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

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).
Mesh Terms:
Activin Receptors, Activin Receptors, Type I, Activins, Alkyl and Aryl Transferases, Amino Acid Sequence, Animals, Base Sequence, Cell Line, Humans, Inhibins, Ligands, Molecular Sequence Data, Mutation, Phosphorylation, Protein-Serine-Threonine Kinases, Receptors, Growth Factor, Receptors, Transforming Growth Factor beta, Recombinant Fusion Proteins, Signal Transduction, Transferases, Transforming Growth Factor beta
Science
Date: Feb. 23, 1996
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