Smad2 transduces common signals from receptor serine-threonine and tyrosine kinases.

de Caestecker MP, Parks WT, Frank CJ, Castagnino P, Bottaro DP, Roberts AB, Lechleider RJ
Genes Dev. 1998 12 (11): 1587-92

PMID: 9620846 · PMCID: PMC316877 · DOI:10.1101/gad.12.11.1587

SMAD proteins mediate signals from receptor serine-threonine kinases (RSKs) of the TGF-beta superfamily. We demonstrate here that HGF and EGF, which signal through RTKs, can also mediate SMAD-dependent reporter gene activation and induce rapid phosphorylation of endogenous SMAD proteins by kinase(s) downstream of MEK1. HGF induces phosphorylation and nuclear translocation of epitope-tagged Smad2 and a mutation that blocks TGF-beta signaling also blocks HGF signal transduction. Smad2 may thus act as a common positive effector of TGF-beta- and HGF-induced signals and serve to modulate cross talk between RTK and RSK signaling pathways.

MeSH Terms (15)

Animals Cell Line DNA-Binding Proteins Epidermal Growth Factor Gene Expression Regulation Genes, Tumor Suppressor Hepatocyte Growth Factor Protein-Serine-Threonine Kinases Protein-Tyrosine Kinases Receptors, Transforming Growth Factor beta Signal Transduction Smad2 Protein Trans-Activators Transcriptional Activation Transfection

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