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    Mol Cell. 1998 Jul;2(1):121-7.

    Characterization of human FAST-1, a TGF beta and activin signal transducer.

    Zhou S, Zawel L, Lengauer C, Kinzler KW, Vogelstein B.

    Source

    Howard Hughes Medical Institute, Johns Hopkins Oncology Center, Baltimore, Maryland 21231, USA.

    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 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.

    PMID:
    9702198
    [PubMed - indexed for MEDLINE]

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