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Science 23 February 1996:
Vol. 271. no. 5252, pp. 1120 - 1122
DOI: 10.1126/science.271.5252.1120
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Reports

The p21RAS Farnesyltransferase alpha  Subunit in TGF-beta and Activin Signaling

Tongwen Wang, (1) Paul D. Danielson, Bi-yu Li, Paresh C. Shah, Stephen D. Kim, Patricia K. Donahoe (1)

The alpha  subunit of p21RAS 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 I 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 p21RAS.

Pediatric Surgical Research Laboratories, Massachusetts General Hospital, Boston, MA 02114, USA.
(1) To whom correspondence should be addressed. E-mail: Donahoe{at}helix.mgh.harvard.edu


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