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Coronin-2A (CORO2A) is an actin-binding protein and a member of the WD repeat-containing protein family, acting as a multifunctional regulator that links nuclear receptor corepression to actin-based cellular processes[1][3][5]. It participates in the turnover of nuclear receptor co-repressor (NCoR) complexes at promoters of inflammatory genes in response to Toll-like receptor (TLR) signaling, thus influencing the transcriptional regulation of inflammation[5][3]. CORO2A interacts with nuclear and cytoplasmic actin, and is involved in SUMO-dependent control of inflammatory gene programs[3][5]. In cytoplasmic contexts, it localizes to actin stress fibers and focal adhesions—regulating focal-adhesion turnover and cell migration, particularly in aggressive cancer cells[3]. CORO2A directly interacts with EHD1 and is required for proper endosomal fission and recycling, especially for clathrin-independent cargo, by negatively regulating branched actin structures; its depletion leads to aberrant actin organization and impaired receptor trafficking[1]. Overexpression of CORO2A has been implicated in breast cancer progression and poor prognosis[2]. No direct pharmacological inhibitors or drugs are currently described.
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