| http://purl.uniprot.org/citations/24789099 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24789099 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24789099 | http://www.w3.org/2000/01/rdf-schema#comment | "The chemokine domain of fractalkine (FKN-CD) binds to the classical RGD-binding site of αvβ3 and that the resulting ternary complex formation (integrin-FKN-CX3CR1) is critical for CX3CR1 signaling and FKN-induced integrin activation. However, only certain cell types express CX3CR1. Here we studied if FKN-CD can activate integrins in the absence of CX3CR1. We describe that WT FKN-CD activated recombinant soluble αvβ3 in cell-free conditions, but the integrin-binding defective mutant of FKN-CD (K36E/R37E) did not. This suggests that FKN-CD can activate αvβ3 in the absence of CX3CR1 through the direct binding of FKN-CD to αvβ3. WT FKN-CD activated αvβ3 on CX3CR1-negative cells (K562 and CHO) but K36E/R37E did not, suggesting that FKN-CD can activate integrin at the cellular levels in a manner similar to that in cell-free conditions. We hypothesized that FKN-CD enhances ligand binding to the classical RGD-binding site (site 1) through binding to a second binding site (site 2) that is distinct from site 1 in αvβ3. To identify the possible second FKN-CD binding site we performed docking simulation of αvβ3-FKN-CD interaction using αvβ3 with a closed inactive conformation as a target. The simulation predicted a potential FKN-CD-binding site in inactive αvβ3 (site 2), which is located at a crevice between αv and β3 on the opposite side of site 1 in the αvβ3 headpiece. We studied if FKN-CD really binds to site 2 using a peptide that is predicted to interact with FKN-CD in site 2. Notably the peptide specifically bound to FKN-CD and effectively suppressed integrin activation by FKN-CD. This suggests that FKN-CD actually binds to site 2, and this leads to integrin activation. We obtained very similar results in α4β1 and α5β1. The FKN binding to site 2 and resulting integrin activation may be a novel mechanism of integrin activation and of FKN signaling."xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0096372"xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0096372"xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/author | "Fujita M."xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/author | "Fujita M."xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/author | "Takada Y."xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/author | "Takada Y."xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/author | "Takada Y.K."xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/author | "Takada Y.K."xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/name | "PLoS ONE"xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/name | "PLoS ONE"xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/pages | "E96372"xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/pages | "E96372"xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/title | "The chemokine fractalkine can activate integrins without CX3CR1 through direct binding to a ligand-binding site distinct from the classical RGD-binding site."xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/title | "The chemokine fractalkine can activate integrins without CX3CR1 through direct binding to a ligand-binding site distinct from the classical RGD-binding site."xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/volume | "9"xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://purl.uniprot.org/core/volume | "9"xsd:string |
| http://purl.uniprot.org/citations/24789099 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24789099 |
| http://purl.uniprot.org/citations/24789099 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24789099 |
| http://purl.uniprot.org/citations/24789099 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/24789099 |
| http://purl.uniprot.org/citations/24789099 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/24789099 |