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Related Experiment Videos

Protein phosphorylation during phagosome maturation

N Emans1, N N Nzala, M Desjardins

  • 1Département d'anatomie, Faculté de médecine, Université de Montréal, Québec, Canada.

FEBS Letters
|November 25, 1996
PubMed
Summary

Protein phosphorylation regulates phagolysosome biogenesis. Tyrosine-phosphorylated proteins on phagosomes suggest phosphorylation/dephosphorylation cycles are key to phagosome-endosome interactions during biogenesis.

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Area of Science:

  • Cell Biology
  • Immunology

Background:

  • Phagolysosome biogenesis involves interactions between phagosomes and endocytic/biosynthetic pathways.
  • Phagosomes and endosomes share characteristics, and protein phosphorylation regulates endosome fusion.

Purpose of the Study:

  • Investigate protein phosphorylation in phagolysosome biogenesis.
  • Determine the role of endogenous kinases in phosphorylating phagosome proteins.

Main Methods:

  • In vitro phosphorylation assays using phagosome-associated kinases.
  • Analysis of protein phosphorylation on phagosome fractions.

Main Results:

  • Proteins phosphorylated on tyrosine residues were identified on phagosomes.
  • Complex phosphorylation and dephosphorylation cycles occur during phagolysosome biogenesis.

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  • Endosome fractions inhibited phagosome protein phosphorylation.

    • Conclusions:

    • Phosphorylation and dephosphorylation events are likely involved in regulating phagolysosome biogenesis.
    • These events may control in vivo interactions between phagosomes and endosomes.