The p21$^{RAS}$ Farnesyltransferase α Subunit in TGF-β and Activin Signaling

The α subunit of p21$^{RAS}$ farnesyltransferase (FNTA), which is also shared by geranylgeranyltransferase, was isolated as a specific cytoplasmic interactor of the transforming growth factor-β (TGF-β) and activin type I receptors with the use of the yeast two-hybrid system. FNTA interacts specifica...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1996-02, Vol.271 (5252), p.1120-1122
Main Authors: Wang, Tongwen, Danielson, Paul D., Li, Bi-yu, Shah, Paresh C., Kim, Stephen D., Donahoe, Patricia K.
Format: Article
Language:English
Subjects:
Activin Receptors
Activin Receptors, Type I
Activins
Alkyl and Aryl Transferases
Amino Acid Sequence
Amino acids
Animals
Antibodies
B lymphocytes
Base Sequence
Cell Line
COS cells
Gin
Humans
Inhibins - metabolism
Libraries
Ligands
Molecular Sequence Data
Mutation
Phosphorylation
Protein-Serine-Threonine Kinases - chemistry
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Receptor, Transforming Growth Factor-beta Type I
Receptor, Transforming Growth Factor-beta Type II
Receptors
Receptors, Growth Factor - metabolism
Receptors, Transforming Growth Factor beta - chemistry
Receptors, Transforming Growth Factor beta - genetics
Receptors, Transforming Growth Factor beta - metabolism
Recombinant Fusion Proteins - metabolism
Signal Transduction
Transferases - metabolism
Transforming Growth Factor beta - metabolism
Yeasts
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Summary:The α subunit of p21$^{RAS}$ farnesyltransferase (FNTA), which is also shared by geranylgeranyltransferase, was isolated as a specific cytoplasmic interactor of the transforming growth factor-β (TGF-β) and activin type I receptors with the use of the yeast two-hybrid system. FNTA interacts specifically with ligand-free TGF-β type I receptor but is phosphorylated and released upon ligand binding. Furthermore, the release is dependent on the kinase activity of the TGF-β type II receptor. Thus, the growth inhibitory and differentiative pathways activated by TGF-β 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$^{RAS}$.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.271.5252.1120