Protein phosphorylation during phagosome maturation

FEBS Letters

Desjardins, Michel¹  Nzala, Nsumu N¹  Emans, Neil¹ 

[1] Départment d'anatomie, Faculté de médecine, Université de Montréal, C.P. 6128, Succ. Centre ville, Montréal, Québec H3C 3J7, Canada

关键词: Phagocytosis;    Lysosome;    Phosphorylation;    Macrophage;   

DOI  :  10.1016/S0014-5793(96)01213-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phagolysosome biogenesis is driven by a series of interactions between phagosomes and organelles of the biosynthetic and endocytic pathways. The presence of endocytic markers on phagosomes suggests that phagosomes and endosomes share common structural and functional characteristics. In that line of thought, protein phosphorylation has been shown to be involved in regulatory aspects of the fusion properties of endosomes and other vacuolar organelles. To study further the mechanisms involved in phagolysosome biogenesis, we have investigated the presence of phagosome proteins that can be phosphorylated in vitro by endogenous phagosome-associated kinases. The results obtained show that proteins phosphorylated on tyrosine residues are present on phagosomes. Moreover, complex phosphorylation/dephosphorylation cycles appear to occur during phagolysosome biogenesis. The addition of endosome fractions to phagosomes inhibit the phosphorylation of phagosome proteins. These results suggest that phosphorylation and dephosphorylation events could play roles in the biogenesis of phagolysosomes and regulate, in part, the complex in vivo interactions between phagosomes and endosomes.

【 授权许可】

Unknown