Source:http://linkedlifedata.com/resource/pubmed/id/16862128
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7102
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pubmed:dateCreated |
2006-8-3
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pubmed:abstractText |
Epithelial tissues maintain a robust architecture during development. This fundamental property relies on intercellular adhesion through the formation of adherens junctions containing E-cadherin molecules. Localization of E-cadherin is stabilized through a pathway involving the recruitment of actin filaments by E-cadherin. Here we identify an additional pathway that organizes actin filaments in the apical junctional region (AJR) where adherens junctions form in embryonic epithelia. This pathway is controlled by Bitesize (Btsz), a synaptotagmin-like protein that is recruited in the AJR independently of E-cadherin and is required for epithelial stability in Drosophila embryos. On loss of btsz, E-cadherin is recruited normally to the AJR, but is not stabilized properly and actin filaments fail to form a stable continuous network. In the absence of E-cadherin, actin filaments are stable for a longer time than they are in btsz mutants. We identify two polarized cues that localize Btsz: phosphatidylinositol (4,5)-bisphosphate, to which Btsz binds; and Par-3. We show that Btsz binds to the Ezrin-Radixin-Moesin protein Moesin, an F-actin-binding protein that is localized apically and is recruited in the AJR in a btsz-dependent manner. Expression of a dominant-negative form of Ezrin that does not bind F-actin phenocopies the loss of btsz. Thus, our data indicate that, through their interaction, Btsz and Moesin may mediate the proper organization of actin in a local domain, which in turn stabilizes E-cadherin. These results provide a mechanism for the spatial order of actin organization underlying junction stabilization in primary embryonic epithelia.
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 4,5-Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptotagmins,
http://linkedlifedata.com/resource/pubmed/chemical/bitesize protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/moesin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1476-4687
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
3
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pubmed:volume |
442
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
580-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16862128-Actins,
pubmed-meshheading:16862128-Adherens Junctions,
pubmed-meshheading:16862128-Animals,
pubmed-meshheading:16862128-Cadherins,
pubmed-meshheading:16862128-Cell Line,
pubmed-meshheading:16862128-Drosophila Proteins,
pubmed-meshheading:16862128-Drosophila melanogaster,
pubmed-meshheading:16862128-Epithelial Cells,
pubmed-meshheading:16862128-Membrane Proteins,
pubmed-meshheading:16862128-Microfilament Proteins,
pubmed-meshheading:16862128-Phosphatidylinositol 4,5-Diphosphate,
pubmed-meshheading:16862128-Protein Binding,
pubmed-meshheading:16862128-RNA Interference,
pubmed-meshheading:16862128-Synaptotagmins
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pubmed:year |
2006
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pubmed:articleTitle |
Spatial control of actin organization at adherens junctions by a synaptotagmin-like protein Btsz.
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pubmed:affiliation |
Institut de Biologie du Développement de Marseille Luminy (IBDML) UMR 6216, CNRS-Université de la Méditerrannée. Campus de Luminy, case 907, 13288 Marseille cedex 09, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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