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National Institute of Environmental Health Sciences

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Publication Detail

Title: RyR1/RyR3 chimeras reveal that multiple domains of RyR1 are involved in skeletal-type E-C coupling.

Authors: Perez, Claudio F; Voss, Andrew; Pessah, Isaac N; Allen, Paul D

Published In Biophys J, (2003 Apr)

Abstract: Skeletal-type E-C coupling is thought to require a direct interaction between RyR1 and the alpha(1S)-DHPR. Most available evidence suggests that the cytoplasmic II-III loop of the dihydropyridine receptor (DHPR) is the primary source of the orthograde signal. However, identification of the region(s) of RyR1 involved in bidirectional signaling with the alpha(1S)-DHPR remains elusive. To identify these regions we have designed a series of chimeric RyR cDNAs in which different segments of RyR1 were inserted into the corresponding region of RyR3 and expressed in dyspedic 1B5 myotubes. RyR3 provides a preferable background than RyR2 for defining domains essential for E-C coupling because it possesses less sequence homology to RyR1 than the RyR2 backbone used in previous studies. Our data show that two regions of RyR1 (chimera Ch-10 aa 1681-2641 and Ch-9 aa 2642-3770), were independently able to restore skeletal-type E-C coupling to RyR3. These two regions were further mapped and the critical RyR1 residues were 1924-2446 (Ch-21) and 2644-3223 (Ch-19). These results both support and refine the previous hypothesis that multiple domains of RyR1 combine to functionally interact with the DHPR during E-C coupling.

PubMed ID: 12668474 Exiting the NIEHS site

MeSH Terms: Action Potentials/physiology; Animals; Caffeine/pharmacology; Calcium/metabolism*; Humans; Muscle Contraction/drug effects; Muscle Contraction/physiology*; Muscle Fibers, Skeletal/chemistry*; Muscle Fibers, Skeletal/drug effects; Muscle Fibers, Skeletal/physiology*; Muscle, Skeletal/chemistry; Muscle, Skeletal/drug effects; Muscle, Skeletal/physiology; Protein Isoforms; Protein Structure, Tertiary; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/classification; Recombinant Fusion Proteins/deficiency; Recombinant Fusion Proteins/physiology; Ryanodine Receptor Calcium Release Channel/chemistry*; Ryanodine Receptor Calcium Release Channel/classification; Ryanodine Receptor Calcium Release Channel/deficiency; Ryanodine Receptor Calcium Release Channel/physiology*

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