| http://purl.uniprot.org/citations/32614325 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/32614325 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/32614325 | http://www.w3.org/2000/01/rdf-schema#comment | "Ubiquitin ligases (E3s) embedded in the endoplasmic reticulum (ER) membrane regulate essential cellular activities including protein quality control, calcium flux, and sterol homeostasis. At least 25 different, transmembrane domain (TMD)-containing E3s are predicted to be ER-localised, but for most their organisation and cellular roles remain poorly defined. Using a comparative proteomic workflow, we mapped over 450 protein-protein interactions for 21 stably expressed, full-length E3s. Bioinformatic analysis linked ER-E3s and their interactors to multiple homeostatic, regulatory, and metabolic pathways. Among these were four membrane-embedded interactors of RNF26, a polytopic E3 whose abundance is auto-regulated by ubiquitin-proteasome dependent degradation. RNF26 co-assembles with TMEM43, ENDOD1, TMEM33 and TMED1 to form a complex capable of modulating innate immune signalling through the cGAS-STING pathway. This RNF26 complex represents a new modulatory axis of STING and innate immune signalling at the ER membrane. Collectively, these data reveal the broad scope of regulation and differential functionalities mediated by ER-E3s for both membrane-tethered and cytoplasmic processes."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.org/dc/terms/identifier | "doi:10.7554/elife.57306"xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.org/dc/terms/identifier | "doi:10.7554/elife.57306"xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Fischer R."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Fischer R."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Paton J.C."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Paton J.C."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Kessler B.M."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Kessler B.M."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Paton A.W."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Paton A.W."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Charles P.D."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Charles P.D."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Bagola K."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Bagola K."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Christianson J.C."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Christianson J.C."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Gyrd-Hansen M."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Gyrd-Hansen M."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Fenech E.J."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Fenech E.J."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Laetitia-Thezenas M."xsd:string |
| http://purl.uniprot.org/citations/32614325 | http://purl.uniprot.org/core/author | "Laetitia-Thezenas M."xsd:string |