| http://purl.uniprot.org/citations/14996829 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14996829 | http://www.w3.org/2000/01/rdf-schema#comment | "Transforming growth factor beta (TGF-beta) ligands exert their biological effects through type II (TbetaRII) and type I receptors (TbetaRI). Unlike TGF-beta1 and -beta3, TGF-beta2 appears to require the co-receptor betaglycan (type III receptor, TbetaRIII) for high affinity binding and signaling. Recently, the TbetaRIII null mouse was generated and revealed significant non-overlapping phenotypes with the TGF-beta2 null mouse, implying the existence of TbetaRIII independent mechanisms for TGF-beta2 signaling. Because a variant of the type II receptor, the type II-B receptor (TbetaRII-B), has been suggested to mediate TGF-beta2 signaling in the absence of TbetaRIII, we directly tested the ability of TbetaRII-B to bind TGF-beta2. Here we show that the soluble extracellular domain of the type II-B receptor (sTbetaRII-B.Fc) bound TGF-beta1 and TGF-beta3 with high affinity (K(d) values = 31.7 +/- 22.8 and 74.6 +/-15.8 pm, respectively), but TGF-beta2 binding was undetectable at corresponding doses. Similar results were obtained for the soluble type II receptor (sTbetaRII.Fc). However, sTbetaRII.Fc or sTbetaRII-B.Fc in combination with soluble type I receptor (sTbetaRI.Fc) formed a high affinity complex that bound TGF-beta2, and this complex inhibited TGF-beta2 in a biological inhibition assay. These results show that TGF-beta2 has the potential to signal in the absence of TbetaRIII when sufficient TGF-beta2, TbetaRI, and TbetaRII or TbetaRII-B are present. Our data also support a cooperative model for receptor-ligand interactions, as has been suggested by crystallization studies of TGF-beta receptors and ligands. Our cell-free binding assay system will allow for testing of models of receptor-ligand complexes prior to actual solution of crystal structures."xsd:string |
| http://purl.uniprot.org/citations/14996829 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m401350200"xsd:string |
| http://purl.uniprot.org/citations/14996829 | http://purl.uniprot.org/core/author | "Lin H.Y."xsd:string |
| http://purl.uniprot.org/citations/14996829 | http://purl.uniprot.org/core/author | "Babitt J.L."xsd:string |
| http://purl.uniprot.org/citations/14996829 | http://purl.uniprot.org/core/author | "Schneyer A.L."xsd:string |
| http://purl.uniprot.org/citations/14996829 | http://purl.uniprot.org/core/author | "Pirani A."xsd:string |
| http://purl.uniprot.org/citations/14996829 | http://purl.uniprot.org/core/author | "del Re E."xsd:string |
| http://purl.uniprot.org/citations/14996829 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14996829 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/14996829 | http://purl.uniprot.org/core/pages | "22765-22772"xsd:string |
| http://purl.uniprot.org/citations/14996829 | http://purl.uniprot.org/core/title | "In the absence of type III receptor, the transforming growth factor (TGF)-beta type II-B receptor requires the type I receptor to bind TGF-beta2."xsd:string |
| http://purl.uniprot.org/citations/14996829 | http://purl.uniprot.org/core/volume | "279"xsd:string |
| http://purl.uniprot.org/citations/14996829 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/14996829 |
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