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http://purl.uniprot.org/citations/12670870http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12670870http://www.w3.org/2000/01/rdf-schema#comment"Integrin-mediated cell-matrix interactions are essential for development, tissue homeostasis, and repair. Upon ligand binding, integrins are recruited into focal adhesions (FAs). Integrin-linked kinase (ILK) is an FA component that interacts with the cytoplasmic domains of integrins, recruits adaptor proteins that link integrins to the actin cytoskeleton, and phosphorylates the serine/threonine kinases PKB/Akt and GSK-3beta. Here we show that mice lacking ILK expression die at the peri-implantation stage because they fail to polarize their epiblast and to cavitate. The impaired epiblast polarization is associated with abnormal F-actin accumulation at sites of integrin attachments to the basement membrane (BM) zone. Likewise, ILK-deficient fibroblasts showed abnormal F-actin aggregates associated with impaired cell spreading and delayed formation of stress fibers and FAs. Finally, ILK-deficient fibroblasts have diminished proliferation rates. However, insulin or PDGF treatment did not impair phosphorylation of PKB/Akt and GSK-3beta, indicating that the proliferation defect is not due to absent or reduced ILK-mediated phosphorylation of these substrates in vivo. Furthermore, expression of a mutant ILK lacking kinase activity and/or paxillin binding in ILK-deficient fibroblasts can rescue cell spreading, F-actin organization, FA formation, and proliferation. Altogether these data show that mammalian ILK modulates actin rearrangements at integrin-adhesion sites."xsd:string
http://purl.uniprot.org/citations/12670870http://purl.org/dc/terms/identifier"doi:10.1101/gad.255603"xsd:string
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/author"Li S."xsd:string
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/author"Sakai K."xsd:string
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/author"Pfeifer A."xsd:string
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/author"Sakai T."xsd:string
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/author"Braun A."xsd:string
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/author"Yurchenco P.D."xsd:string
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/author"Fassler R."xsd:string
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/author"Kostka G."xsd:string
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/author"Docheva D."xsd:string
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/author"Grashoff C."xsd:string
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/name"Genes Dev"xsd:string
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/pages"926-940"xsd:string
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/title"Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation."xsd:string
http://purl.uniprot.org/citations/12670870http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/12670870http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12670870
http://purl.uniprot.org/citations/12670870http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12670870
http://purl.uniprot.org/uniprot/O55222#attribution-B10C06EAD46A9FBDAD7ADBCF2BDD300Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12670870
http://purl.uniprot.org/uniprot/Q61739#attribution-3931D2A4B8594E87396E53CE78513393http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12670870
http://purl.uniprot.org/uniprot/P09055#attribution-3931D2A4B8594E87396E53CE78513393http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12670870
http://purl.uniprot.org/uniprot/#_A0A0A0MQJ3-mappedCitation-12670870http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12670870
http://purl.uniprot.org/uniprot/#_A0A1B0GR42-mappedCitation-12670870http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12670870