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Protein phosphorylation during phagosome maturation
Author(s) -
Emans Neil,
Nzala Nsumu N,
Desjardins Michel
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01213-6
Subject(s) - phagolysosome , phagosome , endosome , endocytic cycle , microbiology and biotechnology , phosphorylation , biogenesis , dephosphorylation , biology , chemistry , endocytosis , biochemistry , phagocytosis , phosphatase , intracellular , receptor , gene
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.