Abstract
Coronin, a 57 kDa actin binding protein elutes with an apparent molecular mass of 400-600 kDa from gel filtration columns. This fraction is not unrelated to the reported 200 kDa complex where coronin is associated with phox proteins of the NADPH-oxidase. Phosphatidylinositol 3-kinase (PI 3-kinase) solubilizes coronin from the 400-600 kDa complex, thus constitutive active PI 3-kinase is sufficient to disrupt the complex, whereas wortmannin stabilizes it. Conversely, the phox protein associated pool of coronin is PI 3-kinase independent. During phagocytosis coronin is recruited together with PI 3-kinase to membranes of nascent and early phagosomes co-localizing with the actin cytoskeleton, confirming that coronin contributes to phagocytosis.
MeSH terms
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Actins / analysis
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Androstadienes / pharmacology
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Animals
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Cell Line
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Cell Membrane / metabolism
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Cytoskeleton / chemistry
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Cytosol / metabolism
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Enzyme Inhibitors / pharmacology
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Fluorescent Antibody Technique
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Humans
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Macrophages / metabolism
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Mice
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Microfilament Proteins / analysis
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Microfilament Proteins / metabolism*
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Molecular Weight
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Phagocytosis
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Phagosomes / metabolism
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Phagosomes / ultrastructure
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Phosphatidylinositol 3-Kinases / analysis
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Phosphatidylinositol 3-Kinases / metabolism*
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Phosphoinositide-3 Kinase Inhibitors
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Receptors, Complement / physiology
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Receptors, Fc / physiology
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Wortmannin
Substances
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Actins
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Androstadienes
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Enzyme Inhibitors
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Microfilament Proteins
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Phosphoinositide-3 Kinase Inhibitors
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Receptors, Complement
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Receptors, Fc
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coronin proteins
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Wortmannin