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. 2020 Nov 17;8:592159. doi: 10.3389/fcell.2020.592159

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Copyright © 2020 Randez-Gil, Bojunga, Estruch, Winderickx, Del Poeta and Prieto.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Pho85, Kcs1 and Vip1 contribute to tau phosphorylation by different kinases. Native wild-type tau (N) and the clinical R406W tau mutant (Vanhelmont et al., 2010) were expressed in wild-type (wt), pho85, kcs1, and vip1 strains, and the electrophoretic profile of the protein from logarithmic-SCD-Ura-grown (Abs₆₀₀ ∼0.3) cells was analyzed by Western blot using Tau5 and phospho-specific antibodies against S³⁹⁶/S⁴⁰⁴ (AD2) and S⁴⁰⁹ (PG5) epitopes. The graphs show the AD2 and PG5 band intensities (±SD) expressed as arbitrary units. Protein extraction, band intensity determination, and statistical analysis were as described in Figure 1C. Data are the mean (±SD) of three independent experiments. *p < 0.05 for AD2 or PG5 band intensity of the mutant strains compared with AD2 or PG5 band intensity of the wild-type control strain. Representative Western blots images are shown.