pubmed-article:17538019 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17538019 | lifeskim:mentions | umls-concept:C0027215 | lld:lifeskim |
pubmed-article:17538019 | lifeskim:mentions | umls-concept:C0001511 | lld:lifeskim |
pubmed-article:17538019 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
pubmed-article:17538019 | lifeskim:mentions | umls-concept:C0061187 | lld:lifeskim |
pubmed-article:17538019 | lifeskim:mentions | umls-concept:C0808080 | lld:lifeskim |
pubmed-article:17538019 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:17538019 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
pubmed-article:17538019 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
pubmed-article:17538019 | lifeskim:mentions | umls-concept:C1705922 | lld:lifeskim |
pubmed-article:17538019 | lifeskim:mentions | umls-concept:C0205144 | lld:lifeskim |
pubmed-article:17538019 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:17538019 | pubmed:dateCreated | 2007-7-26 | lld:pubmed |
pubmed-article:17538019 | pubmed:abstractText | Phosphoinositides regulate several actin-binding proteins but their role at intercellular adhesions has not been defined. We found that phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) was generated at sites of N-cadherin-mediated intercellular adhesion and was a critical regulator of intercellular adhesion strength. Immunostaining for PI(4,5)P2 or transfection with GFP-PH-PLCdelta showed that PI(4,5)P2 was enriched at sites of N-cadherin adhesions and this enrichment required activated Rac1. Isoform-specific immunostaining for type I phosphatidylinositol 4-phosphate 5 kinase (PIP5KI) showed that PIP5KIgamma was spatially associated with N-cadherin-Fc beads. Association of PIP5KIgamma with N-cadherin adhesions was in part dependent on the activation of RhoA. Transfection with catalytically inactive PIP5KIgamma blocked the enrichment of PI(4,5)P2 around beads. Catalytically inactive PIP5KIgamma or a cell-permeant peptide that mimics and competes for the PI(4,5)P2-binding region of the actin-binding protein gelsolin inhibited incorporation of actin monomers in response to N-cadherin ligation and reduced intercellular adhesion strength by more than twofold. Gelsolin null fibroblasts transfected with a gelsolin severing mutant containing an intact PI(4,5)P2 binding region, demonstrated intercellular adhesion strength similar to wild-type transfected controls. We conclude that PIP5KIgamma-mediated generation of PI(4,5)P2 at sites of N-cadherin contacts regulates intercellular adhesion strength, an effect due in part to PI(4,5)P2-mediated regulation of gelsolin. | lld:pubmed |
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pubmed-article:17538019 | pubmed:language | eng | lld:pubmed |
pubmed-article:17538019 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17538019 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17538019 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17538019 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:17538019 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17538019 | pubmed:month | Aug | lld:pubmed |
pubmed-article:17538019 | pubmed:issn | 1059-1524 | lld:pubmed |
pubmed-article:17538019 | pubmed:author | pubmed-author:AndersonR ARA | lld:pubmed |
pubmed-article:17538019 | pubmed:author | pubmed-author:LinkGG | lld:pubmed |
pubmed-article:17538019 | pubmed:author | pubmed-author:LaschingerCC | lld:pubmed |
pubmed-article:17538019 | pubmed:author | pubmed-author:JanmeyP APA | lld:pubmed |
pubmed-article:17538019 | pubmed:author | pubmed-author:McCullochC... | lld:pubmed |
pubmed-article:17538019 | pubmed:author | pubmed-author:AroraP DPD | lld:pubmed |
pubmed-article:17538019 | pubmed:author | pubmed-author:El SayeghT... | lld:pubmed |
pubmed-article:17538019 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17538019 | pubmed:volume | 18 | lld:pubmed |
pubmed-article:17538019 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17538019 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17538019 | pubmed:pagination | 3026-38 | lld:pubmed |
pubmed-article:17538019 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:17538019 | pubmed:meshHeading | pubmed-meshheading:17538019... | lld:pubmed |
pubmed-article:17538019 | pubmed:meshHeading | pubmed-meshheading:17538019... | lld:pubmed |
pubmed-article:17538019 | pubmed:meshHeading | pubmed-meshheading:17538019... | lld:pubmed |
pubmed-article:17538019 | pubmed:meshHeading | pubmed-meshheading:17538019... | lld:pubmed |