Tyrosine phosphorylation and tyrosine kinase activity of the trk proto-oncogene product induced by NGF

@article{Kaplan1991TyrosinePA,
  title={Tyrosine phosphorylation and tyrosine kinase activity of the trk proto-oncogene product induced by NGF},
  author={David R Kaplan and Dionisio Mart{\'i}n-Zanca and Luis F. Parada},
  journal={Nature},
  year={1991},
  volume={350},
  pages={158-160}
}
NERVE growth factor (NGF) is a neurotrophic factor responsible for the differentiation and survival of sympathetic and sensory neurons as well as selective populations of cholinergic neurons1,2. NGF binds to specific cell-surface receptors but the mechanism for transduction of the neurotrophic signal is unknown. Several experiments using the NGF-responsive pheochromocytoma cell line, PC12, have implicated tyrosine phosphorylation in NGF-mediated responses, although no NGF-specific tyrosine… 
Neurotrophin signal transduction by the Trk receptor.
TLDR
The attempts to understand the mechanisms used by Trk to generate the many phenotypic responses of PC12 cells to NGF are summarized.
Tyrosine kinase activity coupled to the high-affinity nerve growth factor-receptor complex.
  • S. Meakin, E. Shooter
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1991
TLDR
It is suggested that the high-affinity NGF-receptor complex is a substrate of tyrosine kinase activity, which can be blocked by an agent that inhibits NGF (and not epidermal growth factor)-induced tyosine phosphorylation in PC12 cells, as well as N GF-induced neuronal differentiation of PC 12 cells.
The low-affinity p75 nerve growth factor (NGF) receptor mediates NGF-induced tyrosine phosphorylation.
TLDR
It is demonstrated that transfection of p75NGFR with mutations in the cytoplasmic domain resulted in an inability of NGF to elicit tyrosine phosphorylation of intracellular substrates, indicating that p75 NGFR is involved in initiating phosphorylated events by NGF.
TrkA Tyrosine Residues Involved in NGF‐induced Neurite Outgrowth of PC12 Cells
TLDR
Intacellular tyrosine residues of TrkA involved in nerve growth factor‐induced neurite outgrowth of PC12 cells are identified using site‐directed mutagenesis and a PC12 cell line expressing very low levels of endogenous Trka (PC12nnr5 cells).
Specificity of nerve growth factor signaling: Differential patterns of early tyrosine phosphorylation events induced by NGF, EGF, and bFGF
TLDR
Data presented suggest that the temporal pattern of induced phosphorylation, the nature of induced associations with other phosphoproteins, and cell type‐specific components may all contribute to the generation of NGF signaling specificity.
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