Characterization of human FAST-1, a TGFβ and activin signal transducer

Shibin Zhou, Leigh Zawel, Christoph Lengauer, Kenneth W. Kinzler, Bert Vogelstein

Research output: Contribution to journalArticlepeer-review

207 Scopus citations


We have identified a human homolog of the Xenopus forkhead activin signal transducer-1 (xFAST-1). Although significantly different in sequence from its Xenopus counterpart, hFAST-1 shared with xFAST-1 the ability to bind to human Smad2 and activate an activin response element (ARE). The hFAST-1-dependent activation of ARE was completely dependent on endogenous Smad4 and stimulation by a TGFβ-like ligand. The hFAST-1 protein was shown to bind to a novel DNA motif, TGT (G/T) (T/G)ATT, an exact copy of which was present within the ARE. A single copy of this motif could activate a reporter in a TGFβ-dependent fashion but only when an adjacent Smad-binding element was present in the construct. These data suggest that responses to TGFβ family members may be mediated by a DNA-binding complex formed by hFAST-1, hSmad2, and hSmad4.

Original languageEnglish (US)
Pages (from-to)121-127
Number of pages7
JournalMolecular cell
Issue number1
StatePublished - Jul 1998

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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