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    Coronin is an actin binding protein which also interacts with microtubules and in some cell types is associated with phagocytosis.Coronin proteins are expressed in a large number of eukaryotic organisms from yeast to man.
    Yeast Coronin Crn1 and Drosophila Dpod1 were found crosslink actin and microtubule cytoskeleton. C.elegans POD-1 and Drosophila Coronin homologue regulate actin cytoskeleton and are involved in vesicular trafficking.
    Seven different isoforms of Coronin have been reported in mammals. The most well studied isoforms are Coronin 1 (Coronin 1A) and Coronin 1B. Coronin 1 exerted an inhibitory effect on cellular steady-state F-actin formation via an Arp2/3-dependent mechanism. Whereas Coronin 1 was required for chemokine-mediated migration, it was dispensable for T cell antigen receptor functions in T cells. Coronin 1B is required for efficient cell protrusion and migration. Recent study demonstrates that Coronin 1B inhibits the Arp2/3 complex activity by replacing it at the branched actin structure.Mammalian Coronin-7 does not interact with actin nor does it execute any actin mediated processes, but rather participate in Golgi trafficking.
    Although Coronin is present almost all eukaryotic organisms and have different functions, but everywhere these proteins have been shown to bind F-actin and localize in the dynamic F-actin rich area of cells. Recent study shows that Coronin prefers ATP/ADP-Pi containing F-actin over ADP containing F-actin, which might explain their unique cellular localization.


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