Characterization of human FAST-1, a TGF beta and activin signal transducer.
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 TGF beta-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 TGF beta-dependent fashion but only when an adjacent Smad-binding element was present in the construct. These data suggest that responses to TGF beta family members may be mediated by a DNA- binding complex formed by hFAST-1, hSmad2, and hSmad4.[1]References
- Characterization of human FAST-1, a TGF beta and activin signal transducer. Zhou, S., Zawel, L., Lengauer, C., Kinzler, K.W., Vogelstein, B. Mol. Cell (1998) [Pubmed]
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