Source:http://linkedlifedata.com/resource/pubmed/id/16449319
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 4
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pubmed:dateCreated |
2006-2-9
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pubmed:abstractText |
The Drosophila protein kinase Par-1 is expressed throughout Drosophila development, but its function has not been extensively characterized because of oocyte lethality of null mutants. In this report, we have characterized the function of Par-1 in embryonic and post-embryonic epithelia. Par-1 protein is dynamically localized during embryonic cell polarization, transiently restricted to the lateral membrane domain, followed by apicolateral localization. We depleted maternal and zygotic par-1 by RNAi and revealed a requirement for Par-1 in establishing cell polarity. Par-1 restricts the coalescing adherens junction to an apicolateral position and prevents its widespread formation along the lateral domain. Par-1 also promotes the localization of lateral membrane proteins such as Delta. These activities are important for the further development of cell polarity during gastrulation. By contrast, Par-1 is not essential to maintain epithelial polarity once it has been established. However, it still has a maintenance role since overexpression causes severe polarity disruption. Additionally, we find a novel role for Par-1 in Notch signal transduction during embryonic neurogenesis and retina determination. Epistasis analysis indicates that Par-1 functions upstream of Notch and is critical for proper localization of the Notch ligand Delta.
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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/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Par-1 protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Notch,
http://linkedlifedata.com/resource/pubmed/chemical/notch protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9533
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
119
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
711-21
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16449319-Animals,
pubmed-meshheading:16449319-Cell Polarity,
pubmed-meshheading:16449319-Drosophila,
pubmed-meshheading:16449319-Drosophila Proteins,
pubmed-meshheading:16449319-Embryo, Nonmammalian,
pubmed-meshheading:16449319-Ligands,
pubmed-meshheading:16449319-Protein Kinases,
pubmed-meshheading:16449319-Protein-Serine-Threonine Kinases,
pubmed-meshheading:16449319-Receptors, Notch,
pubmed-meshheading:16449319-Retina,
pubmed-meshheading:16449319-Signal Transduction
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pubmed:year |
2006
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pubmed:articleTitle |
Par-1 kinase establishes cell polarity and functions in Notch signaling in the Drosophila embryo.
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pubmed:affiliation |
Department of Biochemistry, Molecular Biology and Cell Biology, 2205 Tech Drive, Northwestern University, Evanston, IL 60208, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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