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Journal articles
The protein tyrosine phosphatase SHP-1 regulates phagolysosome biogenesis.
Abstract : The process of phagocytosis and phagosome maturation involves the recruitment of effector proteins that participate in phagosome formation and in the acidification and/or fusion with various endocytic vesicles. In the current study, we investigated the role of the Src homology region 2 domain-containing phosphatase 1 (SHP-1) in phagolysosome biogenesis. To this end, we used immortalized bone marrow macrophages derived from SHP-1-deficient motheaten mice and their wild-type littermates. We found that SHP-1 is recruited early and remains present on phagosomes for up to 4 h postphagocytosis. Using confocal immunofluorescence microscopy and Western blot analyses on purified phagosome extracts, we observed an impaired recruitment of lysosomal-associated membrane protein 1 in SHP-1-deficient macrophages. Moreover, Western blot analyses revealed that whereas the 51-kDa procathepsin D is recruited to phagosomes, it is not processed into the 46-kDa cathepsin D in the absence of SHP-1, suggesting a defect in acidification. Using the lysosomotropic agent LysoTracker as an indicator of phagosomal pH, we obtained evidence that in the absence of SHP-1, phagosome acidification was impaired. Taken together, these results are consistent with a role for SHP-1 in the regulation of signaling or membrane fusion events involved in phagolysosome biogenesis.
Cited literature [69 references]
https://hal-riip.archives-ouvertes.fr/pasteur-01001767
Contributor : Nancy Laflamme Connect in order to contact the contributor
Submitted on : Wednesday, June 4, 2014 - 7:35:52 PM
Last modification on : Thursday, June 18, 2020 - 12:32:05 PM
Long-term archiving on: : Tuesday, April 11, 2017 - 3:47:13 AM
Contributor : Nancy Laflamme Connect in order to contact the contributor
Submitted on : Wednesday, June 4, 2014 - 7:35:52 PM
Last modification on : Thursday, June 18, 2020 - 12:32:05 PM
Long-term archiving on: : Tuesday, April 11, 2017 - 3:47:13 AM