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      The p21(RAS) farnesyltransferase alpha subunit in TGF-beta and activin signaling.

      Science (New York, N.Y.)
      Activin Receptors, Activin Receptors, Type I, Activins, Alkyl and Aryl Transferases, Amino Acid Sequence, Animals, Base Sequence, Cell Line, Humans, Inhibins, metabolism, Ligands, Molecular Sequence Data, Mutation, Phosphorylation, Protein-Serine-Threonine Kinases, chemistry, genetics, Receptors, Growth Factor, Receptors, Transforming Growth Factor beta, Recombinant Fusion Proteins, Signal Transduction, Transferases, Transforming Growth Factor beta

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          Abstract

          The alpha subunit of p21(RAS) farnesyltransferase (FNTA), which is also shared by geranylgeranyltransferase, was isolated as a specific cytoplasmic interactor of the transforming growth factor-beta (TGF-beta) and activin type I receptors with the use of the yeast two-hybrid system. FNTA interacts specifically with ligand-free TGF-beta type l receptor but is phosphorylated and released upon ligand binding. Furthermore, the release is dependent on the kinase activity of the TGF-beta type II receptor. Thus, the growth inhibitory and differentiative pathways activated by TGF-beta and activin involve novel mechanisms of serine-threonine receptor phosphorylation-dependent release of cytoplasmic interactors and regulation of the activation of small G proteins, such as p21(RAS).

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