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. 2011 Nov 9;1:146. doi: 10.1038/srep00146

Figure 4. PIP2 binding sites of TRPM6.

Figure 4

(A) Alignment of the TRP domain of TRPM6, TRPM7 and TRPM8. The highlighted residues in TRPM8 are the PIP2 binding sites. (B) Representative traces of WT-TRPM6 and mutants K1085Q, R1088Q, and K1098Q. (C–D) Effects of 2-APB on the mutants K1085Q and R1088Q. (E) Normalized mean current density of TRPM6 mutants in comparison with WT TRPM6 (n = 10 *p<0.05; ** P<0.01). Mutants K1098Q and the double mutants K1085Q/R1088Q did not produce any current. (F) Average changes of current amplitude by 2-APB (200 μM). 2-APB did not have any effect on the non-functional mutants K1098Q and K1085Q/R1088Q.