TGF beta signals through a heteromeric protein kinase receptor complex

Cell. 1992 Dec 11;71(6):1003-14. doi: 10.1016/0092-8674(92)90395-s.


Transforming growth factor beta (TGF beta) binds with high affinity to the type II receptor, a transmembrane protein with a cytoplasmic serine/threonine kinase domain. We show that the type II receptor requires both its kinase activity and association with another TGF beta-binding protein, the type I receptor, to signal growth inhibition and early gene responses. Receptors I and II associate as interdependent components of a heteromeric complex: receptor I requires receptor II to bind TGF beta, and receptor II requires receptor I to signal. This mode of operation points to fundamental differences between this receptor and the protein-tyrosine kinase cytokine receptors.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding, Competitive
  • Cell Line
  • Mink
  • Models, Biological
  • Molecular Sequence Data
  • Multienzyme Complexes
  • Protein Kinases / metabolism*
  • Receptors, Cell Surface / metabolism*
  • Serine
  • Signal Transduction*
  • Threonine
  • Transforming Growth Factor beta / chemistry
  • Transforming Growth Factor beta / metabolism*


  • Multienzyme Complexes
  • Receptors, Cell Surface
  • Transforming Growth Factor beta
  • Threonine
  • Serine
  • Protein Kinases