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Originally published In Press as doi:10.1074/jbc.M200586200 on July 19, 2002

J. Biol. Chem., Vol. 277, Issue 39, 36296-36303, September 27, 2002
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Differential Localization of the Vacuolar H+ Pump with G Subunit Isoforms (G1 and G2) in Mouse Neurons*

Yoshiko MurataDagger §, Ge-Hong Sun-WadaDagger §, Takao YoshimizuDagger §, Akitsugu Yamamoto§||, Yoh WadaDagger §, and Masamitsu FutaiDagger §**

From the Dagger  Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University and the § Core Research for Evolutional Science and Technology (CREST) of the Japan Science and Technology Corporation, Osaka 567-0047, Japan and the || Department of Physiology, Kansai Medical University, Moriguchi, Osaka 570-8506, Japan

Vacuolar H+-ATPases (V-ATPases), a family of multimeric proton pumps, are involved in a wide variety of physiological processes. We have identified two mouse genes, Atp6g1 and Atp6g2, encoding the G1 and G2 isoforms of the V-ATPase G subunit, respectively. G1 was distributed ubiquitously in the tissues examined, whereas G2 was specifically distributed in central nervous system neurons. G1 was expressed at an early embryonic stage, whereas G2 transcription was significantly induced at 10.5 days postcoitus (embryonic day 10.5, i.e. 2 days before axon outgrowth). Both G1 and G2 were strongly expressed in cortical and hippocampal neurons, cerebellar granule cells, and Purkinje cells. Immunohistochemistry with isoform-specific antibodies revealed that G2 was localized in cell bodies, dendrites, and axons. In addition, electron microscopy and subcellular fractionation indicated that G2 was localized in synaptic vesicles, whereas G1 was not detectable. G1 and G2 exhibit 62% identity, and both isoforms were immunoprecipitated with the c and A subunits of V-ATPase. G2 could complement the yeast deletion mutant Delta vma10, which lacks the G subunit. The V-ATPases containing the G1 and G2 isoforms, respectively, showed similar Km(ATP) values and maximal velocity. These results indicate that G1 and G2 are bona fide subunits of V-ATPases and that the enzyme with the G2 isoform is involved in synaptic vesicle acidification.

* This work was supported in part by grants-in-aid from the Ministry of Education, Science, and Culture of Japan and the Hayashi and Naito Foundations.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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AB076406 and AB076405.

Both authors contributed equally to this work.

** To whom correspondence should be addressed: Div. of Biological Sciences, Osaka University, Mihogaoka 8-1, Ibaraki, Osaka 567-0047, Japan. Tel.: 81-6-6879-8480; Fax: 81-6-6875-5724; E-mail: m-futai@sanken.osaka-u.ac.jp.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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