Cingulin-like protein 1 (CGNL1)

Cingulin-like protein 1 (CGNL1), also known as paracingulin, is a cytoskeletal junctional adaptor protein encoded by the CGNL1 gene and found predominantly at tight and adherens junctions in epithelial and endothelial cells. It plays a pivotal role in assembling and maintaining cell–cell junctions by regulating activities of small GTPases (notably RhoA and Rac1), which are essential for organizing the actin cytoskeleton and preserving epithelial barrier function. CGNL1's structural domains include a globular head, a central coiled-coil rod, and a tail; it can form dimers and interacts with proteins such as ZO-1 and PLEKHA7, enabling localized modulation of cytoskeletal elements and junctional stability. In endothelium, CGNL1 is important for focal adhesion formation, vinculin and paxillin recruitment, and angiogenesis by stabilizing VE-cadherin interactions. While rearrangements of the CGNL1 promoter can cause aromatase excess syndrome, CGNL1 is not considered a therapeutic target nor are there drugs known to interact with it. The gene is conserved across vertebrates, with functions primarily in cell junction dynamics and cytoskeletal regulation.

Other names

ParacingulinJACOPJunction-associated coiled-coil proteinPCINGKIAA1749FLJ14957cingulin-like protein 1junction-associated coiled-coil proteinparacingulin