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rdf:type |
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lifeskim:mentions |
umls-concept:C0010853,
umls-concept:C0013138,
umls-concept:C0026559,
umls-concept:C0035820,
umls-concept:C0037083,
umls-concept:C0040690,
umls-concept:C0851285,
umls-concept:C1150587,
umls-concept:C1367731,
umls-concept:C1551336,
umls-concept:C1705632,
umls-concept:C1707310,
umls-concept:C1710082
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pubmed:dateCreated |
1999-7-19
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pubmed:abstractText |
During Drosophila embryogenesis the two halves of the lateral epidermis migrate dorsally over a surface of flattened cells, the amnioserosa, and meet at the dorsal midline in order to form the continuous sheet of the larval epidermis. During this process of epithelial migration, known as dorsal closure, signaling from a Jun-amino-terminal-kinase cascade causes the production of the secreted transforming-growth-factor-beta-like ligand, Decapentaplegic. Binding of Decapentaplegic to the putative transforming-growth-factor-beta-like receptors Thickveins and Punt activates a transforming-growth-factor-beta-like pathway that is also required for dorsal closure. Mutations in genes involved in either the Jun-amino-terminal-kinase cascade or the transforming-growth-factor-beta-like signaling pathway can disrupt dorsal closure. Our findings show that although these pathways are linked they are not equivalent in function. Signaling by the Jun-amino-terminal-kinase cascade may be initiated by the small Ras-like GTPase Drac1 and acts to assemble the cytoskeleton and specify the identity of the first row of cells of the epidermis prior to the onset of dorsal closure. Signaling in the transforming-growth-factor-beta-like pathway is mediated by Dcdc42, and acts during the closure process to control the mechanics of the migration process, most likely via its putative effector kinase DPAK.
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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/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Cdc42 protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/JNK Mitogen-Activated Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Rac1 protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta,
http://linkedlifedata.com/resource/pubmed/chemical/rac GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/tkv protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9533
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
112 ( Pt 8)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1225-35
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10085257-Animals,
pubmed-meshheading:10085257-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:10085257-Cytoskeleton,
pubmed-meshheading:10085257-Drosophila Proteins,
pubmed-meshheading:10085257-Drosophila melanogaster,
pubmed-meshheading:10085257-Epidermis,
pubmed-meshheading:10085257-GTP-Binding Proteins,
pubmed-meshheading:10085257-Immunohistochemistry,
pubmed-meshheading:10085257-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:10085257-Microscopy, Confocal,
pubmed-meshheading:10085257-Microscopy, Fluorescence,
pubmed-meshheading:10085257-Mitogen-Activated Protein Kinases,
pubmed-meshheading:10085257-Models, Genetic,
pubmed-meshheading:10085257-Morphogenesis,
pubmed-meshheading:10085257-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10085257-Receptors, Cell Surface,
pubmed-meshheading:10085257-Signal Transduction,
pubmed-meshheading:10085257-Transforming Growth Factor beta,
pubmed-meshheading:10085257-Transgenes,
pubmed-meshheading:10085257-rac GTP-Binding Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
Dcdc42 acts in TGF-beta signaling during Drosophila morphogenesis: distinct roles for the Drac1/JNK and Dcdc42/TGF-beta cascades in cytoskeletal regulation.
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pubmed:affiliation |
Drosophila Neurobiology Laboratory and Glaxo-IMCB Group, Institute of Molecular and Cell Biology, Singapore 117609, Republic of Singapore.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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