Calmodulin-regulated spectrin-associated protein family member 3 (CAMSAP3)

Calmodulin-regulated spectrin-associated protein family member 3 (CAMSAP3) is a highly conserved, non-centrosomal microtubule minus-end binding protein essential for the organization and spatial stabilization of microtubules in epithelial and neuronal cells[13][14][8][5][2][1]. CAMSAP3 tethers microtubules to cortical actin or membrane sites, helping establish cellular polarity—especially the apicobasal polarity in epithelial cells and the structural polarity of neurons by promoting single axon formation[8][5]. In multiciliated epithelial cells, CAMSAP3 is critical for organizing basal bodies and the axonemal microtubule architecture required for coordinated ciliary beating, with disruption resulting in ciliopathy-like phenotypes[11][2]. The protein contains characteristic domains mediating binding to microtubules (CKK domain), actin filaments, and association with calmodulin and spectrin, defining its classification among cytoskeletal scaffolding proteins[1]. CAMSAP3 is not currently considered a therapeutic target, and no drugs or endogenous ligands have been described to modulate its function. There are no known clinical applications as a biomarker or established safety concerns associated with its modulation.

Other names

CAMSAP3KIAA1543NezhaPPP1R80Calmodulin-regulated spectrin-associated protein 3Protein NezhaProtein phosphatase 1, regulatory subunit 80

null (no approved drugs—mechanism of action for experimental compounds not established)