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J Biol Chem, Vol. 274, Issue 31, 21913-21919, July 30, 1999
From the Department of Anatomy and Neurobiology College of
Veterinary Medicine and Biomedical Sciences, Colorado State University,
Fort Collins, Colorado 80523
The dihydropyridine receptor (DHPR) in the
skeletal muscle plasmalemma functions as both voltage-gated
Ca2+ channel and voltage sensor for
excitation-contraction (EC) coupling. As voltage sensor, the DHPR
regulates intracellular Ca2+ release via the skeletal
isoform of the ryanodine receptor (RyR-1). Interaction with RyR-1 also
feeds back to increase the Ca2+ current mediated by the
DHPR. To identify regions of the DHPR important for receiving this
signal from RyR-1, we expressed in dysgenic myotubes a chimera (SkLC)
having skeletal (Sk) DHPR sequence except for a cardiac (C) II-III loop
(L). Tagging with green fluorescent protein (GFP) enabled
identification of expressing myotubes. Dysgenic myotubes expressing
GFP-SkLC or SkLC lacked EC coupling and had very small Ca2+
currents. Introducing a short skeletal segment (
The II-III Loop of the Skeletal Muscle Dihydropyridine Receptor
Is Responsible for the Bi-directional Coupling with the Ryanodine
Receptor
1S
residues 720-765) into the cardiac II-III loop (replacing
1C residues 851-896) of GFP-SkLC restored both EC
coupling and Ca2+ current densities like those of the wild
type skeletal DHPR. This 46-amino acid stretch of skeletal sequence was
recently shown to be capable of transferring strong, skeletal-type EC
coupling to an otherwise cardiac DHPR (Nakai, J., Tanabe, T., Konno,
T., Adams, B., and Beam, K.G. (1998) J. Biol. Chem.
273, 24983-24986). Thus, this segment of the skeletal II-III loop
contains a motif required for both skeletal-type EC coupling and
RyR-1-mediated enhancement of Ca2+ current.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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