Coronin-1C (CORO1C)

Coronin-1C (CORO1C) is a highly conserved cytoskeletal regulator belonging to the WD40 repeat protein family. It binds and modulates the dynamics of F-actin through unique structural domains and is ubiquitously expressed in human tissues. Coronin-1C participates in actin filament rearrangement essential for cell motility, phagocytosis, and endocytosis. It also regulates vesicular trafficking, endosome fission, and lamellipodial protrusion. The protein features multiple isoforms due to alternative splicing and promoter usage, with tissue-specific roles including skeletal muscle and neuromuscular junction functions. In cancer biology, Coronin-1C is implicated in tumor progression and metastasis, notably acting as a suppressor of melanoma cell invasion. Knockout or loss of Coronin-1C enhances matrix degradation, invasion, and metastasis, especially to the brain and liver. While it presents as an attractive therapeutic target, direct clinical interventions or drugs are not yet available, and targeting approaches must consider its fundamental cellular roles and potential for deleterious side effects

Other names

Coronin-1CCORO1CCRN2CRNN4coronin-3HCRNN4hCRNN4coronin-1Ccoroninactin binding protein 1C

Not applicable, no drugs formally listed as targeting Coronin-1C in clinical use; generally, actin cytoskeleton-targeting agents disrupt cell movement and invasion, which may overlap with the biological pathway regulated by Coronin-1C