The RNA-mediated higher order assembly of TDP-43, a protein associated with neurodegenerative diseases, preserves its solubility by reducing the risk of multivalent interactions between low complexity domains.
Exploring natural Hsp104 variation reveals unexpected tuning of a passive activity that inhibits aggregation of specific substrates to selectively counter TDP-43 or alpha-synuclein proteotoxicity connected to neurodegenerative disease.
OptoGranules reveal the function of G3BP1 as a stress granule scaffold and demonstrate that protracted stress granule assembly is sufficient to drive neurodegeneration and the evolution of ALS-FTD pathology.
Zfp106 functions as an RNA binding protein, binds directly to GGGGCC RNA repeats, is required in motor neurons to prevent ALS-like neurodegeneration in mice, and can suppress neurotoxicity in an established fly model of ALS.
Analysis of the Escherichia coli DnaB helicase•bacteriophage λ helicase loader (λP) complex provides insights into helicase opening, delivery to the origin and ssDNA entry, and closing in preparation for translocation.