Coronin, actin binding protein 1B (CORO1B)

Coronin, actin binding protein 1B (CORO1B) is an intracellular, WD repeat-containing actin-binding protein that regulates actin cytoskeleton remodeling. It localizes to the leading edge of migrating cells, coordinating the disassembly and remodeling of Arp2/3-mediated branched actin networks in lamellipodia by interacting with cortactin and cofilin. In endothelial and epithelial cells, CORO1B plays a critical role in cell–cell junction stability and tube formation during angiogenesis. Phosphorylation by kinases such as PKC modulates its activities. While it is widely expressed and essential for fundamental cellular processes, it is not currently considered a direct druggable target, though it is implicated in cell migration, vessel formation, and possibly cancer and neural repair[1][2][3][4][5].

Other names

CORO1BCoronin-1BCoronin 2 (used in some older protein nomenclature, but may also refer to different coronin family members in other classification schemes[2])coronin, actin binding protein, 1BDKFZp762I166

Not applicable; no drugs with known mechanism of action targeting CORO1B directly. CORO1B functions by antagonizing cortactin, promoting actin branch debranching, and modulating interactions with Arp2/3 and cofilin[2][4][5].