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

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

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1
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
DOI:
10.1016/s1097-2765(00)80120-3
[Indexed for MEDLINE]
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