ArticleCell2022
Homotypic fibrillization of TMEM106B across diverse neurodegenerative diseases.
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Article in Cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.
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107citing papers in PubMed
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107 citing papers in PubMed, 154 citations in OpenAlex.
- Lysosomal dysfunction in neurodegenerative disease.Nature reviews. Neurology · 2026Review
- TMEM106B is a selective modulator of TDP-43 pathology in Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026Article
- Associations between TMEM106B C-terminal fragment aggregation, age, and TDP-43 or tau pathology.Brain pathology (Zurich, Switzerland) · 2026Article
- Clinical Associations of Cerebrospinal Fluid TMEM106B in Familial and Sporadic Frontotemporal Dementia.JAMA neurology · 2026Article
- CTE-type tau filaments in Alzheimer's disease with co-morbid LATE-NC.Acta neuropathologica · 2026Article
- Cryo-EM structures of ALECT2 filaments from human renal biopsies.Nature communications · 2026Article
- TMEM106B C-terminal fragments drive nucleocytoplasmic transport failure and TDP-43 mislocalization in the aging human brain.bioRxiv : the preprint server for biology · 2026Article
- Shifts in protein aggregate stability define proteostasis decline in the aging human brain.bioRxiv : the preprint server for biology · 2026Article
- Cracking the code of native amyloid fibrils: advances and next steps to enable pathology-informed therapeutic and diagnostic.Nature structural & molecular biology · 2026Review
- Neurodegeneration risk variants promote lysosomal TMEM106B fibril accumulation.bioRxiv : the preprint server for biology · 2026Article
- Granulin loss and TMEM106B risk converge on lysosomal C-terminal fragment pathology in frontotemporal dementia.bioRxiv : the preprint server for biology · 2026Article
- Genetic correlation analysis identifies TMEM106B, ACE, and ERC2 as genetic loci shared between Alzheimer's disease and primary psychiatric disorders.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026Article
- Unraveling Alzheimer's complexity with a distinct AβNature chemical biology · 2026Article
- The amyloidogenic C-terminal region of TMEM106B modulates lipid membrane biophysical properties: Functional and pathological insights.The Journal of biological chemistry · 2026Article
- Structure first - exploration and discovery with cryo-electron microscopy.Journal of cell science · 2026Review
- TRIM2 E3 ligase substrate discovery reveals zinc-mediated regulation of TMEM106B in the endolysosomal pathway.EMBO reports · 2026Article
- Effects of transmembrane protein 106B genetic variations on disease progression in Parkinson's disease.Frontiers in aging neuroscience · 2026Article
- Structural insights into human signal peptide peptidase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Lysosomal escape and TMEM106B fibrillar core determine TDP-43 seeding outcomes.bioRxiv : the preprint server for biology · 2025Article
- Research progress on TMEM proteins in cancer progression and chemoresistance (Review).International journal of molecular medicine · 2025Review
47 more citing papers are in PubMed but not listed here.
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Authors and funding
23 authors at 12 institutions in 3 countries.
Andrew ChangMortimer B. Zuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10027, USA; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Irving Medical Center, 630 West 168th Street, New York, NY 10032, USA.
Xinyu XiangMortimer B. Zuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10027, USA; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Irving Medical Center, 630 West 168th Street, New York, NY 10032, USA; Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Jing WangMortimer B. Zuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10027, USA; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Irving Medical Center, 630 West 168th Street, New York, NY 10032, USA.
Carolyn LeeMortimer B. Zuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10027, USA; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Irving Medical Center, 630 West 168th Street, New York, NY 10032, USA; Department of Microbiology & Immunology, Columbia University, New York, NY 10032, USA.
Tamta ArakhamiaMortimer B. Zuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10027, USA; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Irving Medical Center, 630 West 168th Street, New York, NY 10032, USA.
Marija SimjanoskaMortimer B. Zuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10027, USA; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Irving Medical Center, 630 West 168th Street, New York, NY 10032, USA.
Chi WangDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Yari CarlomagnoDepartment of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.
Guoan ZhangProteomics and Metabolomics Core Facility, Weill Cornell Medicine, New York, NY 10021, USA.
Shikhar DhingraMortimer B. Zuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10027, USA.
Manon ThierryCentre for Cognitive Neurology, Department of Neurology, New York University School of Medicine, New York, NY 10016, USA.
Jolien PerneelApplied and Translational Neurogenomics, VIB Center for Molecular Neurology, VIB, Antwerp, Belgium; Department of Biomedical Sciences, University of Antwerp, Antwerp, Belgium.
Bavo HeemanApplied and Translational Neurogenomics, VIB Center for Molecular Neurology, VIB, Antwerp, Belgium; Department of Biomedical Sciences, University of Antwerp, Antwerp, Belgium.
