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Fig. 5 | BMC Biology

Fig. 5

From: Ion- and water-binding sites inside an occluded hourglass pore of a trimeric intracellular cation (TRIC) channel

Fig. 5

Effects of Y153A mutation on the electrophysiological behaviors of SsTRIC channel. a Tyr153 and the surrounding residues in SsTRIC. The plug motif is highlighted in yellow. Tyr153 is highlighted as a van der Waals (VDW) model, and the residues surrounding Tyr153 are shown as cyan stick models. The red dashed lines with distances (Å) labeled nearby indicate hydrogen bond or ionic interactions between two adjacent residues. The view is from the cytoplasmic side. b Superposition of a SsTRIC monomer with a CeTRIC-B2 monomer. The protein backbones are shown as cartoon models in yellow (SsTRIC) or blue (CeTRIC-B2). The PIP2 molecule in CeTRIC-B2 is presented as a stick model in blue and red. PDB code: 5EIK for CeTRIC-B2. c Representative electrophysiological recordings of the wild-type SsTRIC (red) and Y153A mutant (blue) measured at +60 mV. d The all-points amplitude histogram of the Y153A (blue) and wild-type (red) data. The presence of six open-state peaks indicates these patches likely contain two trimers of Y153A/wild-type SsTRIC channels. The bin width is set at 0.03 pA/bin. The histograms were both fitted with seven Gaussian functions. C, O1–O6 represent the closed state and opening of one to six monomers. e Open probability (NP o) analysis on the Y153A mutant (blue) and wild-type channel (red). NP o = t o/T, where t o is the total time that the channel is observed in the six open states and T is the total recording time. For the wild type, n = 5; for the mutant, n = 3. See Additional file 11 for the supporting data values. f and g Dwell time analyses on the open state (O1) (f) and closed state (g) of the Y153A mutant (blue) and wild-type channel (red). The * and ** symbols indicate ae P value <0.05 and 0.01 by t test, respectively. The standard errors of the mean values (SEMs) are indicated by the error bars

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