Dépôt numérique

The Protein Tyrosine Phosphatase SHP-1 Regulates Phagolysosome Biogenesis

Gomez, Carolina P.; Tiemi, Shio Marina; Duplay, Pascale; Olivier, Martin et Descoteaux, Albert ORCID logoORCID: https://orcid.org/0000-0002-0633-5309 (2012). The Protein Tyrosine Phosphatase SHP-1 Regulates Phagolysosome Biogenesis Journal of Immunology , vol. 189 , nº 5. pp. 2203-2210. DOI: 10.4049/jimmunol.1103021.

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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 homol. region 2 domain-contg. 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 exts., we obsd. an impaired recruitment of lysosomal-assocd. 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.

Type de document: Article
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Centre: Centre INRS-Institut Armand Frappier
Date de dépôt: 07 mars 2024 20:19
Dernière modification: 07 mars 2024 20:19
URI: https://espace.inrs.ca/id/eprint/14031

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