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. Author manuscript; available in PMC: 2020 Jul 6.
Published in final edited form as: Cell Rep. 2020 Jun 2;31(9):107704. doi: 10.1016/j.celrep.2020.107704

Figure 2. TMEM163 Specifically Enhances P2XR Activity.

Figure 2.

(A) Domain architecture of TMEM163 with its structural homolog, ZnT3, with FLAG epitope tag at the C terminus of ZnT3 (ZnT3-FLAG).

(B) 300 nM ATP-evoked currents were measured from oocytes injected with combinations of cRNAs as indicated (P2X3R 25 pg; all others 2 ng) using TEVC recording (Vh = −30 mV, n = 7–9).

(C) Expression of ZnT3-FLAG was confirmed at the expected molecular weight by western blotting (WB) of cRNA-injected oocyte lysate with anti-FLAG antibody.

(D–F) Representative traces and quantification of agonist-evoked currents in cRNA-injected oocytes. cRNAs of 100 pg of P2X3R, 500 pg of GluK2 and 2 ng of Neto2, 1 ng of GluA1, 2 ng of TMEM163, and 2 ng of control (Neto2 for P2XR and GluA1 and ZnT3 for GluK2) were injected individually. TMEM163 co-expression enhanced 300 nM ATP-evoked currents of P2X3R (D), but not 500 μM glutamate-evoked currents of the kainate receptor, GluK2/Neto2 (E), or 10 μM glutamate with 50 μM cyclothiazide-evoked currents of the AMPA receptor, GluA1 (F) (n = 6–7).

Data are mean ± SEM. Mann-Whitney U-test (D). **p < 0.01.