Cardiac L-type calcium channel regulation by Leucine-Rich Repeat-Containing Protein 10

Figures

• 

  Figure 1.. LRRC10. (a) Tertiary structure of human LRRC10 as predicted by AlphaFold [26]. (b) Alignment of amino acid sequences of LRRC10 in humans, mice, and zebrafish. Blue and light blue highlights denote amino acid residues that are conserved between three and two species, respectively. Black lines indicate the seven leucine-rich repeats (LRR) containing the highly conserved segments (HCS) “LxxLxLxxNxL” in gray boxes. Colored dots in both panels indicate the positions of variant amino acid residues discussed in this review.

• 

  Figure 2.. Modulation of ICa,L by LRRC10. (a) Representative ICa,L traces (at − 60, −30, 0, and +30 mV) recorded from HEK-293 cells expressing the LTCC complex (CaV1.2, β2, and α2δ) without LRRC10 (black), with wild-type (WT) LRRC10 (blue), or with I195T LRRC10 (red). (b) Current-voltage relationship of ICa,L in HEK-293 cells under the three different conditions, plotted in colors corresponding to (a). Asterisks (*) denote statistically significant differences (p < 0.05) compared to ICa,L in HEK-293 cells expressing LTCC without LRRC10. The voltage clamp protocol used to elicit ICa,L is shown in the inset. (c) Voltage-dependent activation curves of ICa,L under the three different conditions, plotted in colors corresponding to (a). Note that the activation curve is shifted to the left with co-expression of WT LRRC10, whereas I195T LRRC10 shifts the activation curve to the right. Reproduced with modification from [18].