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Proteomic analysis reveals a role for protein kinase C-alpha in phagosome maturation.

Abstract : Acquisition of microbicidal properties by phagosomes requires the action of molecules which regulate the interactions between phagosomes and endocytic organelles. Members of the protein kinase C (PKC) superfamily of serine/threonine kinases are recruited to phagosomes with various kinetics during phagolysosome biogenesis. To study the role of PKC-alpha in this process, we compared the composition of latex bead-containing phagosomes isolated from control and dominant-negative (DN) PKC-alpha-overexpressing RAW 264.7 macrophages. Western blot analysis indicated that the levels of both lysosomal-associated membrane protein-1 and flotillin-1, which are acquired through interactions with late endosomes and lysosomes, are reduced in phagosomes from DN PKC-alpha-overexpressing macrophages. Proteomic characterization of latex bead-containing phagosomes revealed that recruitment of the small GTPase Rab7, cathepsin D, and cathepsin S is inhibited by DN PKC-alpha. Collectively, these data provide evidence that PKC-alpha plays a role in phagolysosome biogenesis, a critical process of the innate immune response against infections.
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https://hal-riip.archives-ouvertes.fr/pasteur-00820046
Contributor : Charles M. Dozois <>
Submitted on : Friday, May 3, 2013 - 4:35:18 AM
Last modification on : Monday, July 20, 2020 - 12:34:50 PM

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John Derek Ng Yan Hing, Michel Desjardins, Albert Descoteaux. Proteomic analysis reveals a role for protein kinase C-alpha in phagosome maturation.. Biochemical and Biophysical Research Communications, Elsevier, 2004, 319 (3), pp.810-6. ⟨10.1016/j.bbrc.2004.05.054⟩. ⟨pasteur-00820046⟩

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