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. 2013 Jan;83(1):106–121. doi: 10.1124/mol.112.081802

Fig. 10.

Fig. 10.

PKC phosphorylation sites. (A) mutation of three serines (Ser833, Ser836, and Ser840) in GluK5 to aspartate nearly eliminated potentiation by PMA, compared with wild-type. (B) this pseudo-phosphorylated mutant GluK2/GluK5-S833D/S836D/S840D (GluK2/GluK5-TD) but not the triple glutamate (TE) mutant showed reduced potentiation by PMA (n ≥ 4, **P < 0.01; one-way ANOVA with Bonferroni’s post-test). The triple-D mutant also demonstrated larger whole-cell currents (C), compared with GluK2/GluK5-S833E/S836E/S840E (GluK2/GluK5-TE) or the wild-type (n ≥ 4, **P < 0.01; one-way ANOVA with Bonferroni’s post-test). (D) the GluK5-S833E-S836E-S840E-Δ884 mutant coexpressed with GluK2 and mGlu1 displayed normal currents, no potentiation by ACPD or PMA. (E) bar graph showing quantification of the data in D from multiple oocytes.