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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| Authors: | Akiyoshi Taniguchi Koichi Matsuzaki Katsuya Nakano Mikio Kan Wallace L Mckeehan |
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| Institution: | (1) Albert B. Alkek Institute of Biosciences and Technology, Center for Cancer Biology and Nutrition, Department of Biochemistry & Biophysics, Texas A&M University, 2121 West Holcombe Boulevard, 77030-3303 Houston, Texas;(2) Present address: Department of Clinical Chemistry, School of Pharmaceutical Sciences, Toho University, Miyama 2-2-1, Funabashi, 274 Chiba, Japan;(3) Present address: Third Department of Internal Medicine, Kansai Medical University, 10-15 Fumizonocho, Moriguchi, 570 Osaka, Japan |
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| Abstract: | Summary 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. |
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| Keywords: | growth factors FGF heparan sulfate heparin growth control cytokines |
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