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Moesin and Myosin interact with SHP-1 during phagolysosome biogenesis in macrophages

Gomez, Carolina P; Descoteaux, Albert . Moesin and Myosin interact with SHP-1 during phagolysosome biogenesis in macrophages In: 16e symposium annuel de parasitologie moléculaire du Québec, 6-7 juin 2016, Université McGill, Montréal, QC.

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Résumé

Phagolysosome biogenesis requires the recruitment of effector proteins which regulate formation, acidification, or fusion of the phagosome with endocytic organelles. Amongst these proteins, phosphatases are known for their role during the maturation process. We previously showed that the Src homology 2 domain-containing phosphatase 1 (SHP-1) is recruited to the phagosome and regulates phagolysosome biogenesis in murine macrophages. However, the protein interactions that allowed for this effect are yet unknown. Through mass spectrometry, we identified two proteins interacting with SHP-1 during phagocytosis: Moesin (Moe) and Myosin (Myo). Our data show that in bone marrow-derived macrophages (BMMs) and in immortalized BMMs both Moe and Myo are recruited to the phagosome and that they co-localize with SHP-1 (confocal microscopy and immuno-precipitation). Furthermore, siRNA-mediated knockdown of either Moe or Myo provided us with the ability to assess the phagosomal recruitment of SHP-1, and phagolysosome biogenesis, including acidification of the vacuole, generation of reactive oxygen species, and microbicidal activity. Our results show that Moe and Myo affect the phagosomal recruitment of SHP-1 and, consequently, the maturation of the phagolysosomes. Since pathogens such as Leishmania activate SHP-1 and alter phagolysosomal biogenesis, our findings may be useful to understand the pathogenesis of intracellular infections.

Type de document: Document issu d'une conférence ou d'un atelier
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Centre: Centre INRS-Institut Armand Frappier
Date de dépôt: 01 mai 2018 20:17
Dernière modification: 01 mai 2018 20:17
URI: http://espace.inrs.ca/id/eprint/7070

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