98%
921
2 minutes
20
The amyotrophic lateral sclerosis/parkinsonism-dementia complex (ALS/PDC) of the island of Guam and the Kii peninsula of Japan is a fatal neurodegenerative disease of unknown cause that is characterized by the presence of abundant filamentous tau inclusions in brains and spinal cords. Here, we used electron cryo-microscopy to determine the structures of tau filaments from the cerebral cortex of three cases of ALS/PDC from Guam and eight cases from Kii, as well as from the spinal cord of two of the Guam cases. Tau filaments had the chronic traumatic encephalopathy (CTE) fold, with variable amounts of Type I and Type II filaments. Paired helical tau filaments were also found in three Kii cases and tau filaments with the corticobasal degeneration fold in one Kii case. We identified a new Type III CTE tau filament, where protofilaments pack against each other in an antiparallel fashion. ALS/PDC is the third known tauopathy with CTE-type filaments and abundant tau inclusions in cortical layers II/III, the others being CTE and subacute sclerosing panencephalitis. Because these tauopathies are believed to have environmental causes, our findings support the hypothesis that ALS/PDC is caused by exogenous factors.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10743375 | PMC |
http://dx.doi.org/10.1073/pnas.2306767120 | DOI Listing |
J Neurochem
September 2025
Center for Translational Research in Neurodegenerative Disease, University of Florida, Gainesville, Florida, USA.
The two most prominent post-translational modifications of pathologic tau are Ser/Thr/Tyr phosphorylation and Lys acetylation. Whether acetylation impacts the susceptibility of tau to templated seeding in diseases like Alzheimer's disease (AD) and Progressive Supranuclear Palsy (PSP) is largely uncharacterized. Towards this, we examined how acetylation mimicking or nullifying mutations on five sites of tau (K311, K353, K369, K370, K375), located within the tau filament core, influenced the susceptibility of P301L (PL) tau to seeds from AD (AD-tau) or PSP (PSP-tau) brain donors in HEK293T cells.
View Article and Find Full Text PDFAlzheimers Dement
September 2025
Talisman Therapeutics, Babraham Research Campus, Cambridge, UK.
Introduction: Mutations in the MAPT gene that are causal for frontotemporal dementia (FTD) lead to mislocalization of tau protein to the neuronal cell body, changing microtubule dynamics to disrupt the nuclear envelope and nucleocytoplasmic transport.
Methods: We report a high content imaging-based phenotypic screen to identify novel small molecules that correct nuclear envelope defects in human neurons expressing the MAPT IVS10+16 mutation causal for FTD.
Results: Screening a 19,786-compound chemical diversity library, we identified > 100 compounds that corrected nuclear membrane defects in MAPT IVS10+16 neurons, with 23 demonstrating robust dose-dependent rescue.
Cytoskeleton (Hoboken)
September 2025
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori, Japan.
The precise control of microtubule dynamics is essential for diverse cellular processes and is a promising target for optical regulation using photoresponsive molecules. In this study, we developed Tau-derived peptides bearing azobenzene moieties on their side chains that enabled reversible photocontrol of microtubule polymerization by binding to the inside of microtubules. Two peptide derivatives with azobenzene located at different positions were synthesized by simple on-resin Fmoc solid-phase chemistry.
View Article and Find Full Text PDFBiochemistry
August 2025
Department of Neuroscience, Developmental and Regenerative Biology, University of Texas atSan Antonio, 1 UTSA Circle, San Antonio, Texas 78249, United States.
Neurofibrillary tangles are intracellular aggregates composed of the microtubule-associated protein tau. These insoluble aggregates are found in the brain of those affected by Alzheimer's disease and other related tauopathies. Hyperphosphorylation of tau in disease has been hypothesized to cause tau to dissociate from microtubules and form amyloid-like oligomers and fibrils.
View Article and Find Full Text PDFAutophagy
September 2025
Center for Brain Research, Indian Institute of Science, Bangalore, India.
MAPT/tau proteins propagate between brain regions in a prion-like manner, driving the onset and progression of dementia in Alzheimer disease (AD). However, the basis for variability in dementia progression among AD patients remains poorly understood. Here, we demonstrate that cognitively resilient AD patients, characterized by reduced MAPT/tau pathology, maintain lysosomal integrity, whereas cognitively vulnerable patients, exhibiting greater MAPT/tau burden, display lysosomal dysfunction.
View Article and Find Full Text PDF