Source:http://linkedlifedata.com/resource/pubmed/id/15704109
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2005-3-3
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pubmed:abstractText |
Dorsal closure in the fruit fly Drosophila melanogaster is a complex morphogenetic process, driven by sequential signaling cascades and involving multiple forces, which contribute to cell movements and rearrangements as well as to changes in cell shape. During closure, lateral epidermal cells elongate along the dorsoventral axis and subsequently spread dorsally to cover the embryonic dorsal surface. Amnioserosal cells, which are the original occupants of the most dorsal position in the developing embryo, constrict during closure; thus, the increase in epidermal surface area is accommodated by a reduction in the amnioserosal surface area. Several of the epidermal requirements for closure have been established in functional assays. In contrast, amnioserosal requirements for closure have remained elusive, in part because laser ablation and clonal approaches are limited to only subsets of amnioserosal cells. Here, we report our use of the UAS-GAL4 system to target expression of the cell autonomous toxin Ricin-A to all cells of the amnioserosa. We show that ablation of the amnioserosa leads to clear defects in dorsal closure and, thus, directly demonstrate a role for the amnioserosa in dorsal closure. We also show that DJNK (Drosophila Jun N-terminal kinase) signaling, an epidermal trigger of closure, is unaffected by amnioserosal ablation. These data, together with our demonstration that amnioserosal ablated and Dpp signaling mutant embryos exhibit shared loss-of-function phenotypes, point to a requirement for the amnioserosa in dorsal closure that is downstream of Dpp, perhaps as part of a paracrine response to this signaling cascade.
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pubmed:grant | |
pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/JNK Mitogen-Activated Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Ricin,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase,
http://linkedlifedata.com/resource/pubmed/chemical/dpp protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1058-8388
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pubmed:author | |
pubmed:copyrightInfo |
Copyright (c) 2005 Wiley-Liss, Inc.
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pubmed:issnType |
Print
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pubmed:volume |
232
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
791-800
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15704109-Amnion,
pubmed-meshheading:15704109-Animals,
pubmed-meshheading:15704109-Animals, Genetically Modified,
pubmed-meshheading:15704109-Body Patterning,
pubmed-meshheading:15704109-Cell Movement,
pubmed-meshheading:15704109-Cell Shape,
pubmed-meshheading:15704109-Drosophila,
pubmed-meshheading:15704109-Drosophila Proteins,
pubmed-meshheading:15704109-Embryo, Nonmammalian,
pubmed-meshheading:15704109-Epidermis,
pubmed-meshheading:15704109-Gene Expression Regulation, Developmental,
pubmed-meshheading:15704109-Genes, Reporter,
pubmed-meshheading:15704109-Green Fluorescent Proteins,
pubmed-meshheading:15704109-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:15704109-Models, Biological,
pubmed-meshheading:15704109-Mutation,
pubmed-meshheading:15704109-Ricin,
pubmed-meshheading:15704109-Signal Transduction,
pubmed-meshheading:15704109-Transcription, Genetic,
pubmed-meshheading:15704109-Transgenes,
pubmed-meshheading:15704109-beta-Galactosidase
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pubmed:year |
2005
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pubmed:articleTitle |
Amnioserosa is required for dorsal closure in Drosophila.
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pubmed:affiliation |
Department of Human Genetics, Eccles Institute of Human Genetics, University of Utah, Salt Lake City, Utah 84112, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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