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J. Biol. Chem., Vol. 279, Issue 19, 19387-19390, May 7, 2004

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ACCELERATED PUBLICATION

Co-expression of MG29 and Ryanodine Receptor Leads to Apoptotic Cell Death

EFFECT MEDIATED BY INTRACELLULAR Ca²⁺ RELEASE^*

Zui Pan, Yutaka Hirata, Ramakrishnan Y. Nagaraj, Jiying Zhao, Miyuki Nishi, Salim M. Hayek¶, Manjunatha B. Bhat¶, Hiroshi Takeshima, and Jianjie Ma||

From the Department of Physiology and Biophysics, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, the Department of Biochemistry, Tohoku University, Sendai 980-8575, Japan, and the ^¶Center for Anesthesiology Research, Cleveland Clinic Foundation, Cleveland, Ohio 44106

Perturbation of intracellular Ca²⁺ homeostasis has been shown to regulate the process of cell proliferation and apoptosis. Our previous studies show that mitsugumin 29 (MG29), a synaptophysin-related protein localized in the triad junction of skeletal muscle, serves an essential role in muscle Ca²⁺ signaling by regulating the process of store-operated Ca²⁺ entry. Here we report a functional interaction between MG29 and the ryanodine receptor (RyR)/Ca²⁺ release channel. The purified MG29 protein enhances activity of the RyR/Ca²⁺ release channel incorporated into the lipid bilayer membrane. Co-expression of MG29 and RyR in Chinese hamster ovary cells leads to apoptotic cell death resulting from depletion of intracellular Ca²⁺ stores, despite neither protein expression alone exhibits any significant effect on cell viability. In transient expression studies, the presence of RyR in the endoplasmic reticulum leads to retention of MG29 from the plasma membrane into the intracellular organelles. This functional interaction between MG29 and RyR could have important implications in the Ca²⁺ signaling processes of muscle cells. Our data also show that perturbation of intracellular Ca²⁺ homeostasis can serve as a key signal in the initiation of apoptosis.

Received for publication, January 20, 2004 , and in revised form, March 22, 2004.

^* This work was supported by National Institutes of Health Grants RO1-CA95739, RO1-AG15556, and RO1-HL69000 (to J. M.). 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: Dept. of Physiology and Biophysics, UMDNJ-Robert Wood Johnson Medical School, Piscataway, NJ 08854. Tel.: 732-235-4494; Fax: 732-235-4483; E-mail: maj2{at}umdnj.edu.

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