Source:http://linkedlifedata.com/resource/pubmed/id/11165482
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2001-2-22
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| pubmed:abstractText |
Smad6 and Smad7 comprise a subclass of vertebrate Smads that antagonize, rather than transduce, TGF-beta family signaling. These Anti-Smads can block BMP signaling, as evidenced by their ability to induce a secondary dorsal axis when misexpressed ventrally in Xenopus embryos. Smad7 inhibits additional TGF-beta related pathways, and causes spina bifida when misexpressed dorsally. We have performed structure-function analyses to identify domains of Anti-Smads that are responsible for their shared and unique activities. We find that the C-terminal domain of Smad7 displays strong axis inducing activity but cannot induce spina bifida. The isolated N-terminal domain of Smad7 is inactive but restores the ability of the C-terminus to cause spina bifida when the two are co-expressed. By contrast, the N- and C-terminal domains of Smad6 have weak axis inducing activity when expressed individually, but show full activity when co-expressed. Chimeric analysis demonstrates that the C-terminal domain of Smad7, but not Smad6, can induce spina bifida when fused to the N-terminal domain of either Smad6 or Smad7. Thus, although the C-terminal domain is the primary determinant of the intrinsic activity of Xenopus Anti-Smads, the N-terminal domain is essential for full activity, is interchangeable between Smad6 and 7, and can function in trans.
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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/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/Smad6 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Smad6 protein, Xenopus,
http://linkedlifedata.com/resource/pubmed/chemical/Smad7 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Smad7 protein, Xenopus,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0925-4773
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
100
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
251-62
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:11165482-Animals,
pubmed-meshheading:11165482-Blotting, Western,
pubmed-meshheading:11165482-Bone Morphogenetic Proteins,
pubmed-meshheading:11165482-DNA-Binding Proteins,
pubmed-meshheading:11165482-Gene Deletion,
pubmed-meshheading:11165482-Models, Genetic,
pubmed-meshheading:11165482-Mutation,
pubmed-meshheading:11165482-Phenotype,
pubmed-meshheading:11165482-Plasmids,
pubmed-meshheading:11165482-Protein Structure, Tertiary,
pubmed-meshheading:11165482-RNA,
pubmed-meshheading:11165482-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:11165482-Signal Transduction,
pubmed-meshheading:11165482-Smad6 Protein,
pubmed-meshheading:11165482-Smad7 Protein,
pubmed-meshheading:11165482-Spinal Dysraphism,
pubmed-meshheading:11165482-Structure-Activity Relationship,
pubmed-meshheading:11165482-Time Factors,
pubmed-meshheading:11165482-Trans-Activators,
pubmed-meshheading:11165482-Xenopus,
pubmed-meshheading:11165482-Xenopus Proteins
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| pubmed:year |
2001
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| pubmed:articleTitle |
Dissection of inhibitory Smad proteins: both N- and C-terminal domains are necessary for full activities of Xenopus Smad6 and Smad7.
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| pubmed:affiliation |
Department of Cell and Developmental Biology, L215, School of Medicine, Oregon Health Sciences University, Portland 97201-3098, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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