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. 2021 Jan 27;41(4):797–810. doi: 10.1523/JNEUROSCI.1920-20.2020

Figure 5.

Figure 5.

Effect of individual cysteine mutations on Tau conformation and aggregation propensity. A, Representative Western blots of aqueous soluble and insoluble fractions generated from adult heads following pan-neuronal expression of the indicated transgenes. Syx was used as loading control. The Syx-normalized level of wt Tau in the soluble fraction over the insoluble fraction was fixed to 1. Error bars indicate mean ± SEM relative sol/ins ratios of the mutants, over that of the wt Tau. *p < 0.05, significantly low amount of the C322A mutant in the insoluble fraction (Dunnett's). Detailed statistics can be found in the text. B, Transgenic flies expressing wt Tau or the single cysteine mutants under the control of the Elav;Ras-Gal4 driver were aged for 10 d. Proteins from adult heads were sequentially extracted with RIPA buffer and 70% FA and probed for Tau (5A6). Soluble RIPA fraction has also been probed with the conformation-specific MC1 antibody, and all transgenes displayed positive immunoreactivity. Syx was used as loading control.