| pubmed-article:18786395 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C1426592 | lld:lifeskim |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C1863551 | lld:lifeskim |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C1425164 | lld:lifeskim |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C1549781 | lld:lifeskim |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:18786395 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:18786395 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:18786395 | pubmed:dateCreated | 2008-9-12 | lld:pubmed |
| pubmed-article:18786395 | pubmed:abstractText | Formins induce the nucleation and polymerization of unbranched actin filaments. They share three homology domains required for profilin binding, actin polymerization, and regulation. Diaphanous-related formins (DRFs) are activated by GTPases of the Rho/Rac family, whose interaction with the N-terminal formin domain is thought to displace a C-terminal Diaphanous-autoregulatory domain (DAD). We have determined the structure of the N-terminal domains of FHOD1 consisting of a GTPase-binding domain (GBD) and the DAD-recognition domain FH3. In contrast to the formin mDia1, the FHOD1-GBD reveals a ubiquitin superfold as found similarly in c-Raf1 or PI3 kinase. This GBD is recruited by Rac and Ras GTPases in cells and plays an essential role for FHOD1-mediated actin remodeling. The FHOD1-FH3 domain is composed of five armadillo repeats, similarly to other formins. Mutation of one residue in the predicted DAD-interaction surface efficiently activates FHOD1 in cells. These results demonstrate that DRFs have evolved different molecular solutions to govern their autoregulation and GTPase specificity. | lld:pubmed |
| pubmed-article:18786395 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18786395 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18786395 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18786395 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18786395 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18786395 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18786395 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18786395 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:18786395 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:18786395 | pubmed:author | pubmed-author:RakAlexeyA | lld:pubmed |
| pubmed-article:18786395 | pubmed:author | pubmed-author:FacklerOliver... | lld:pubmed |
| pubmed-article:18786395 | pubmed:author | pubmed-author:GeyerMatthias... | lld:pubmed |
| pubmed-article:18786395 | pubmed:author | pubmed-author:PylypenkoOlen... | lld:pubmed |
| pubmed-article:18786395 | pubmed:author | pubmed-author:SchulteAntjeA | lld:pubmed |
| pubmed-article:18786395 | pubmed:author | pubmed-author:SchönichenAnd... | lld:pubmed |
| pubmed-article:18786395 | pubmed:author | pubmed-author:StolpBettinaB | lld:pubmed |
| pubmed-article:18786395 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18786395 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:18786395 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:18786395 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18786395 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18786395 | pubmed:pagination | 1313-23 | lld:pubmed |
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| pubmed-article:18786395 | pubmed:meshHeading | pubmed-meshheading:18786395... | lld:pubmed |
| pubmed-article:18786395 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18786395 | pubmed:articleTitle | The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation. | lld:pubmed |
| pubmed-article:18786395 | pubmed:affiliation | Abteilung Physikalische Biochemie, Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany. | lld:pubmed |
| pubmed-article:18786395 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18786395 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:29109 | entrezgene:pubmed | pubmed-article:18786395 | lld:entrezgene |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18786395 | lld:pubmed |
