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Fig. 3.

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ZDB-FIG-220717-5

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. 3.

Length of the β₄ C terminus is not crucial for skeletal muscle DHPR–RyR1coupling. (A) Amino acid sequence alignment depicting variable lengths of the C termini of β_1a and β₄ subunits (GenBank accession nos.: rabbit β_1a, M25514; rat β₄, L02315). To determine whether the length of the C terminus was functionally critical, the last 51 amino acids from the β₄ C terminus were deleted, yielding mutant β₄(Δ51). (B) Q_max values were indistinguishable (P > 0.05) between relaxed myotubes expressing the deletion mutant β₄(Δ51) (n = 17), β_1a (n = 16), or β₄ (n = 12). (C) Maximal Ca²⁺ transients (ΔF/F₀)_max for β₄(Δ51) expressing relaxed myotubes (n = 10) was similar (P > 0.05) to that of β₄ (n = 13). (D) Similarly, total maximal Ca²⁺ transients (intg.(ΔF/F₀)_max) for β₄(Δ51) expressing relaxed myotubes was statistically indistinguishable (P > 0.05) from that of β₄. Error bars indicate SEM. P determined by unpaired Student’s t test.

Expression Data

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Antibody Labeling

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Acknowledgments

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