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First published online 23 June 2009
doi: 10.1242/jcs.050443

Journal of Cell Science 122, 2504-2513 (2009)
Published by The Company of Biologists 2009
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Research Article

Direct recruitment of H+-ATPase from lysosomes for phagosomal acidification

Ge-Hong Sun-Wada1, Hiroyuki Tabata1, Nobuyuki Kawamura1, Minako Aoyama2 and Yoh Wada2,*

1 Department of Biochemistry, Faculty of Pharmaceutical Sciences, Doshisha Women's College, Kohdo, Kyotanabe, Kyoto 610-0395, Japan
2 Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, Mihogaoka 8-1, Ibaraki, Osaka 567-0047, Japan

* Author for correspondence (e-mail: yohwada{at}sanken.osaka-u.ac.jp)

Accepted 17 April 2009

The nascent phagosome progressively establishes an acidic milieu by acquiring a proton pump, the vacuolar-type ATPase (V-ATPase). However, the origin of phagosomal V-ATPase remains poorly understood. We found that phagosomes were enriched with the V-ATPase a3 subunit, which also accumulated in late endosomes and lysosomes. We modified the mouse Tcirg1 locus encoding subunit a3, to express an a3-GFP fusion protein. Live-cell imaging and immunofluorescence microscopy revealed that nascent phagosomes received the a3-GFP from tubular structures extending from lysosomes located in the perinuclear region. Macrophages from a3-deficient mice exhibited impaired acidification of phagosomes and delayed digestion of bacteria. These results show that lysosomal V-ATPase is recruited directly to the phagosomes via tubular lysosomes to establish the acidic environment hostile to pathogens.

Key words: Acidification, Macrophage, Microtubules, Tubular lysosome, V-ATPase


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JCS 2009 122: 1404. [Full Text]  





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