| pubmed-article:17714703 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17714703 | lifeskim:mentions | umls-concept:C0887870 | lld:lifeskim |
| pubmed-article:17714703 | lifeskim:mentions | umls-concept:C0010853 | lld:lifeskim |
| pubmed-article:17714703 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:17714703 | lifeskim:mentions | umls-concept:C1166758 | lld:lifeskim |
| pubmed-article:17714703 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
| pubmed-article:17714703 | lifeskim:mentions | umls-concept:C1422572 | lld:lifeskim |
| pubmed-article:17714703 | lifeskim:mentions | umls-concept:C1416989 | lld:lifeskim |
| pubmed-article:17714703 | lifeskim:mentions | umls-concept:C1158770 | lld:lifeskim |
| pubmed-article:17714703 | lifeskim:mentions | umls-concept:C1424810 | lld:lifeskim |
| pubmed-article:17714703 | lifeskim:mentions | umls-concept:C0680829 | lld:lifeskim |
| pubmed-article:17714703 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:17714703 | pubmed:dateCreated | 2007-9-21 | lld:pubmed |
| pubmed-article:17714703 | pubmed:abstractText | RhoA is a crucial regulator of stress fiber and focal adhesion formation through the activation of actin nucleation and polymerization. It also regulates the nuclear translocation of myocardin-related transcription factor-A and -B (MRTF-A/B, MAL or MKL 1/2), which are co-activators of serum response factor (SRF). In dominant-negative MRTF-A (DN-MRTF-A)-expressing NIH 3T3 cell lines, the expressions of several cytoskeletal/focal adhesion genes were down-regulated, and the formation of stress fiber and focal adhesion was severely diminished. MRTF-A/B-knockdown cells also exhibited such cytoskeletal defects. In reporter assays, both RhoA and MRTF-A enhanced promoter activities of these genes in a CArG-box-dependent manner, and DN-MRTF-A inhibited the RhoA-mediated activation of these promoters. In dominant-negative RhoA (RhoA-N19)-expressing NIH 3T3 cell lines, the nuclear translocation of MRTF-A/B was predominantly prevented, resulting in the reduced expression of cytoskeletal/focal adhesion proteins. Further, constitutive-active MRTF-A/B increased the expression of endogenous cytoskeletal/focal adhesion proteins, and thereby rescued the defective phenotype of stress fibers and focal adhesions in RhoA-N19 expressing cells. These results indicate that MRTF-A/B act as pivotal mediators of stress fiber and focal adhesion formation via the transcriptional regulation of a subset of cytoskeletal/focal adhesion genes. | lld:pubmed |
| pubmed-article:17714703 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17714703 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17714703 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17714703 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17714703 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:17714703 | pubmed:issn | 0014-4827 | lld:pubmed |
| pubmed-article:17714703 | pubmed:author | pubmed-author:SobueKenjiK | lld:pubmed |
| pubmed-article:17714703 | pubmed:author | pubmed-author:MoritaTsuyosh... | lld:pubmed |
| pubmed-article:17714703 | pubmed:author | pubmed-author:MayanagiTaira... | lld:pubmed |
| pubmed-article:17714703 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17714703 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:17714703 | pubmed:volume | 313 | lld:pubmed |
| pubmed-article:17714703 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17714703 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17714703 | pubmed:pagination | 3432-45 | lld:pubmed |
| pubmed-article:17714703 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:17714703 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17714703 | pubmed:articleTitle | Reorganization of the actin cytoskeleton via transcriptional regulation of cytoskeletal/focal adhesion genes by myocardin-related transcription factors (MRTFs/MAL/MKLs). | lld:pubmed |
| pubmed-article:17714703 | pubmed:affiliation | Depertment of Neuroscience (D13), Osaka University Graduate School of Medicine, Yamadaoka 2-2, Suita, Osaka, Japan. | lld:pubmed |
| pubmed-article:17714703 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17714703 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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