| pubmed-article:17335807 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17335807 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:17335807 | lifeskim:mentions | umls-concept:C0071253 | lld:lifeskim |
| pubmed-article:17335807 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
| pubmed-article:17335807 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
| pubmed-article:17335807 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
| pubmed-article:17335807 | lifeskim:mentions | umls-concept:C0205219 | lld:lifeskim |
| pubmed-article:17335807 | lifeskim:mentions | umls-concept:C0032200 | lld:lifeskim |
| pubmed-article:17335807 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
| pubmed-article:17335807 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
| pubmed-article:17335807 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:17335807 | lifeskim:mentions | umls-concept:C0596963 | lld:lifeskim |
| pubmed-article:17335807 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:17335807 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:17335807 | pubmed:dateCreated | 2007-3-23 | lld:pubmed |
| pubmed-article:17335807 | pubmed:abstractText | Cancer cells depend on chemotaxis for invasion and frequently overexpress and/or activate Src. We previously reported that v-Src accelerates motility by promoting phosphoinositide 3-kinase (PI3-K) signalling but abrogates chemotaxis. We here addressed the mechanism of the loss of chemotactic response to platelet-derived growth factor (PDGF) gradients in fibroblasts harbouring a thermosensitive v-Src kinase. At non-permissive temperature, PDGF receptor (PDGFR) signalling, assessed by phosphoY(751)-specific antibodies (a docking site for PI3-K), was not detected without PDGF and showed a concentration-dependent PDGF response. Both immunolabeling of PI3-K (p110) and live cell imaging of its product (phosphatidylinositol 3,4,5 tris-phosphate) showed PI3-K recruitment and activation at lamellipodia polarized towards a PDGF gradient. Centrosomes and PDGFR- and Src-bearing endosomes were also oriented towards this gradient. Upon v-Src thermoactivation, (i) Y(751) phosphorylation was moderately induced without PDGF and synergistically increased with PDGF; (ii) PI3-K was recruited and activated all along the plasma membrane without PDGF and did not polarize in response to a PDGF gradient; and (iii) polarization of centrosomes and of PDGFR-bearing endosomes were also abrogated. Thus, PDGF can further increase PDGFR auto-phosphorylation despite strong Src kinase activity, but diffuse downstream activation of PI3-K by Src abrogates cell polarization and chemotaxis: "signalling requires silence". | lld:pubmed |
| pubmed-article:17335807 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17335807 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335807 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17335807 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17335807 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335807 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17335807 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17335807 | pubmed:issn | 0014-4827 | lld:pubmed |
| pubmed-article:17335807 | pubmed:author | pubmed-author:SaxS ASA | lld:pubmed |
| pubmed-article:17335807 | pubmed:author | pubmed-author:MettlenMarcel... | lld:pubmed |
| pubmed-article:17335807 | pubmed:author | pubmed-author:PlatekAnnaA | lld:pubmed |
| pubmed-article:17335807 | pubmed:author | pubmed-author:CourtoyPierre... | lld:pubmed |
| pubmed-article:17335807 | pubmed:author | pubmed-author:de... | lld:pubmed |
| pubmed-article:17335807 | pubmed:author | pubmed-author:TytecaDonatie... | lld:pubmed |
| pubmed-article:17335807 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17335807 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:17335807 | pubmed:volume | 313 | lld:pubmed |
| pubmed-article:17335807 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17335807 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17335807 | pubmed:pagination | 1090-105 | lld:pubmed |
| pubmed-article:17335807 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:17335807 | pubmed:meshHeading | pubmed-meshheading:17335807... | lld:pubmed |
| pubmed-article:17335807 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17335807 | pubmed:articleTitle | Constitutive diffuse activation of phosphoinositide 3-kinase at the plasma membrane by v-Src suppresses the chemotactic response to PDGF by abrogating the polarity of PDGF receptor signalling. | lld:pubmed |
| pubmed-article:17335807 | pubmed:affiliation | Université catholique de Louvain, Christian de Duve Institute of Cellular Pathology, CELL Unit, UCL 75.41, avenue Hippocrate, 75, B-1200 Brussels, Belgium. | lld:pubmed |
| pubmed-article:17335807 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17335807 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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