Figure 4.
Figure 4. Specific carboxyl-terminal cysteine residues form cross-links. (A) Representative blots from HEK293F cells transfected with hP2X1 C349A H355C, I356C, L357C, P358C, K359C, or R360C treated with 3.2 U/ml apyrase, then BMB or DMSO (apyrase only). Of the mutants tested, only P358C and R360C showed strong enhancement of the ∼110 kD band with BMB treatments. This suggests that only these residues can dimerize within 10.9 Å. Boxes show images were taken from the same blot while the the dotted line shows where lanes have been removed for clarity. (B) Histogram showing the average percentage dimer present for the above mutants tested with all three cross-linkers. This shows that only P358C and R360C show 40–60% dimerization. (*, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001; n = 3–5).

Specific carboxyl-terminal cysteine residues form cross-links. (A) Representative blots from HEK293F cells transfected with hP2X1 C349A H355C, I356C, L357C, P358C, K359C, or R360C treated with 3.2 U/ml apyrase, then BMB or DMSO (apyrase only). Of the mutants tested, only P358C and R360C showed strong enhancement of the ∼110 kD band with BMB treatments. This suggests that only these residues can dimerize within 10.9 Å. Boxes show images were taken from the same blot while the the dotted line shows where lanes have been removed for clarity. (B) Histogram showing the average percentage dimer present for the above mutants tested with all three cross-linkers. This shows that only P358C and R360C show 40–60% dimerization. (*, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001; n = 3–5).

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