Cadherin EGF LAG seven-pass G-type receptor 1 (CELSR1)

Cadherin EGF LAG seven-pass G-type receptor 1 (CELSR1) is a neural-specific, developmentally regulated, nonclassical cadherin that acts as a core component of the planar cell polarity (PCP) pathway and is essential for the establishment of tissue polarity across epithelia and in neural development[1][4][5]. CELSR1 has a unique seven-transmembrane architecture characteristic of adhesion G protein-coupled receptors and possesses nine extracellular cadherin domains, seven EGF-like repeats, and two laminin G-like domains. It mediates homophilic cell-cell adhesion both in *cis* (on the same cell) and *trans* (between adjacent cells) via its cadherin domains, facilitating the asymmetric organization of other PCP proteins, notably Frizzled6 and Vangl2, which is crucial for processes such as neural tube closure and inner ear patterning[2][3][4][7]. Mutations in *CELSR1* can lead to severe developmental disorders, particularly neural tube defects and congenital heart disease[5]. While CELSR1 is considered a prospective therapeutic target for conditions associated with PCP dysfunction, there are currently no known drugs or clinical modulators targeting this receptor, and its endogenous ligands and downstream signaling mechanisms remain poorly characterized[5][7].

Other names

Flamingo homolog 2Cadherin family member 9Adhesion G protein-coupled receptor C1ADGRC1CDHF9FMI2HFMI2ME2LMPHM9Protocadherin flamingo 2