Coro1a, short for Coronin 1A, is an actin-binding protein that plays diverse roles in multiple biological processes. It is involved in pathways related to cytoskeletal remodeling, which is crucial for various cellular functions such as endocytosis, cell movement, and vesicle trafficking. Its functions are essential for normal cellular and organismal development [1,2].

In Leydig cells exposed to cadmium, Coro1a up-regulation leads to cytoskeleton disruption, reducing low-density lipoprotein (LDL) uptake, lipid droplet number, total cholesterol, and progesterone production. Silencing Coro1a rescues these effects, highlighting its role in steroidogenesis [1]. In neuronal morphogenesis, Coro1a localizes to growth cones and filopodial structures and is required for netrin-dependent axon turning, branching, and corpus callosum development, collaborating with TRIM67 in the netrin pathway [2]. In triple-negative breast cancer (TNBC), Coro1a is crucial for cancer progression, and its neddylation-mediated degradation by a molecular glue shows antitumor effects [3]. In non-alcoholic steatohepatitis (NASH), CREBH inhibits Coro1a expression, and overexpression of Coro1a in liver cells inhibits autophagic flux and elevates inflammatory cytokine levels [4]. Also, Coro1a is associated with neutrophil extracellular trap (NET) formation, as Wip1 directly dephosphorylates Coro1a, negatively regulating NET formation during infection [5].

In summary, Coro1a is a key protein involved in cytoskeletal-related functions, influencing processes like steroidogenesis, neuronal development, cancer progression, autophagy in NASH, and immune response through NET formation. Gene knockout or knockdown models in these contexts have been instrumental in revealing its functions, providing insights into diseases such as cadmium-induced steroid hormone deficiency, TNBC, NASH, and bacterial infections [1,2,3,4,5].