Coactosin-like protein 1 (COTL1)

Coactosin-like protein 1 (COTL1) is a highly conserved, small actin-binding protein that stabilizes filamentous actin (F-actin) and participates in the regulation of the actin cytoskeleton[1][4][8]. It is a member of the ADF/cofilin homology domain superfamily, binding selectively to F-actin but not monomeric actin, and distinguishes itself by stabilizing, rather than depolymerizing, actin filaments[8]. COTL1 acts as a chaperone for 5-lipoxygenase (ALOX5), stabilizing it and promoting leukotriene biosynthesis, implicating it in inflammatory signaling[1][7][8]. It is involved in maintaining and repairing epithelial barrier integrity, regulating actin remodeling during cell-cell junction and migration events, and is essential for proper adipocyte differentiation; mice deficient in COTL1 show resistance to obesity and steatosis[3][8]. In cancer, COTL1 is overexpressed and acts as a tumor antigen, being recognized by both cellular and humoral immune responses[4][6]. No drugs are currently known to target COTL1 directly, but its interactions with ALOX5 make it indirectly relevant to leukotriene pathway modulation.

Other names

Coactosin-like F-actin binding protein 1Coactosin-like proteinCLPcoactosin-like 1epididymis secretory sperm binding protein

None established for direct drug targeting; mechanistically, COTL1 modulates leukotriene biosynthesis via 5-LO stabilization