Open AccessThe low-affinity p75 nerve growth factor (NGF) receptor mediates NGF-induced tyrosine phosphorylation.
Author(s) -
Margaret M. Berg,
David Sternberg,
Barbara L. Hempstead,
Moses V. Chao
Publication year - 1991
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.88.16.7106
Subject(s) - tyrosine phosphorylation , nerve growth factor , phosphorylation , trk receptor , tyrosine , receptor tyrosine kinase , low affinity nerve growth factor receptor , tyrosine kinase , microbiology and biotechnology , biology , tropomyosin receptor kinase a , signal transduction , chemistry , receptor , biochemistry
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.