Wiktor Burdzinski

Abstract From sponges to mammals, TGFβ signalling is a central regulator of body plan, cell fate and tissue homeostasis, with receptor architecture highly conserved across metazoans. Here we identify unexpected evolutionary divergence within a key receptor structure: 12 independent ligand-binding domain (LBD) duplications across three receptor classes (ACVR1, BMPR2 and TGFBR2) in diverse vertebrate lineages, including fish, amphibians, birds, and mammals.

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Abstract TGFβs, BMPs and Activins regulate numerous developmental and homeostatic processes and signal through hetero-tetrameric receptor complexes composed of two types of serine/threonine kinase receptors. Each of the 33 different ligands possesses unique affinities towards specific receptor types. However, the lack of specific tools hampered simultaneous testing of ligand binding towards all BMP/TGFβ receptors.