High-affinity NGF binding requires coexpression of the trk proto-oncogene and the low-affinity NGF receptor

Nature. 1991 Apr 25;350(6320):678-83. doi: 10.1038/350678a0.


Nerve growth factor (NGF) interacts with two different low-affinity receptors that can be distinguished by affinity crosslinking. Reconstitution experiments by membrane fusion and transient transfection into heterologous cells indicate that high-affinity NGF binding requires coexpression and binding to both the low-affinity NGF receptor and the tyrosine kinase trk gene product. These studies reveal a new growth factor receptor-mediated mechanism of cellular differentiation involving trk and the low-affinity NGF receptor.

Publication types

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

MeSH terms

  • Animals
  • Cell Line
  • Cell Membrane / physiology
  • Cross-Linking Reagents
  • Kinetics
  • Membrane Fusion
  • Models, Biological
  • Nerve Growth Factors / metabolism*
  • Protein-Tyrosine Kinases / genetics*
  • Proto-Oncogene Proteins / genetics*
  • Proto-Oncogenes*
  • Receptor, trkA
  • Receptors, Cell Surface / genetics*
  • Receptors, Cell Surface / metabolism
  • Receptors, Nerve Growth Factor
  • Transfection


  • Cross-Linking Reagents
  • Nerve Growth Factors
  • Proto-Oncogene Proteins
  • Receptors, Cell Surface
  • Receptors, Nerve Growth Factor
  • Protein-Tyrosine Kinases
  • Receptor, trkA