Promiscuity and specificity in BMP receptor activation

FEBS Lett. 2012 Jul 4;586(14):1846-59. doi: 10.1016/j.febslet.2012.02.043. Epub 2012 Mar 8.


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.

Publication types

  • Review

MeSH terms

  • Animals
  • Bone Morphogenetic Protein Receptors / metabolism*
  • Cysteine / chemistry
  • Epitopes / chemistry
  • Homeostasis
  • Humans
  • Hydrogen Bonding
  • Ligands
  • Models, Biological
  • Models, Molecular
  • Molecular Conformation
  • Phylogeny
  • Protein Binding
  • Protein Interaction Mapping
  • Signal Transduction
  • Time Factors
  • Transforming Growth Factor beta / metabolism


  • Epitopes
  • Ligands
  • Transforming Growth Factor beta
  • Bone Morphogenetic Protein Receptors
  • Cysteine