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Low-density lipoprotein receptor class A domain containing 4 (LDLRAD4) is a single-pass membrane receptor in the LDLR family, characterized by the presence of a class A domain that mediates ligand binding. LDLRAD4 mainly acts as a negative regulator of the TGF-beta signaling pathway, thus impacting key cellular processes such as proliferation, migration, apoptosis, and extracellular matrix production. It is expressed in various tissues, with upregulation documented in liver cancer cells where it promotes tumorigenesis. Its molecular interactions include binding to R-SMAD proteins and the E3 ubiquitin ligase Nedd4. Pathogenic mutations or dysregulation in LDLRAD4 can contribute to cancer and rare developmental disorders. Elevated expression or functional alteration may serve as a biomarker or therapeutic target in oncology and other diseases.
Inhibits TGF-beta signaling by binding SMAD2/3 and competing with canonical pathway components, thereby modulating cell growth, differentiation, and apoptosis
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