Molecular Cell
Volume 2, Issue 1, July 1998, Pages 121-127
Journal home page for Molecular Cell

Short Articles
Characterization of Human FAST-1, a TGFβ and Activin Signal Transducer

https://doi.org/10.1016/S1097-2765(00)80120-3Get rights and content
Under a Creative Commons license
open archive

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.

Cited by (0)