TDP-43 shapeshifts to encipher FTD severity

TDP-43 forms cytoplasmic aggregates in degenerating neurons of frontotemporal dementia (FTD) patients. Laferrière et al. now establish that TDP-43 assemblies from distinct FTD subtypes have different structures, neurotoxicities, and seeding activities, which correlate with FTD severity. Thus, distin...

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Bibliographic Details
Published in:Nature neuroscience 2019-01, Vol.22 (1), p.3-5
Main Authors: Barbieri, Edward M., Shorter, James
Format: Article
Language:English
Subjects:
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Amyotrophic lateral sclerosis
Animal Genetics and Genomics
Assemblies
Behavioral Sciences
Biochemistry
Biological Techniques
Biomedical and Life Sciences
Biomedicine
Brain
Dementia disorders
Development and progression
Disease
Disease Progression
DNA binding proteins
Frontotemporal Dementia
Frontotemporal Lobar Degeneration
Health aspects
Humans
Hypotheses
Medical schools
Nervous system diseases
Neurobiology
Neurodegenerative diseases
Neurons
Neurosciences
Neurotoxicity
News & Views
news-and-views
Patients
Physiology
Prions (Proteins)
Protein binding
Proteins
RNA
Seeds
Universities and colleges
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Summary:TDP-43 forms cytoplasmic aggregates in degenerating neurons of frontotemporal dementia (FTD) patients. Laferrière et al. now establish that TDP-43 assemblies from distinct FTD subtypes have different structures, neurotoxicities, and seeding activities, which correlate with FTD severity. Thus, distinct pathological TDP-43 assemblies akin to prion strains might underpin distinct FTD subtypes.
ISSN:1097-6256
1546-1726
DOI:10.1038/s41593-018-0299-6