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TitleAge-dependent formation of TMEM106B amyloid filaments in human brains.
Journal, issue, pagesNature, Vol. 605, Issue 7909, Page 310-314, Year 2022
Publish dateMar 28, 2022
AuthorsManuel Schweighauser / Diana Arseni / Mehtap Bacioglu / Melissa Huang / Sofia Lövestam / Yang Shi / Yang Yang / Wenjuan Zhang / Abhay Kotecha / Holly J Garringer / Ruben Vidal / Grace I Hallinan / Kathy L Newell / Airi Tarutani / Shigeo Murayama / Masayuki Miyazaki / Yuko Saito / Mari Yoshida / Kazuko Hasegawa / Tammaryn Lashley / Tamas Revesz / Gabor G Kovacs / John van Swieten / Masaki Takao / Masato Hasegawa / Bernardino Ghetti / Maria Grazia Spillantini / Benjamin Ryskeldi-Falcon / Alexey G Murzin / Michel Goedert / Sjors H W Scheres /
PubMed AbstractMany age-dependent neurodegenerative diseases, such as Alzheimer's and Parkinson's, are characterized by abundant inclusions of amyloid filaments. Filamentous inclusions of the proteins tau, amyloid- ...Many age-dependent neurodegenerative diseases, such as Alzheimer's and Parkinson's, are characterized by abundant inclusions of amyloid filaments. Filamentous inclusions of the proteins tau, amyloid-β, α-synuclein and transactive response DNA-binding protein (TARDBP; also known as TDP-43) are the most common. Here we used structure determination by cryogenic electron microscopy to show that residues 120-254 of the lysosomal type II transmembrane protein 106B (TMEM106B) also form amyloid filaments in human brains. We determined the structures of TMEM106B filaments from a number of brain regions of 22 individuals with abundant amyloid deposits, including those resulting from sporadic and inherited tauopathies, amyloid-β amyloidoses, synucleinopathies and TDP-43 proteinopathies, as well as from the frontal cortex of 3 individuals with normal neurology and no or only a few amyloid deposits. We observed three TMEM106B folds, with no clear relationships between folds and diseases. TMEM106B filaments correlated with the presence of a 29-kDa sarkosyl-insoluble fragment and globular cytoplasmic inclusions, as detected by an antibody specific to the carboxy-terminal region of TMEM106B. The identification of TMEM106B filaments in the brains of older, but not younger, individuals with normal neurology indicates that they form in an age-dependent manner.
External linksNature / PubMed:35344985 / PubMed Central
MethodsEM (helical sym.)
Resolution2.64 - 3.64 Å
Structure data

14174

7qvc

EMDB-14174, PDB-7qvc:
TMEM106B filaments with Fold I from Alzheimer's disease (case 1)
Method: EM (helical sym.) / Resolution: 2.64 Å

14176

7qvf

EMDB-14176, PDB-7qvf:
TMEM106B filaments with Fold I-d from Multiple system atrophy (case 18)
Method: EM (helical sym.) / Resolution: 3.64 Å

14187

7qwg

EMDB-14187, PDB-7qwg:
TMEM106B filaments with Fold IIa from Multiple system atrophy (case 19)
Method: EM (helical sym.) / Resolution: 3.38 Å

14188

7qwl

EMDB-14188, PDB-7qwl:
TMEM106B filaments with Fold IIb from Multiple system atrophy (case 19)
Method: EM (helical sym.) / Resolution: 3.47 Å

14189

7qwm

EMDB-14189, PDB-7qwm:
TMEM106B filaments with Fold III from Multiple system atrophy (case 17)
Method: EM (helical sym.) / Resolution: 2.76 Å

Source
  • homo sapiens (human)
  • human (human)
KeywordsPROTEIN FIBRIL / Amyloid / neurodegeneration / filament / TMEM106B

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