Interaction of transforming growth factor-β receptor I with farnesyl-protein transferase-α in yeast and mammalian cells

Francesc Ventura, Fang Liu, Jacqueline Doody, Joan Massagué

Research output: Contribution to journalArticlepeer-review

45 Scopus citations

Abstract

Transforming growth factor β (TGF-β) signals through two transmembrane serine/threonine kinases, known as TβR-I and TβR-II. Several lines of evidence suggest that TβR-II acts as a primary receptor, binding TGF-β and phosphorylating TβR-I whose kinase activity then propagates the signal to unknown substrates. We report an interaction between TβR-I and the farnesylprotein transferase-α subunit (FT-α) both in a yeast two-hybrid system and in mammalian cells. These findings raise the possibility that TGF-β might regulate cellular functions by altering the ability of FT-α to catalyze isoprenylation of targets such as G proteins, lamins, or cytoskeletal components. However, we provide evidence that TGF-β action does not alter the overall protein isoprenyl transferase activity in Mv1Lu mink lung epithelial cells. In fact, the β subunits of farnesyl transferase and geranylgeranyl transferase, which are necessary for the activity of FT-α, prevent the association of FT-α with TβR-I. Furthermore, farnesyl transferase activity is shown to be dispensable for TGF-β signaling of growth inhibitory and transcriptional responses in these cells. These results suggest that the interaction between TβR-I and FT-α does not affect the known functions of these two proteins.

Original languageEnglish (US)
Pages (from-to)13931-13934
Number of pages4
JournalJournal of Biological Chemistry
Volume271
Issue number24
DOIs
StatePublished - 1996
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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