Article Abstract:
Betaglycan (transforming growth factor-beta (TGF-beta) type III receptor), a distinct TGF-beta, binds membrane protein TGF beta to receptor II, develops a high affinity ternary complex, enhances cell sensitivity to TGF-beta and receptor binding affinity and removes significant differences between TGF-beta isoform. TGF-beta signals through a heteromeric protein receptor that possesses a resticted ability to bind ligand, and betaglycan overcomes this restriction. TGF-beta's access to the signaling receptors is directly controlled by betaglycan.
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Article Abstract:
MAD (Mothers against dpp) belong to a novel class of signaling proteins that function downstream in the Ser/Thr kinase signaling pathways. MAD and its mammalian homolog MADR1 are regulated by signal transduction pathway of DPP/BMP2 (Decantaplegic/bone morphogenic protein2). The activation of BMP2 signaling pathways results in the quantitative phosphorylation of MADR1 in a specific tryptic peptide. MADR1 phosphorylation is not regulated by transforming growth factor beta and activin due to the specificity of MAD protein regulation.
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Article Abstract:
Drosophila decapentaplegic (dpp) signaling is mediated by the punt gene product and the Drosophila punt gene encodes atr-II, a type II receptor that binds activin. Drosophila with punt mutations have characteristics similar to those with mutations in the sax, tkv and dpp genes. The punt gene product will bind bone morphogenetic protein-2 (BMP2) with tkv or sax, but not alone.
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