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Cadherin EGF LAG seven-pass G-type receptor 3 (CELSR3) is a large transmembrane protein of the flamingo subgroup in the cadherin superfamily, characterized by nine cadherin repeats, seven epidermal growth factor-like (EGF) domains, two laminin G repeats, and a seven-helix transmembrane domain[1][2][5]. It functions primarily in cell adhesion and planar cell polarity signaling, coordinating directional growth, migration, and connectivity of neurons during development[2][3][1]. CELSR3 interacts with Frizzled3 to modulate neural circuit formation and is implicated in the formation of central nervous system architecture, neuronal migration, and cilia organization[2][3]. Its dysregulation has been associated with neurodevelopmental disorders, cancer, and aberrant tissue organization[2][3][4][7]. No FDA- or EMA-approved drugs currently target CELSR3 directly, and its mechanisms of pharmacological modulation are not established; it is, however, a candidate biomarker and target in oncology and neurology research[2][4][7].
Not established for any approved drugs; receptor participates in cell adhesion, PCP signaling, calcium signaling, and possibly non-canonical Wnt signaling via Frizzled3; experimental modulation affects intracellular calcium via PLC
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