The low-affinity p75 nerve growth factor (NGF) receptor mediates NGF-induced tyrosine phosphorylation Academic Article uri icon

Overview

MeSH Major

  • Nerve Growth Factors
  • Protein-Tyrosine Kinases
  • Proto-Oncogene Proteins
  • Proto-Oncogenes
  • Receptors, Cell Surface

abstract

  • Protein tyrosine phosphorylation is a potential mechanism for initial signaling in PC12 cells during differentiation in response to nerve growth factor (NGF). NGF-induced tyrosine phosphorylation has been found to be initiated by the trk protooncogene, which participates in the formation of high-affinity NGF binding sites. In contrast to transfection of wild-type low-affinity p75 NGF receptors, transfection of p75NGFR with mutations in the cytoplasmic domain resulted in an inability of NGF to elicit tyrosine phosphorylation of intracellular substrates, indicating that p75NGFR is involved in initiating phosphorylation events by NGF. Even though the p75NGFR receptor does not possess any inherent tyrosine kinase activity, these experiments demonstrate that the p75NGFR has a potential role in NGF-induced tyrosine phosphorylation.

publication date

  • September 12, 1991

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC52242

PubMed ID

  • 1714587

Additional Document Info

start page

  • 7106

end page

  • 10

volume

  • 88

number

  • 16