Introduction
The TGF-β superfamily consists of over 30 structurally related members. The proteins encoded by TGF-β superfamily genes are processed to produce mature peptides by proteolytic cleavage. The TGF-β superfamily signaling begins with the secretion of TGF-β ligand peptides. These peptides are dimerized into homodimers or heterodimers and are secreted from the cell. Secreted dimers bind to their respective type I and type II serine/threonine kinase receptors and elicit transcriptional responses through phosphorylation of the receptors-regulated Smad proteins (R-Smads). In vertebrates, the type I receptors for bone morphogenetic proteins (BMPs) phosphorylate Smad1 or the closely related Smad5 and Smad8; whereas the type I receptors for TGF-βs, Activins and Nodal signal through Smad2 and Smad3. Phosphorylated R-Smads form heteromeric complexes with a common Smad, Smad4, and translocate into the nucleus to regulate target gene expression. Diverse nuclear DNA binding proteins interact with R-Smad/Smad4 complexes in the nucleus, mediating cell type-specific responses to TGF-β signaling.
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