Figure 5
Heat sensitivity of TRPV1 single-point mutants with mutations that neutralized amino acid hydrophobicity. (a) Structural location of all the residues mutated in the ankyrin repeats and the beginning of the S4-S5 linker. In cyan are residues that when mutated to Thr, lead to non-functional channels. In purple are residues that, when mutated to Thr, do not affect temperature activation. (b) Average conductance at +160 mV as a function of temperature for mutants. Data represent mean ± SEM. N on top of the bars represent number of individual patches. (c) Conductance-voltage (G-V) relationship of plateau current for wild-type TRPV1, V292T, L337T, I352T, and F559T at different temperatures. (d) Voltage of half maximal activation (Vhalf) for wild-type TRPV1, V292T, L337T, I352T, and F559T as a function of temperature. Vhalf was obtained from the fitting parameters of a Boltzmann distribution to the G-V. Data represent mean ± SEM. Lines are linear fits to the data. Wild-type TRPV1 n = 7, V292T n = 9, L337T n = 11, I352T n = 5, and F559T n = 7. Each Vhalf value was tested for statistical significance using an unpaired Student’s t-test. n.s. indicates not significant (p > 0.05).
