Abstract
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.
Original language | English (US) |
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Pages (from-to) | 678-683 |
Number of pages | 6 |
Journal | Nature |
Volume | 350 |
Issue number | 6320 |
DOIs | |
State | Published - 1991 |
ASJC Scopus subject areas
- General