Coronin

Coronin is an actin binding protein which also interacts with microtubules and in some cell types is associated with phagocytosis.

Initially, a 55 kDa protein was isolated from the actomyosin complex of Dictyostelium discoideum, which was later shown to bind actin in vitro.

But null mutation of coronin in D. discoideum resulted in impaired cytokinesis, and many actin mediated processes like endocytosis, cell motility etc.

The WD domain has no intrinsic catalytic activity and is thought to serve as a stable platform for simultaneous interaction.

The coronin-like proteins from budding yeast Crn1 and one of the coronins in Caenorhabditis elegans has a much longer unique region i.e. 194 vs 144aa.

Caenorhabditis elegans POD-1 and Drosophila coronin homologue regulate the actin cytoskeleton and are involved in vesicular trafficking.

[13] N-terminus signature region is reduced to 5aa and appears in front of each WD-repeat core domain (e.g., CRN7, POD-1) Human proteins which are members of the coronin family include: