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    Cell. 1993 Nov 19;75(4):681-92.

    Cloning of a TGF beta type I receptor that forms a heteromeric complex with the TGF beta type II receptor.

    Franzén P, ten Dijke P, Ichijo H, Yamashita H, Schulz P, Heldin CH, Miyazono K.

    Ludwig Institute for Cancer Research, Biomedical Center, Uppsala, Sweden.

    A cDNA clone encoding a 53 kd serine/threonine kinase receptor with an overall structure similar to that of the type II receptor for transforming growth factor beta (TGF beta) was obtained. 125I-TGF beta 1 bound to porcine endothelial cells transfected with the cDNA and formed a cross-linked complex of 70 kd, characteristic of a TGF beta type I receptor. Immunoprecipitation of the cross-linked complexes by antibodies against the cloned receptor revealed the 70 kd complex as well as a 94 kd TGF beta type II receptor complex. The immunoprecipitated novel serine/threonine kinase receptor had biochemical properties of the TGF beta type I receptor and was observed in different cell types. Transfection of the cloned cDNA into TGF beta type I receptor-deficient cells restored TGF beta-induced plasminogen activator inhibitor 1 production. These results suggest that signal transduction by TGF beta involves the formation of a heteromeric complex of two different serine/threonine kinase receptors.

    PMID: 8242743 [PubMed - indexed for MEDLINE]

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