Extended Data Fig. 7: HSP110 role beyond HSP70 recycling.
From: Molecular dissection of amyloid disaggregation by human HSP70
a, Disaggregation of α-syn fibrils monitored by ThT fluorescence. Preformed fibrils of α-syn were incubated with DNAJB1, 1× HSP70 or 5× HSP70 and in the absence or presence of HSP110 as indicated. b, Fold change in FRET efficiencies (A/D) between equimolar HSP70AF488 and HSP70AF594 in presence of 20× α-syn fibrils, 0.5× DNAJB1 and ATP after titration of HSP110 (2.5, 5, 10, 20, 40, 80, 160, 320, 640 nM) relative to the absence of NEF. c, Steady-state HSP70AF488 polarization in the presence of 0.5× DNAJB1 and 20× α-syn fibrils as a function of HSP110 concentration. d, Fold change in FRET efficiencies (A/D) of indicated HSP70 donor (AF488) and acceptor (AF594) pairs (numbering indicates position of modified cysteine residue in HSP70) in presence of 20× α-syn fibrils, 0.5× DNAJB1 and ATP after titration of HSP110 (8, 25, 74, 222, 667 nM, 2, 6 μM) compared to the absence of NEF. e, Fold change in HSP70 FRET efficiencies (A/D in presence of 20× α-syn fibrils, 0.5× DNAJB1 and ATP after titration of HSP110 (2.5, 5, 10, 20, 40, 80, 160, 320, 640 nM) or BAG1 constructs (12.5, 25, 50, 100, 200, 400, 800 nM, 1.6, 3.2 μM) relative to the absence of NEF. Reaction conditions and number of independent replicates are specified in Extended Data Table 2. For all plots, data are mean ± s.e.m. Solid lines represent fits of the data to the one-site binding equation.
