Title : Bi-directional regulation of Ser-985 phosphorylation of c-met via protein kinase C and protein phosphatase 2A involves c-Met activation and cellular responsiveness to hepatocyte growth factor.

Pub. Date : 2004 Jun 18

PMID : 15075332






3 Functional Relationships(s)
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1 Previous studies indicated that treatment of cells with 12-O-tetradecanoylphorbol-13-acetate induced phosphorylation of Ser-985 at the juxtamembrane of c-Met, the receptor tyrosine kinase for hepatocyte growth factor (HGF), and this was associated with decreased tyrosine phosphorylation of c-Met. Tyrosine MET proto-oncogene, receptor tyrosine kinase Homo sapiens
2 Addition of HGF to A549 cells in culture induced c-Met tyrosine phosphorylation, the result being mitogenic response and cell scattering. Tyrosine MET proto-oncogene, receptor tyrosine kinase Homo sapiens
3 In contrast, in the presence of H(2)O(2) stress, HGF-dependent tyrosine phosphorylation of c-Met was largely suppressed with a reciprocal relationship to Ser-985 phosphorylation, and this event was associated with abrogation of cellular responsiveness to HGF. Tyrosine MET proto-oncogene, receptor tyrosine kinase Homo sapiens