Abstract
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 language | English (US) |
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Pages (from-to) | 121-127 |
Number of pages | 7 |
Journal | Molecular cell |
Volume | 2 |
Issue number | 1 |
DOIs | |
State | Published - Jul 1998 |
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology