The GOLD domain-containing protein TMED7 inhibits TLR4 signalling from the endosome upon LPS stimulation
dc.contributor.author | Doyle, SL | |
dc.contributor.author | Husebye, Harald | |
dc.contributor.author | Connolly, D | |
dc.contributor.author | Espevik, Terje | |
dc.contributor.author | O'Neill, LAJ | |
dc.contributor.author | McGettrick, AF | |
dc.date.accessioned | 2019-10-14T07:29:41Z | |
dc.date.available | 2019-10-14T07:29:41Z | |
dc.date.created | 2012-06-04T14:08:11Z | |
dc.date.issued | 2012 | |
dc.identifier.citation | Nature Communications. 2012, 3 . | nb_NO |
dc.identifier.issn | 2041-1723 | |
dc.identifier.uri | http://hdl.handle.net/11250/2621831 | |
dc.description.abstract | Toll-like receptor 4 is an innate immune receptor responsible for the recognition of the Gram-negative cell wall component lipopolysaccharide. Here we show that transmembrane emp24 domain-containing protein 7 (TMED7) inhibits MyD88-independent toll-like receptor 4 signalling. TMED7 overexpression inhibits the ability of TRAM, an adaptor utilized by toll-like receptor 4, or lipopolysaccharide to activate the interferon regulatory factor 3-signalling pathway, whereas TMED7 knockdown enhances production of the cytokine, RANTES, following lipopolysaccharide stimulation. Upon lipopolysaccharide stimulation, TMED7 co-localizes with TRAM and toll-like receptor 4 in late endosomes where it encounters the negative regulator of TRAM, TAG. The TMED7 sequence is found in TAG because of a read-through from the tmed7 gene into the ticam2 gene. TMED7 is essential for TAG-mediated disruption of the TRAM/TRIF complex and the degradation of toll-like receptor 4. A TMED homologue, logjam, has a negative role in the Toll and IMD pathways in Drosophila melanogaster; therefore, TMEDs may have a conserved role in the regulation of innate immunity. | nb_NO |
dc.language.iso | eng | nb_NO |
dc.publisher | Nature Research | nb_NO |
dc.title | The GOLD domain-containing protein TMED7 inhibits TLR4 signalling from the endosome upon LPS stimulation | nb_NO |
dc.type | Journal article | nb_NO |
dc.type | Peer reviewed | nb_NO |
dc.description.version | publishedVersion | nb_NO |
dc.source.pagenumber | 11 | nb_NO |
dc.source.volume | 3 | nb_NO |
dc.source.journal | Nature Communications | nb_NO |
dc.identifier.doi | 10.1038/ncomms1706 | |
dc.identifier.cristin | 927697 | |
dc.description.localcode | Open Access | nb_NO |
cristin.unitcode | 194,65,15,0 | |
cristin.unitname | Institutt for klinisk og molekylær medisin | |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.qualitycode | 2 |