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Letters to Nature
Nature 360, 169 - 171 (12 November 1992); doi:10.1038/360169a0

Function of a truncated dihydropyridine receptor as both voltage sensor and calcium channel

Kurt G. Beam*, Brett A. Adams*, Tetsuhiro Niidome, Shosaku Numa & Tsutomu Tanabe§

* Department of Physiology, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, Colorado 80523, USA
Departments of Medical Chemistry and Molecular Genetics, Kyoto University Faculty of Medicine, Kyoto 606, Japan
Deceased.
§ Present address: Howard Hughes Medical Institute and Department of Cellular and Molecular Physiology, Boyer Center for Molecular Medicine, Yale University School of Medicine, PO Box 9812, New Haven, Connecticut 06536-0812, USA.

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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