| pubmed-article:19000756 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19000756 | lifeskim:mentions | umls-concept:C0258823 | lld:lifeskim |
| pubmed-article:19000756 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:19000756 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:19000756 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:19000756 | pubmed:dateCreated | 2008-12-23 | lld:pubmed |
| pubmed-article:19000756 | pubmed:abstractText | EVL-I is a splice variant of EVL (Ena/VASP like protein), whose in vivo function and regulation are still poorly understood. We found that Protein Kinase D (PKD) interacts in vitro and in vivo with EVL-I and phosphorylates EVL-I in a 21 amino acid alternately-included insert in the EVH2 domain. Following knockdown of the capping protein CPbeta and spreading on laminin, phosphorylated EVL-I can support filopodia formation and the phosphorylated EVL-I is localized at filopodial tips. Furthermore, we found that the lamellipodial localization of EVL-I is unaffected by phosphorylation, but that impairment of EVL-I phosphorylation is associated with ruffling of lamellipodia upon PDBu stimulation. Besides the lamellipodial and filopodial localization of phosphorylated EVL-I in fibroblasts, we determined that EVL-I is hyperphosphorylated and localized in the cell-cell contacts of certain breast cancer cells and mouse embryo keratinocytes. Taken together, our results show that phosphorylated EVL-I is present in lamellipodia, filopodia and cell-cell contacts and suggest the existence of signaling pathways that may affect EVL-I via phosphorylation of its EVH2 domain. | lld:pubmed |
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| pubmed-article:19000756 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19000756 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19000756 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19000756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19000756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19000756 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19000756 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:19000756 | pubmed:issn | 1873-3913 | lld:pubmed |
| pubmed-article:19000756 | pubmed:author | pubmed-author:GertlerFrankF | lld:pubmed |
| pubmed-article:19000756 | pubmed:author | pubmed-author:VandenheedeJa... | lld:pubmed |
| pubmed-article:19000756 | pubmed:author | pubmed-author:Van... | lld:pubmed |
| pubmed-article:19000756 | pubmed:author | pubmed-author:JanssensKatri... | lld:pubmed |
| pubmed-article:19000756 | pubmed:author | pubmed-author:De KimpeLineL | lld:pubmed |
| pubmed-article:19000756 | pubmed:author | pubmed-author:VandoninckSan... | lld:pubmed |
| pubmed-article:19000756 | pubmed:author | pubmed-author:BalsamoMichel... | lld:pubmed |
| pubmed-article:19000756 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19000756 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:19000756 | pubmed:owner | NLM | lld:pubmed |
