Coronins are a family of WD repeat-containing, actin-binding proteins that localize to submembraneous areas and regulate cell motility and cytoskeletal rearrangement. Coronin 1A (CORO1A, CLIPINA, CLABP, TACO, p57) can form coiled coil-mediated homotrimeric complexes that influence early phagosome formation. PKC-dependent phosphorylation of Coronin 1B (CORO1B) at Serine 2 regulates leading edge dynamics and cell motility in fibroblasts through interactions with Arp2/3 complex. Coronin 1C (CORO1C, Coronin 3, HCRNN4) is abundant in differentiating Neuro-2a cells, PC-12 cells and primary oligodendrocytes, where it is thought to influence neuron morphogenesis and migration. Coronin 2A (CORO2A, CLIPINB, IR10, WDR2) is a component of the approximately 1.5-2 megadalton N-CoR (nuclear receptor corepressor) complex of 10-12 proteins, which recruits HDACs to generate repressive chromatin. Coronin 7 (CORO7, CRN7) localizes to the Golgi membrane and influences the organization of intracellular membrane compartments and vesicular trafficking. Coronin 2B (CORO2B, CLIPINC) and Coronin 6 (CORO6) are similar to other members of this family, since they possess a conserved basic N-terminal motif and 3-10 WD repeats clustered in one to two core domains.