Ligand-dependent and -independent interactions with the transforming growth factor type II and I receptor subunits reside in the aminoterminal portion of the ectodomain of the type III subunit

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Abstract

The type III receptor for transforming growth factor beta (TGFβ), which exhibits no kinase activity, binds TGFβ1 and TGFβ2 and is involved in assembly and activity of the multi-subunit TGFβ signal transduction complex. Recently we showed that TGFβ receptor type III (TβRIII) can participate in a complex composed of the dimeric TGFβ ligand and a type III, II, and I receptor subunit. The interaction of the TβRIII subunit with TβRII is TGFβ-dependent, whereas interaction with TβRI is TGFβ-independent. Here we use coexpression of the three types of TGFβ receptors in baculoviral- infected insect cells to determine which parts of the unglycosylated TβRIII receptor participate in the binding of TGFβ, the TGFβ-dependent interaction with TβRII and the TGFβ-independent interaction with TβRI. The results suggest that the first 500 amino acid residues in the aminoterminal portion of TβRIII exhibit all three properties.

Original languageEnglish
Pages (from-to)232-238
Number of pages7
JournalIn Vitro Cellular and Developmental Biology - Animal
Volume34
Issue number3
DOIs
Publication statusPublished - 1998 Jan 1

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Keywords

  • Cytokines
  • FGF
  • Growth control
  • Growth factors
  • Heparan sulfate
  • Heparin

ASJC Scopus subject areas

  • Developmental Biology
  • Cell Biology

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