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• W2649090908 abstract "Abstract TDP-43 is a primarily nuclear RNA-binding protein, whose abnormal phosphorylation and cytoplasmic aggregation characterizes affected neurons in patients with amyotrophic lateral sclerosis and frontotemporal dementia. Here, we report that physiological nuclear TDP-43 in mouse and human brain forms homo-oligomers that are resistant to cellular stress. Physiological TDP-43 oligomerization is mediated by its N-terminal domain, which can adopt dynamic, solenoid-like structures, as revealed by a 2.1 Å crystal structure in combination with nuclear magnetic resonance spectroscopy and electron microscopy. These head-to-tail TDP-43 oligomers are unique among known RNA-binding proteins and represent the functional form of the protein in vivo, since their destabilization results in loss of alternative splicing regulation of known neuronal RNA targets. Our findings indicate that N-terminal domain-driven oligomerization spatially separates the adjoining highly aggregation-prone, C-terminal low-complexity domains of consecutive TDP-43 monomers, thereby preventing low-complexity domain inter-molecular interactions and antagonizing the formation of pathologic aggregates." @default.
• W2649090908 created "2017-06-30" @default.
• W2649090908 creator A5009946736 @default.
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• W2649090908 date "2017-06-29" @default.
• W2649090908 modified "2023-10-06" @default.
• W2649090908 title "Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation" @default.
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• W2649090908 doi "https://doi.org/10.1038/s41467-017-00062-0" @default.
• W2649090908 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5491494" @default.
• W2649090908 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28663553" @default.
• W2649090908 hasPublicationYear "2017" @default.
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