High-affinity NGF binding requires coexpression of the trk proto-oncogene and the low-affinity NGF receptor.
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.
Hempstead
B L
BL
Department of Medicine, Cornell University Medical College, New York, New York 10021.
Martin-Zanca
D
D
Kaplan
D R
DR
Parada
L F
LF
Chao
M V
MV
D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000502:physiology; D003432:Cross-Linking Reagents; D007700:Kinetics; D008561:Membrane Fusion; D008954:Models, Biological; D009414:Nerve Growth Factors / Q000378:metabolism*; D011505:Protein-Tyrosine Kinases / Q000235:genetics*; D011518:Proto-Oncogene Proteins / Q000235:genetics*; D011519:Proto-Oncogenes; D020917:Receptor, trkA; D011956:Receptors, Cell Surface / Q000235:genetics* / Q000378:metabolism; D017475:Receptors, Nerve Growth Factor; D014162:Transfection
D003432:Cross-Linking Reagents; D009414:Nerve Growth Factors; D011518:Proto-Oncogene Proteins; D011956:Receptors, Cell Surface; D017475:Receptors, Nerve Growth Factor; D011505:Protein-Tyrosine Kinases; D020917:Receptor, trkA