| pubmed-article:20627078 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20627078 | lifeskim:mentions | umls-concept:C0549183 | lld:lifeskim |
| pubmed-article:20627078 | lifeskim:mentions | umls-concept:C2936904 | lld:lifeskim |
| pubmed-article:20627078 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:20627078 | lifeskim:mentions | umls-concept:C1417167 | lld:lifeskim |
| pubmed-article:20627078 | lifeskim:mentions | umls-concept:C1959633 | lld:lifeskim |
| pubmed-article:20627078 | lifeskim:mentions | umls-concept:C0162610 | lld:lifeskim |
| pubmed-article:20627078 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:20627078 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:20627078 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:20627078 | pubmed:dateCreated | 2010-7-14 | lld:pubmed |
| pubmed-article:20627078 | pubmed:abstractText | The body muscles of Caenorhabditis elegans extend plasma membrane extensions called muscle arms to the midline motor axons to form the postsynaptic membrane of the neuromuscular junction. Through a screen for muscle arm development defective (Madd) mutants, we previously discovered that the UNC-40/DCC guidance receptor directs muscle arm extension through the Rho-GEF UNC-73. Here, we describe a gene identified through our mutant screen called madd-2, and show that it functions in an UNC-40 pathway. MADD-2 is a C1-TRIM protein and a homolog of human MID1, mutations in which cause Opitz Syndrome. We demonstrate that MADD-2 functions cell autonomously to direct muscle and axon extensions to the ventral midline of worms. Our results suggest that MADD-2 may enhance UNC-40 pathway activity by facilitating an interaction between UNC-40 and UNC-73. The analogous phenotypes that result from MADD-2 and MID1 mutations suggest that C1-TRIM proteins may have a conserved biological role in midline-oriented developmental events. | lld:pubmed |
| pubmed-article:20627078 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20627078 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20627078 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20627078 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20627078 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20627078 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20627078 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20627078 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20627078 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:20627078 | pubmed:issn | 1878-1551 | lld:pubmed |
| pubmed-article:20627078 | pubmed:author | pubmed-author:RoyPeter JPJ | lld:pubmed |
| pubmed-article:20627078 | pubmed:author | pubmed-author:SelmanGuiller... | lld:pubmed |
| pubmed-article:20627078 | pubmed:author | pubmed-author:AlexanderMari... | lld:pubmed |
| pubmed-article:20627078 | pubmed:author | pubmed-author:ByrneAlexandr... | lld:pubmed |
| pubmed-article:20627078 | pubmed:author | pubmed-author:ChanKevin... | lld:pubmed |
| pubmed-article:20627078 | pubmed:author | pubmed-author:SeetharamanAs... | lld:pubmed |
| pubmed-article:20627078 | pubmed:author | pubmed-author:D'SouzaSerena... | lld:pubmed |
| pubmed-article:20627078 | pubmed:copyrightInfo | Copyright 2010 Elsevier Inc. All rights reserved. | lld:pubmed |
| pubmed-article:20627078 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20627078 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:20627078 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:20627078 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20627078 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20627078 | pubmed:pagination | 961-72 | lld:pubmed |
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| pubmed-article:20627078 | pubmed:meshHeading | pubmed-meshheading:20627078... | lld:pubmed |
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| pubmed-article:20627078 | pubmed:meshHeading | pubmed-meshheading:20627078... | lld:pubmed |
| pubmed-article:20627078 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20627078 | pubmed:articleTitle | MADD-2, a homolog of the Opitz syndrome protein MID1, regulates guidance to the midline through UNC-40 in Caenorhabditis elegans. | lld:pubmed |
| pubmed-article:20627078 | pubmed:affiliation | Department of Molecular Genetics, The Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, 160 College Street, Toronto, ON M5S 3E1, Canada. | lld:pubmed |
| pubmed-article:20627078 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20627078 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:20627078 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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