Data from: Isoform-specific steric zippers drive aberrant assembly and mislocalization of shortened TDP-43

TDP-43 is an essential RNA-binding protein. Cytoplasmic aggregation of
TDP-43 is a hallmark of amyotrophic lateral sclerosis (ALS),
frontotemporal dementia (FTD), and related neurodegenerative disorders.
Shortened TDP-43 (sTDP-43) splice isoforms, which lack most of the
prion-like domain (PrLD) but are enriched in motor neurons, are highly
insoluble in cells and ALS patient tissue despite the near-complete
absence of the PrLD. This dataset provides the quantitative data
underlying experiments that define the sequence-encoded basis for aberrant
sTDP-43 assembly. Data include: thioflavin T (ThT) fluorescence and
turbidity kinetic measurements from in vitro aggregation and
fibrillization assays; fluorescence microscopy quantification of aggregate
area using CellProfiler; sedimentation (supernatant/pellet fractionation)
densitometry; aggregation prevention assays with RNA and IC50
determinations; electrophoretic mobility shift assay (EMSA) quantification
of RNA binding; ZipperDB fibrillization propensity scores; longitudinal
neuronal survival data from rodent primary cortical neurons; and
nuclear/cytoplasmic localization ratios from HEK293T cells. Proteins
examined include full-length TDP-43 (flTDP-43), sTDP-43, sTDP-43ΔC-tail,
steric zipper-disrupting variants (sTDP-435G, sTDP-43I281P, sTDP-43L291P,
sTDP-43I281PL291P), sTDP-43_18aa, and sTDP-432P_mut_18aa.