Evidence for a pool of coronin in mammalian cells that is sensitive to PI 3-kinase.

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.