FIGURE

Fig. 6.

ID

ZDB-FIG-220717-9

Publication

Dayal et al., 2022 - The distal C terminus of the dihydropyridine receptor β_1a subunit is essential for tetrad formation in skeletal muscle

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Fig. 6.

Hydrophobic residues (L₄₉₆L₅₀₀W₅₀₃) in the β_1a distal C terminus are not important for skeletal muscle EC coupling. (A) Amino acid sequence of rabbit β_1a C terminus depicting the position of the three hydrophobic residues LLW (red box with yellow filling), which were exchanged with alanines (AAA). (B) Relaxed myotubes expressing triple mutant β_1a(LLW-AAA) (n = 16) displayed Q_max values similar (P > 0.05) to β_1a (n = 16). (Right) Exemplar charge movement recording from relaxed myotubes expressing β_1a(LLW-AAA). (Scale bars, 5 ms [horizontal], 3 pA/pF [vertical].) (C) Plots of voltage dependence of maximal Ca²⁺ transients were indistinguishable (P > 0.05) between β_1a(LLW-AAA) (n = 13) and β_1a (n = 9)-expressing relaxed myotubes. (Right) Exemplar Ca²⁺ transient recordings from relaxed myotubes expressing mutant β_1a(LLW-AAA). (Scale bars, 50 ms [horizontal], ΔF/F₀ = 1 [vertical].) Error bars indicate SEM. P determined by unpaired Student’s t test.

Expression Data

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Antibody Labeling

Phenotype Data

Phenotype Detail

Acknowledgments

This image is the copyrighted work of the attributed author or publisher, and ZFIN has permission only to display this image to its users. Additional permissions should be obtained from the applicable author or publisher of the image. Full text @ Proc. Natl. Acad. Sci. USA