LIM domain only protein 7 (LMO7)

LIM domain only protein 7 (LMO7) is a large, multifunctional scaffolding protein characterized by the presence of a LIM domain (a cysteine-rich, zinc-binding motif), a PDZ domain, an F-box domain, a calponin homology (CH) domain, and intrinsically disordered regions[1][2]. LMO7 is predominantly expressed in muscle and cardiac tissues, where it regulates cytoskeletal organization, cell adhesion, and gene transcription[1][2][3]. It is involved in the assembly of protein complexes at cell–cell junctions (notably through E-cadherin and nectin–afadin complexes), modulates actin cytoskeleton dynamics, and participates in the regulation of genes critical for muscle development, such as MyoD and Pax7[1][2][4]. LMO7 shuttles between the nucleus and cytoplasm, functioning in signal transduction between these compartments[2]. Dysregulation of LMO7 contributes to tumorigenesis by promoting cell proliferation, epithelial–mesenchymal transition (EMT), cell migration, and invasion, with roles in diverse cancers and muscular dystrophies[1][2][4]. LMO7 is being investigated as a prognostic marker and potential therapeutic target in cancer, although its pleiotropic cellular roles pose therapeutic challenges[1].

Other names

LIM domain 7FBXO20FBX20KIAA0858LMO-7LMO7bLOMPF-box only protein 20F-box protein Fbx20LIM domain only 7 proteinzinc-finger domain-containing protein