Source:http://linkedlifedata.com/resource/pubmed/id/21149453
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2011-2-14
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pubmed:abstractText |
Bone morphogenetic proteins (BMPs) regulate many mammalian physiologic and pathophysiologic processes. These proteins bind with the kinase receptors BMPR-I and BMPR-II, thereby activating Smad transcription factor. In this study, we demonstrate that neogenin, a receptor for netrins and proteins of the repulsive guidance molecule family, is a receptor for BMPs and modulates Smad signal transduction. Neogenin was found to bind directly with BMP-2, BMP-4, BMP-6, and BMP-7. Knockdown of neogenin in C2C12 cells resulted in the enhancement of the BMP-2-induced processes of osteoblastic differentiation and phosphorylation of Smad1, Smad5, and Smad8. Conversely, overexpression of neogenin in C2C12 cells suppressed these processes. Our results also indicated that BMP-induced activation of RhoA was mediated by neogenin. Inhibition of RhoA promoted BMP-2-induced processes of osteoblastic differentiation and phosphorylation of Smad1/5/8. However, treatment with Y-27632, an inhibitor of Rho-associated protein kinase, did not modulate BMP-induced phosphorylation of Smad1/5/8. Taken together, our findings suggest that neogenin negatively regulates the functions of BMP and that this effect of neogenin is mediated by the activation of RhoA.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/BMPR2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RHOA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Smad Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/neogenin,
http://linkedlifedata.com/resource/pubmed/chemical/rhoA GTP-Binding Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1083-351X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
18
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pubmed:volume |
286
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5157-65
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pubmed:meshHeading |
pubmed-meshheading:21149453-Bone Morphogenetic Protein Receptors, Type I,
pubmed-meshheading:21149453-Bone Morphogenetic Protein Receptors, Type II,
pubmed-meshheading:21149453-Bone Morphogenetic Proteins,
pubmed-meshheading:21149453-Cell Differentiation,
pubmed-meshheading:21149453-Enzyme Activation,
pubmed-meshheading:21149453-HEK293 Cells,
pubmed-meshheading:21149453-Humans,
pubmed-meshheading:21149453-Membrane Proteins,
pubmed-meshheading:21149453-Osteoblasts,
pubmed-meshheading:21149453-Phosphorylation,
pubmed-meshheading:21149453-Protein Binding,
pubmed-meshheading:21149453-Smad Proteins,
pubmed-meshheading:21149453-rhoA GTP-Binding Protein
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pubmed:year |
2011
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pubmed:articleTitle |
Neogenin, a receptor for bone morphogenetic proteins.
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pubmed:affiliation |
Department of Molecular Neuroscience, Graduate School of Medicine, Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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