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Originally published In Press as doi:10.1074/jbc.M006189200 on November 28, 2000

J. Biol. Chem., Vol. 276, Issue 8, 6030-6036, February 23, 2001
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Glutamine-dependent Antiapoptotic Interaction of Human Glutaminyl-tRNA Synthetase with Apoptosis Signal-regulating Kinase 1*

Young-Gyu KoDagger , Eun-Kyoung KimDagger , Taeho KimDagger , Heonyong ParkDagger , Hee-Sae Park§, Eui-Ju Choi§, and Sunghoon KimDagger

From the Dagger  National Creative Research Initiatives Center for ARS Network, Sung Kyun Kwan University, Suwon, Kyunggido 440-746, Korea and the § National Creative Research Initiatives, Center for Cell Death, Graduate School of Biotechnology, Korea University, Seoul 136-701, Korea

Glutamine has been known to be an apoptosis suppressor, since it blocks apoptosis induced by heat shock, irradiation, and c-Myc overexpression. Here, we demonstrated that HeLa cells were susceptible to Fas-mediated apoptosis under the condition of glutamine deprivation. Fas ligation activated apoptosis signal-regulating kinase 1 (ASK1) and c-Jun N-terminal kinase (JNK; also known as stress-activated protein kinase (SAPK)) in Gln-deprived cells but not in normal cells, suggesting that Gln might be involved in the activity control of ASK1 and JNK/SAPK. As one of the possible mechanisms for the suppressive effect of Gln on ASK1, we investigated the molecular interaction between human glutaminyl-tRNA synthetase (QRS) and ASK1 and found the Gln-dependent association of the two molecules. While their association was enhanced by the elevation of Gln concentration, they were dissociated by Fas ligation within 5 min. The association involved the catalytic domains of the two enzymes. The ASK1 activity was inhibited by the interaction with QRS as determined by in vitro kinase and transcription assays. Finally, we have shown that QRS inhibited the cell death induced by ASK1, and this antiapoptotic function of QRS was weakened by the deprivation of Gln. Thus, the antiapoptotic interaction of QRS with ASK1 is controlled positively by the cellular concentration of Gln and negatively by Fas ligation. The results of this work provide one possible explanation for the working mechanism of the antiapoptotic activity of Gln and suggest a novel function of mammalian ARSs.

* This work was supported by a grant from the National Creative Research Initiatives of the Ministry of Science and Technology of Korea.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence may be addressed: National Creative Research Initiatives Center for ARS Network, Sung Kyun Kwan University, 300 Chunchundong, Jangangu Suwon, Kyunggido 440-746, Korea. Tel.: 82-31-290-5680; Fax: 82-31-290-5682; E-mail: shkim@yurim.skku.ac.kr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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