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TitleNeurodegeneration risk variants promote lysosomal TMEM106B fibril accumulation.
Journal, issue, pagesbioRxiv, Year 2026
Publish dateMar 28, 2026
AuthorsJohn Michael Replogle / Jordan D Marks / Martin G Fernandez / Hebao Yuan / Dahyun Yu / Elizabeth Winters / Vidhya Maheswari Jawahar / Rishi Deshmukh / Renaldo Sutanto / Isabelle Kowal / Ashley Frankenfield / Rachel Shi / Yari Carlomagno / Karen Jansen-West / Tiffany W Todd / Andrii Kopach / Iradukunda Sandra Ndayambaje / Yue A Qi / Ananth Shantaraman / Ignacio Pozo-Cabanell / Udit Sheth / Mei Yue / Duc Duong / Shawn M Ferguson / David A Bennett / Markus Damme / Brad F Boeve / Gregory S Day / Benjamin Kellman / William C Skarnes / Ronald C Petersen / Keith A Josephs / Neill R Graff-Radford / Justin A McDonough / Mercedes Prudencio / Sami J Barmada / Yongjie Zhang / Ling Hao / Michael DeTure / Bailey Rawlinson / Erica Engelberg-Cook / Monica Castanedes Casey / Nathan Perez / Dennis W Dickson / Aliza Wingo / Yue Liu / Nicholas T Seyfried / Thomas S Wingo / Shyamal Mosalaganti / Leonard Petrucelli / Michael E Ward /
PubMed AbstractVariants in and , which encode lysosomal proteins, interact through unknown mechanisms to increase the risk of age-related cognitive decline and neurodegeneration. Here, we show that these variants ...Variants in and , which encode lysosomal proteins, interact through unknown mechanisms to increase the risk of age-related cognitive decline and neurodegeneration. Here, we show that these variants converge on a single molecular intermediate: the cleaved intra-lysosomal fibril core of TMEM106B, a precursor to amyloid fibrils that accumulate in the aging brain. A protein-coding risk variant (p.T185) drives fibril core accumulation by impairing its degradation and risk variants amplify this effect. Mice over-expressing the fibril core develop hallmarks of neurodegeneration, and cryo-electron tomography reveals intra-lysosomal fibrils in cultured neurons, mice, and diseased human brain. In -mutation carriers, in whom fibril burden is greatest, fibrils extrude through ruptured lysosomal membranes. These findings identify intra-lysosomal TMEM106B fibrillization as a convergent neurodegeneration mechanism and potential therapeutic target.
External linksbioRxiv / PubMed:41929000 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution37.0 Å
Structure data

EMDB-76230: Structure of TMEM106B doublet from patient brain derived lysosomes
Method: EM (subtomogram averaging) / Resolution: 37.0 Å

EMDB-76248: Structure of TMEM106B singlet from patient brain derived lysosomes
Method: EM (subtomogram averaging) / Resolution: 37.0 Å

Source
  • Homo sapiens (human)

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