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Direct recruitment of H+-ATPase from lysosomes for phagosomal acidification.
- Source :
-
Journal of cell science [J Cell Sci] 2009 Jul 15; Vol. 122 (Pt 14), pp. 2504-13. Date of Electronic Publication: 2009 Jun 23. - Publication Year :
- 2009
-
Abstract
- 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.
- Subjects :
- Animals
Cells, Cultured
Hydrogen-Ion Concentration
Lysosomes microbiology
Macrophages, Peritoneal microbiology
Mice
Mice, Inbred C57BL
Mice, Transgenic
Microscopy, Confocal
Phagosomes microbiology
Protein Transport
Recombinant Fusion Proteins metabolism
Time Factors
Vacuolar Proton-Translocating ATPases genetics
Lysosomes enzymology
Macrophages, Peritoneal enzymology
Phagocytosis
Phagosomes enzymology
Vacuolar Proton-Translocating ATPases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9533
- Volume :
- 122
- Issue :
- Pt 14
- Database :
- MEDLINE
- Journal :
- Journal of cell science
- Publication Type :
- Academic Journal
- Accession number :
- 19549681
- Full Text :
- https://doi.org/10.1242/jcs.050443