Regulatory role of major tyrosine autophosphorylation site of kinase domain of c-Met receptor (scatter factor/hepatocyte growth factor receptor) - PubMed (original) (raw)
. 1994 Jun 10;269(23):16131-6.
Affiliations
- PMID: 7515877
Free article
Regulatory role of major tyrosine autophosphorylation site of kinase domain of c-Met receptor (scatter factor/hepatocyte growth factor receptor)
M Komada et al. J Biol Chem. 1994.
Free article
Abstract
Ligand-induced tyrosine kinase activation of the scatter factor/hepatocyte growth factor receptor (c-Met) is thought to be essential for the biological responses of target cells. To assess the regulatory role of the major tyrosine autophosphorylation site (tyrosine 1233) of the mouse c-Met receptor in the tyrosine kinase activation of the receptor, we constructed a mutant receptor in which the tyrosine residue was replaced with phenylalanine. When the cells expressing the mutant receptor were incubated with the ligand, no biological responses were observed, and the level of tyrosine phosphorylation of the receptor was very low compared with that of the wild-type receptor. The in vitro kinase activity of the mutant receptor toward an exogenous substrate and the receptor itself was also low. Furthermore, tyrosine phosphorylation of the cellular proteins by ligand stimulation was not detected in intact cells expressing the mutant receptor. The low level of kinase activity and the lack of biological activity of the mutant receptor indicate that the major autophosphorylation site positively regulates the tyrosine kinase of the c-Met receptor and phosphorylation of cellular substrates in the scatter factor/hepatocyte growth factor signaling pathway.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous