Proteomic analysis reveals a role for protein kinase C-alpha in phagosome maturation. - Archive ouverte HAL Access content directly
Journal Articles Biochemical and Biophysical Research Communications Year : 2004

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

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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.

Dates and versions

pasteur-00820046 , version 1 (03-05-2013)

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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, 2004, 319 (3), pp.810-6. ⟨10.1016/j.bbrc.2004.05.054⟩. ⟨pasteur-00820046⟩

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