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. 2022 Oct 31;14:921772. doi: 10.3389/fnsyn.2022.921772

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Copyright © 2022 Hayashi.

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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Characterization of tyrosine phosphorylated GluA2 in lipid rafts fraction. (A) Proteins expressed in cultured cortical neurons were separated by Optiprep-density gradients from the least dense fraction 1 (Fr. 1) to the densest Fr. 6. Representative immunoblots of tyrosine phosphorylated GluA2 (anti-GluA2pY) and GluA2, Fyn, or Caveolin-1 (Cav1) proteins expression are shown. (B) Comparison of tyrosine phosphorylated GluA2 in Fr. 1 (white bar) and Fr. 6 (dotted bar). Band intensities are normalized to Fr. 1 (n = 3). (C) Comparison of GluA2 protein amount in Fr. 1 (white bar) and Fr. 6 (dotted bar). Band intensities are normalized to Fr. 6 (n = 3). (D) Ratio of tyrosine phosphorylated GluA2 to GluA2 protein amount in Fr. 1 (white bar) and Fr. 6 (dotted bar). Values are normalized to Fr. 6 (n = 3). Error bars represent SEM. *p < 0.05, ^**p < 0.01, ^***p < 0.001, t-test.