Abstract
THE skeletal muscle dihydropyridine (DHP) receptor serves dual functions, as a voltage sensor for excitation–contraction coupling and as an L-type calcium channel1–3. Biochemical analysis indicates the presence of two forms of the DHP receptor polypeptide in skeletal muscle, a full-length translation product present as a minor species and a much more abundant form that has a truncated carboxy-terminus4–6. On the basis of these and other observations7, it has been proposed8 that, in skeletal muscle, only the full-length DHP receptor can function as a calcium channel and that the truncated form can only function as a voltage sensor for excitation–contraction coupling. To resolve this issue, we have now constructed a complementary DNA (pC6Δl) encoding a protein corresponding to the truncated DHP receptor in skeletal muscle. Expression of pC6Δl in dysgenic myotubes fully restores both excitation–contraction coupling and calcium current, consistent with the idea that a single class of DHP receptors performs both functions.
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Beam, K., Adams, B., Niidome, T. et al. Function of a truncated dihydropyridine receptor as both voltage sensor and calcium channel. Nature 360, 169–171 (1992). https://doi.org/10.1038/360169a0
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DOI: https://doi.org/10.1038/360169a0
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