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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2010-7-14
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mid1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/UNC-40 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/UNC-73 protein, C elegans
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1878-1551
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
961-72
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pubmed:meshHeading |
pubmed-meshheading:20627078-Animals,
pubmed-meshheading:20627078-Body Patterning,
pubmed-meshheading:20627078-Caenorhabditis elegans,
pubmed-meshheading:20627078-Caenorhabditis elegans Proteins,
pubmed-meshheading:20627078-Cell Adhesion Molecules,
pubmed-meshheading:20627078-Cell Differentiation,
pubmed-meshheading:20627078-Functional Laterality,
pubmed-meshheading:20627078-Gene Expression Regulation, Developmental,
pubmed-meshheading:20627078-Growth Cones,
pubmed-meshheading:20627078-Humans,
pubmed-meshheading:20627078-Microtubule Proteins,
pubmed-meshheading:20627078-Motor Neurons,
pubmed-meshheading:20627078-Muscle, Striated,
pubmed-meshheading:20627078-Nerve Tissue Proteins,
pubmed-meshheading:20627078-Nervous System,
pubmed-meshheading:20627078-Neuromuscular Junction,
pubmed-meshheading:20627078-Nuclear Proteins,
pubmed-meshheading:20627078-Transcription Factors
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pubmed:year |
2010
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pubmed:articleTitle |
MADD-2, a homolog of the Opitz syndrome protein MID1, regulates guidance to the midline through UNC-40 in Caenorhabditis elegans.
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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.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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