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J. Biol. Chem., Vol. 279, Issue 8, 6994-7000, February 20, 2004

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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||

From the Department of Life Science, Kwangju Institute of Science & Technology, Gwangju, 500-712, Korea, the Department of Genetics, Hanwha Chemical Co. R&D Center, Daejeon, 305-345, Korea, and the ^¶Department of Physiology and Biophysics, University of Medicine & Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854

In mammalian striated muscles, ryanodine receptor (RyR), triadin, junctin, and calsequestrin form a quaternary complex in the lumen of sarcoplasmic reticulum. Such intermolecular interactions contribute not only to the passive buffering of sarcoplasmic reticulum 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 (amino acids 4860-4917), but not the first intraluminal loop of RyR1 (amino acids 4581-4640) could bind triadin. Specifically, three negatively charged residues Asp⁴⁸⁷⁸, Asp⁴⁹⁰⁷, and Glu⁴⁹⁰⁸ appear to be critical for the association with triadin. Using deletional approaches, we showed that a KEKE motif of triadin (amino acids 200-232) is essential for the binding to RyR1. Because 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 Asp⁴⁸⁷⁸, Asp⁴⁹⁰⁷, and Glu⁴⁹⁰⁸ 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.

Received for publication, November 13, 2003

^* This work was supported by Korea Ministry of Science and Technology Systems Biology Research Grant M1-0309-00-0006, Korea Science and Engineering Foundation Basic Research Program 1999-1-20700-002-5, and Ministry of Education Brain Korea 21 Project, and National Institutes of Health Grants RO1-AG15556 and RO1-HL69000. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| To whom correspondence should be addressed. Tel.: 82-62-970-2485; Fax: 82-62-970-3411; E-mail: dhkim{at}kjist.ac.kr.

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