Smad2 transduces common signals from receptor serinethreonine and tyrosine kinases

Mark P. De Caestecker, W. Tony Parks, Chistopher J. Frank, Paola Castagnino, Donald P. Bottaro, Anita B. Roberts, Robert J. Lechleider*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

255 Scopus citations


SMAD proteins mediate signals from receptor serinethreonine kinases (RSKs) of the TGF-β 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-β signaling also blocks HGF signal transduction. Smad2 may thus act as a common positive effector of TGF-β- and HGF-induced signals and serve to modulate cross talk between RTK and RSK signaling pathways.

Original languageEnglish (US)
Pages (from-to)1587-1592
Number of pages6
JournalGenes and Development
Issue number11
StatePublished - Jun 1 1998


  • HGF
  • Protein phosphorylation
  • Receptor kinases
  • SMAD
  • Signal transduction
  • TGF-β

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology


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