l(2)01810 causes glutamine-dependent megamitochondrial formation when it is overexpressed in Drosophila cells. In the present study, we elucidated the function of l(2)01810 during megamitochondrial formation. The overexpression of l(2)01810 and the inhibition of glutamine synthesis showed that l(2)01810 is involved in the accumulation of glutamate. l(2)01810 was predicted to contain transmembrane domains and was found to be localized to the plasma membrane. By using 14C-labelled glutamate, l(2)01810 was confirmed to uptake glutamate into Drosophila cells with high affinity (Km=69.4 μM). Also, l(2)01810 uptakes glutamate in a Na+-independent manner. Interestingly, however, this uptake was not inhibited by cystine, which is a competitive inhibitor of Na+-independent glutamate transporters, but by aspartate. A signal peptide consisting of 34 amino acid residues targeting to endoplasmic reticulum was predicted at the N-terminus of l(2)01810 and this signal peptide is essential for the protein's localization to the plasma membrane. In addition, l(2)01810 has a conserved functional domain of a vesicular-type glutamate transporter, and Arg146 in this domain was found to play a key role in glutamate transport and megamitochondrial formation. These results indicate that l(2)01810 is a novel type of glutamate transporter and that glutamate uptake is a rate-limiting step for megamitochondrial formation.
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Research Article|
September 28 2011
l(2)01810 is a novel type of glutamate transporter that is responsible for megamitochondrial formation
Myoung Sup Shim;
Myoung Sup Shim
*Laboratory of Molecular Genetics and Genomics, School of Biological Sciences, Institute of Molecular Biology and Genetics, Seoul National University, Seoul 151-742, Korea
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Jin Young Kim;
Jin Young Kim
*Laboratory of Molecular Genetics and Genomics, School of Biological Sciences, Institute of Molecular Biology and Genetics, Seoul National University, Seoul 151-742, Korea
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Kwang Hee Lee;
Kwang Hee Lee
*Laboratory of Molecular Genetics and Genomics, School of Biological Sciences, Institute of Molecular Biology and Genetics, Seoul National University, Seoul 151-742, Korea
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Hee Kyoung Jung;
Hee Kyoung Jung
*Laboratory of Molecular Genetics and Genomics, School of Biological Sciences, Institute of Molecular Biology and Genetics, Seoul National University, Seoul 151-742, Korea
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Bradley A. Carlson;
Bradley A. Carlson
†Laboratory of Cancer Prevention, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, U.S.A.
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Xue-Ming Xu;
Xue-Ming Xu
†Laboratory of Cancer Prevention, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, U.S.A.
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Dolph L. Hatfield;
Dolph L. Hatfield
†Laboratory of Cancer Prevention, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, U.S.A.
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Byeong Jae Lee
Byeong Jae Lee
1
*Laboratory of Molecular Genetics and Genomics, School of Biological Sciences, Institute of Molecular Biology and Genetics, Seoul National University, Seoul 151-742, Korea
1To whom correspondence should be addressed (email imbglmg@snu.ac.kr).
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Publisher: Portland Press Ltd
Received:
March 31 2011
Revision Received:
June 20 2011
Accepted:
July 05 2011
Accepted Manuscript online:
July 05 2011
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem J (2011) 439 (2): 277–286.
Article history
Received:
March 31 2011
Revision Received:
June 20 2011
Accepted:
July 05 2011
Accepted Manuscript online:
July 05 2011
Citation
Myoung Sup Shim, Jin Young Kim, Kwang Hee Lee, Hee Kyoung Jung, Bradley A. Carlson, Xue-Ming Xu, Dolph L. Hatfield, Byeong Jae Lee; l(2)01810 is a novel type of glutamate transporter that is responsible for megamitochondrial formation. Biochem J 15 October 2011; 439 (2): 277–286. doi: https://doi.org/10.1042/BJ20110582
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