define a new ...[more]

PMID: 34588692

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Project description:Tauopathies are neurodegenerative disorders characterized by aggregation of microtubule associated tau protein in neurons and glia. They are clinically and pathologically heterogeneous depending on the isoform of tau protein that accumulates (three or four 31-to-32-amino-acid repeats [3R or 4R] in the microtubule binding domain), as well as the cellular and neuroanatomical distribution of tau pathology. Growing evidence suggests that distinct tau conformers may contribute to the characteristic features of various tauopathies. Globular glial tauopathy (GGT) is a rare 4R tauopathy with globular cytoplasmic inclusions within neurons and glial cells. Given the unique cellular distribution and morphology of tau pathology in GGT, we sought to determine if tau species in GGT had distinctive biological properties. To address this question, we performed seeding analyses with postmortem brain tissues using a commercial tau biosensor cell line. We found that brain lysates from GGT cases had significantly higher seeding competency than other tauopathies, including corticobasal degeneration (CBD), progressive supranuclear palsy (PSP), and Alzheimer's disease (AD). The robust seeding activity of GGT brain lysates was independent of phosphorylated tau burden and diminished upon removal of tau from samples, suggesting that seeding properties were indeed mediated by tau in the lysates. In addition, cellular inclusions in the tau biosensor cell line induced by GGT had a distinct, globular morphology that was markedly different from inclusions induced by other tauopathies, further highlighting the unique nature of tau species in GGT. Characterization of different tau species in GGT showed that detergent-insoluble, fibril-like tau contained the highest seeding activity, as reflected in its ability to increase tau aggregation in primary glial cultures. Taken together, our data suggest that unique seeding properties differentiate GGT-tau from other tauopathies, which provides new insight into pathogenic heterogeneity of primary neurodegenerative tauopathies.

Dataset Information

Single particle cryo-EM dataset of sarkosyl-insoluble fraction from the frontal cortex of an individual with Type I globular glial tauopathy

Publications

Structure-based classification of tauopathies.

Similar Datasets

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