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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Cell Line
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Cell Membrane / physiology
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Cross-Linking Reagents
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Kinetics
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Membrane Fusion
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Models, Biological
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Nerve Growth Factors / metabolism*
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Protein-Tyrosine Kinases / genetics*
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Proto-Oncogene Proteins / genetics*
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Proto-Oncogenes*
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Receptor, trkA
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Receptors, Cell Surface / genetics*
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Receptors, Cell Surface / metabolism
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Receptors, Nerve Growth Factor
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Transfection
Substances
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Cross-Linking Reagents
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Nerve Growth Factors
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Proto-Oncogene Proteins
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Receptors, Cell Surface
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Receptors, Nerve Growth Factor
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Protein-Tyrosine Kinases
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Receptor, trkA