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. 2021 Jun 17;14:661368. doi: 10.3389/fnmol.2021.661368

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Copyright © 2021 Cantrelle, Loyens, Trivelli, Reimann, Despres, Gandhi, Hackenberger, Landrieu and Smet-Nocca.

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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Phosphorylation patterns of ¹⁵N-TauPHF1-G (A,C,D,E) by GSK3β without priming by CDK2 and ¹⁵N-TauS262A-G (B,F) by GSK3β with CDK2 priming. (A,B) Phosphorylation levels of the PHF-1 epitope. (A) TauPHF1 (blue bars) and TauPHF1-G (orange bars) phosphorylated by GSK3β. (B) TauS262A-G phosphorylated by CDK2 (pink bars) and GSK3β after CDK2 priming (purple bars). (C,D) ¹H-¹⁵N HSQC spectra of TauPHF1 (blue) and TauPHF1-G (orange) phosphorylated by GSK3β without priming by CDK2 showing the resonances of PHF-1 residues corresponding to the phosphorylated state (C) and the non-phosphorylated state (D). Resonances related to the O-GlcNAcylated forms of S400 is indicated by “gS400”. (E,F) Mass spectrometry analyses of ¹⁵N-TauPHF1-G (E) before (green) and after GSK3β phosphorylation (orange) and ¹⁵N-TauS262A-G (F) before (green) and after CDK2 (pink) or CDK2/GSK3β (purple) phosphorylation.