Introduction
Members of the transforming growth factor β (TGF-β) superfamily are highly conserved across animals. They are found in both vertebrates and invertebrates, are ubiquitously expressed in diverse tissues and function during the earliest stages of development and throughout life. The TGF-β superfamily of secreted factors comprises more than 30 members including activins, nodals, bone morphogenetic proteins (BMPs), and growth and differentiation factors (GDFs).
Members of the TGF-β superfamily exert their effects by binding to specific serine/threonine kinase type I and type II receptor complexes. These receptors, known as TGF-β type I and type II receptors, or TβR-I and TR-II, are structurally similar and include small disulfide-rich ectodomains that adopt a three-finger toxin fold (∼120 residues), single-spanning transmembrane domains (∼30 residues), and cytoplasmic serine-threonine kinase domains (∼400 residues) .
Members of the TGF-β superfamily exert their effects by binding to specific serine/threonine kinase type I and type II receptor complexes. These receptors, known as TGF-β type I and type II receptors, or TβR-I and TR-II, are structurally similar and include small disulfide-rich ectodomains that adopt a three-finger toxin fold (∼120 residues), single-spanning transmembrane domains (∼30 residues), and cytoplasmic serine-threonine kinase domains (∼400 residues) .
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