Cordon-bleu WH2 repeat protein (COBL)

Cordon-bleu WH2 repeat protein (COBL) is a multifunctional actin regulatory protein containing three C-terminal WH2 (Wiskott-Aldrich syndrome protein homology 2) domains[1][2][3][4]. COBL orchestrates actin nucleation, filament severing, and regulation of dynamic actin structures essential for numerous morphogenetic and cellular processes. In neurons, COBL drives dendritic arborization and neuromorphogenesis; in epithelial cells, it localizes to the basal region of microvilli, regulating their length and assembling specialized actin-based protrusions. It interacts with partners such as syndapin and BAR domain-containing proteins. The protein is crucial for brush border microvilli development, neural tube closure in embryogenesis, and the organization of cellular protrusions. Its core molecular property is catalyzing the generation and remodeling of unbranched actin filaments; however, it is not known to be a direct therapeutic target nor a major player in disease pathogenesis[1][2][3][4].

Other names

Protein cordon-bleuCOBLKIAA0633COBL_HUMANCobl protein, human

Not applicable; COBL is not targeted by any drugs. Its mechanism in cell biology involves actin nucleation/severing via WH2 domains and interaction with BAR domain proteins (such as syndapin, SNX9, ASAP1)