Abstract
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.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Bone Morphogenetic Protein Receptors
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Bone Morphogenetic Proteins
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Cell Line
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Cloning, Molecular / methods
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DNA Primers
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DNA, Complementary
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Glioblastoma
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Growth Substances / metabolism
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Molecular Sequence Data
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Phylogeny
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Polymerase Chain Reaction
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Proteins / metabolism*
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RNA, Messenger / metabolism
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Rats
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Receptors, Cell Surface / biosynthesis
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Receptors, Cell Surface / chemistry
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Receptors, Cell Surface / metabolism*
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Receptors, Growth Factor*
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
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Substantia Nigra / metabolism
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Transcription, Genetic
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Transfection
Substances
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Bone Morphogenetic Proteins
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DNA Primers
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DNA, Complementary
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Growth Substances
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Proteins
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RNA, Messenger
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Receptors, Cell Surface
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Receptors, Growth Factor
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Recombinant Proteins
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Bone Morphogenetic Protein Receptors