Lauren M ForgraveDepartment of Pathology and Laboratory Medicine, University of British Columbia, Vancouver, BC V6T 2B5, Canada; Department of Pathology and Laboratory Medicine, St. Paul's Hospital, Providence Health Care, Vancouver, Canada.
Michael DeTureDepartment of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.
Mari L DeMarcoDepartment of Pathology and Laboratory Medicine, University of British Columbia, Vancouver, BC V6T 2B5, Canada; Department of Pathology and Laboratory Medicine, St. Paul's Hospital, Providence Health Care, Vancouver, Canada.
Casey N CookDepartment of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.
Rosa RademakersApplied and Translational Neurogenomics, VIB Center for Molecular Neurology, VIB, Antwerp, Belgium; Department of Biomedical Sciences, University of Antwerp, Antwerp, Belgium.
Dennis W DicksonDepartment of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.
Leonard PetrucelliDepartment of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.
Michael H B StowellDepartment of Molecular, Cellular and Developmental Biology, University of Colorado Boulder, Boulder, CO 80309, USA. Electronic address: stowellm@colorado.edu.
Ian R A MackenzieDepartment of Pathology and Laboratory Medicine, University of British Columbia, Vancouver, BC V6T 2B5, Canada. Electronic address: ian.mackenzie@vch.ca.
Anthony W P FitzpatrickMortimer B. Zuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10027, USA; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Irving Medical Center, 630 West 168th Street, New York, NY 10032, USA. Electronic address: anthony.fitzpatrick@columbia.edu.
Columbia University · USMayo Clinic in Florida · USColumbia University Irving Medical Center · USVIB-UAntwerp Center for Molecular Neurology · BECornell University · USNew York University · USProvidence Health Care · CAStanford University · USSt. Paul's Hospital · CAUniversity of Antwerp · BEUniversity of British Columbia · CAUniversity of Colorado Boulder · US
Funding
Project 3: Neuropathology of the multi-proteinopathy of c9FTD/ALS.P01NS084974 · NINDS · MAYO CLINIC JACKSONVILLE · PI PETRUCELLI, LEONARD · 2014 to 2024
$17.6MUtilization of proteomics and lipidomics to identify modifiers of LBDU54NS110435 · NINDS · MAYO CLINIC JACKSONVILLE · PI FITZPATRICK, ANTHONY WILLIAM PAUL · 2019 to 2023
$14.5MPatient-Based Structural Biology of Tauopathies and TDP-43 Proteinopathies using Cryo-Electron Microscopy and Mass SpectrometryU01NS110438 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI FITZPATRICK, ANTHONY WILLIAM PAUL, PETRUCELLI, LEONARD · 2018 to 2022
$7.8MIdentifying exosome-mediated cargo transport machinery in Alzheimer's diseaseRF1AG061829 · NIA · UNIVERSITY OF COLORADO · PI SHEN, JINGSHI, STOWELL, MICHAEL H. B. · 2018 to 2018
$2.7MMechanistic insights into the link between the A152T risk variant and tauopathyR01AG063780 · NIA · MAYO CLINIC JACKSONVILLE · PI COOK, CASEY N · 2020 to 2024
$2.5MCIHR 74580NIA NIH HHS R01 AG063780NIA NIH HHS RF1 AG061829NINDS NIH HHS P01 NS084974NINDS NIH HHS U01 NS110438NINDS NIH HHS U54 NS110435
Abstract
Misfolding and aggregation of disease-specific proteins, resulting in the formation of filamentous cellular inclusions, is a hallmark of neurodegenerative disease with characteristic filament structures, or conformers, defining each proteinopathy. Here we show that a previously unsolved amyloid fibril composed of a 135 amino acid C-terminal fragment of TMEM106B is a common finding in distinct human neurodegenerative diseases, including cases characterized by abnormal aggregation of TDP-43, tau, or α-synuclein protein. A combination of cryoelectron microscopy and mass spectrometry was used to solve the structures of TMEM106B fibrils at a resolution of 2.7 Å from postmortem human brain tissue afflicted with frontotemporal lobar degeneration with TDP-43 pathology (FTLD-TDP, n = 8), progressive supranuclear palsy (PSP, n = 2), or dementia with Lewy bodies (DLB, n = 1). The commonality of abundant amyloid fibrils composed of TMEM106B, a lysosomal/endosomal protein, to a broad range of debilitating human disorders indicates a shared fibrillization pathway that may initiate or accelerate neurodegeneration.
Indexed as
Frontotemporal DementiaMembrane ProteinsNerve Tissue ProteinsNeurodegenerative DiseasesAmyloidCryoelectron MicroscopyDNA-Binding ProteinsHumansAmyloidDNA-Binding ProteinsMembrane ProteinsNerve Tissue ProteinsTMEM106B protein, humanamyloid fibrilscryo-EMDLBendosomeFTLD-TDPlysosomeneurodegenerationproteolysisPSPTMEM106B
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