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Promiscuity and specificity in BMP receptor activation
Author(s) -
Mueller Thomas D.,
Nickel Joachim
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.02.043
Subject(s) - receptor , superfamily , biology , microbiology and biotechnology , bone morphogenetic protein , ligand (biochemistry) , transforming growth factor , growth differentiation factor , g protein coupled receptor , signal transduction , biochemistry , gene
Bone Morphogenetic Proteins (BMPs), together with Transforming Growth Factor (TGF)‐β and Activins/Inhibins constitute the TGF‐β superfamily of ligands. This superfamily is formed by more than 30 structurally related secreted proteins. Since TGF‐β members act as morphogens, either a strict relation between a particular ligand to a distinct cellular receptor and/or temporospatial expression patterns of ligands and receptors is expected. Instead, only a limited number of receptors exist implicating promiscuous interactions of ligands and receptors. Furthermore, in complex tissues a multitude of different ligands can be found, which signal via overlapping subsets of receptors. This raises the intriguing question how concerted interactions of different ligands and receptors generate highly specific cellular signals, which are required during development and tissue homeostasis.