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M312446200v1
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Papers In Press, published online ahead of print November 24, 2003
J. Biol. Chem, 10.1074/jbc.M312446200
Submitted on November 13, 2003
Revised on November 24, 2003
Accepted on November 24, 2003

Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin

Jae Man Lee, Seong-Hwan Rho, Dong Wook Shin, Chunghee Cho, Woo Jin Park, Soo Hyun Eom, Jianjie Ma, and Do Han Kim

Life Science, Kwangju Institute of Science and Technology, Gwangju 500-712

Corresponding Author: dhkim{at}kjist.ac.kr

In mammalian striated muscles, ryanodine receptor (RyR), triadin, junctin, and calsequestrin (CSQ) form a quaternary complex in the lumen of sarcoplasmic reticulum (SR). Such intermolecular interactions contribute not only to the passive buffering of SR luminal Ca2+, but also to the active Ca2+ release process during excitation-contraction coupling. Here we tested the hypothesis that specific charged amino acids within the luminal portion of RyR mediate its direct interaction with triadin. Using in vitro binding assay and site-directed mutagenesis, we found that the second intraluminal loop of the skeletal muscle RyR1 (a.a. 4860-4917), but not the first intraluminal loop of RyR1 (a.a. 4581-4640) could bind triadin. Specifically, three negatively charged residues D4878, D4907, and E4908 appear to be critical for the association with triadin. Using deletional approaches, we showed that a KEKE motif of triadin (a.a. 200-232) is essential for the binding to RyR1. Since the second intraluminal loop of RyR has been previously shown to contain the ion-conducting pore as well as the selectivity filter of the Ca2+ release channel, and D4878, D4907, and E4908 residues are predicted to locate at the periphery of the pore assembly of the channel, our data suggest that a physical interaction between RyR1 and triadin could play an active role in the overall Ca2+ release process of excitation-contraction coupling in muscle cells.


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