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Cleaved TMEM106B forms amyloid aggregates in central and peripheral nervous systems

Acta Neuropathologica. 2024-06; 
Mehtap Bacioglu, Manuel Schweighauser, Derrick Gray, Sofia L?vestam, Taxiarchis Katsinelos, Annelies Quaegebeur, John van Swieten, Zane Jaunmuktane, Stephen W. Davies, Sjors H. W. Scheres, Michel Goedert, Bernardino Ghetti, and Maria Grazia Spillantini
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Proteins, Expression, Isolation and Analysis To characterise its epitope, the TMEM106B C-terminal fragment (120-274) incorporated into pET3A was purchased from Genscript. Get A Quote

摘要

Filaments made of residues 120-254 of transmembrane protein 106B (TMEM106B) form in an age-dependent manner and can be extracted from the brains of neurologically normal individuals and those of subjects with a variety of neurodegenerative diseases. TMEM106B filament formation requires cleavage at residue 120 of the 274 amino acid protein; at present, it is not known if residues 255-274 form the fuzzy coat of TMEM106B filaments. Here we show that a second cleavage appears likely, based on staining with an antibody raised against residues 263-274 of TMEM106B. We also show that besides the brain TMEM106B inclusions form in dorsal root ganglia and spinal cord, where they were mostly found in non-neuronal cells. We... More

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