Proceedings of the National Academy of Sciences · 1995 · 550 citations · 34 references
Life SciencesBiochemistryMolecular BiologyCell SignalingGene ExpressionSignal TransductionBone Morphogenetic Protein SignalingCell Surface Receptor SignalingCell-surface ReceptorsLigand BindingReceptor RegulationReceptor-mediated SignalingBmp ReceptorsBmp Signal ModulationBmp Signal TransductionBone Morphogenetic Protein ReceptorsCdna CloningComplementary Dna (Cdna) CloningReceptorsTranscriptional Activation
Bone morphogenetic proteins (BMPs) are members of the transforming growth factor‑beta superfamily that signal through type I and type II serine‑threonine kinase receptors. The study reports the cloning and characterization of a human BMP type II receptor. The authors cloned the cDNA of BMPR‑II, a receptor distantly related to the C. elegans DAF‑4.
Bone morphogenetic proteins (BMPs) are members of the transforming growth factor beta superfamily. Several members of this family have been shown to transduce their signals through binding to type I and type II serine-(threonine) kinase receptors. Here we report the cDNA cloning and characterization of a human type II receptor for BMPs (BMPR-II), which is distantly related to DAF-4, a BMP type II receptor from Caenorhabditis elegans. In transfected COS-1 cells, osteogenic protein (OP)-1/BMP-7, and less efficiently BMP-4, bound to BMPR-II. BMPR-II bound ligands only weakly alone, but the binding was facilitated by the presence of previously identified type I receptors for BMPs. Binding of OP-1/BMP-7 to BMPR-II was also observed in nontransfected cell lines. Moreover, a transcriptional activation signal was transduced by BMPR-II in the presence of type I receptors after stimulation by OP-1/BMP-7.
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TGFβ signals through a heteromeric protein kinase receptor complex
Jeffrey L. Wrana, Liliana Attisano, Juan M. Cárcamo et al. · Cell · 1992 · 1.5K citations