Source:http://linkedlifedata.com/resource/pubmed/id/18184661
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
2008-3-17
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pubmed:abstractText |
The bone morphogenetic protein (BMP) family, the largest subfamily of the structurally conserved transforming growth factor-beta (TGF-beta) superfamily of growth factors, are multifunctional regulators of development, proliferation, and differentiation. The TGF-beta type III receptor (TbetaRIII or betaglycan) is an abundant cell surface proteoglycan that has been well characterized as a TGF-beta and inhibin receptor. Here we demonstrate that TbetaRIII functions as a BMP cell surface receptor. TbetaRIII directly and specifically binds to multiple members of the BMP subfamily, including BMP-2, BMP-4, BMP-7, and GDF-5, with similar kinetics and ligand binding domains as previously identified for TGF-beta. TbetaRIII also enhances ligand binding to the BMP type I receptors, whereas short hairpin RNA-mediated silencing of endogenous TbetaRIII attenuates BMP-mediated Smad1 phosphorylation. Using a biologically relevant model for TbetaRIII function, we demonstrate that BMP-2 specifically stimulates TbetaRIII-mediated epithelial to mesenchymal cell transformation. The ability of TbetaRIII to serve as a cell surface receptor and mediate BMP, inhibin, and TGF-beta signaling suggests a broader role for TbetaRIII in orchestrating TGF-beta superfamily signaling.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Inhibins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transforming Growth...,
http://linkedlifedata.com/resource/pubmed/chemical/SMAD1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Smad1 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta,
http://linkedlifedata.com/resource/pubmed/chemical/betaglycan
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
283
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7628-37
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pubmed:dateRevised |
2011-9-22
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pubmed:meshHeading |
pubmed-meshheading:18184661-Animals,
pubmed-meshheading:18184661-Bone Morphogenetic Proteins,
pubmed-meshheading:18184661-COS Cells,
pubmed-meshheading:18184661-Cercopithecus aethiops,
pubmed-meshheading:18184661-Humans,
pubmed-meshheading:18184661-Inhibins,
pubmed-meshheading:18184661-Kinetics,
pubmed-meshheading:18184661-Phosphorylation,
pubmed-meshheading:18184661-Protein Binding,
pubmed-meshheading:18184661-Proteoglycans,
pubmed-meshheading:18184661-Receptors, Transforming Growth Factor beta,
pubmed-meshheading:18184661-Signal Transduction,
pubmed-meshheading:18184661-Smad1 Protein,
pubmed-meshheading:18184661-Transforming Growth Factor beta
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pubmed:year |
2008
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pubmed:articleTitle |
Bone morphogenetic proteins signal through the transforming growth factor-beta type III receptor.
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pubmed:affiliation |
Department of Pharmacology and Cancer Biology, Duke University, Durham, North Carolina 27708, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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