| First Author | Malakhova OA | Year | 2003 |
| Journal | Genes Dev | Volume | 17 |
| Issue | 4 | Pages | 455-60 |
| PubMed ID | 12600939 | Mgi Jnum | J:119425 |
| Mgi Id | MGI:3702206 | Doi | 10.1101/gad.1056303 |
| Citation | Malakhova OA, et al. (2003) Protein ISGylation modulates the JAK-STAT signaling pathway. Genes Dev 17(4):455-60 |
| abstractText | ISG15 is one of the most strongly induced genes upon viral infection, type I interferon (IFN) stimulation, and lipopolysaccharide (LPS) stimulation. Here we report that mice lacking UBP43, a protease that removes ISG15 from ISGylated proteins, are hypersensitive to type I IFN. Most importantly, in UBP43-deficient cells, IFN-beta induces a prolonged Stat1 tyrosine phosphorylation, DNA binding, and IFN-mediated gene activation. Furthermore, restoration of ISG15 conjugation in protein ISGylation-defective K562 cells increases IFN-stimulated promoter activity. These findings identify UBP43 as a novel negative regulator of IFN signaling and suggest the involvement of protein ISGylation in the regulation of the JAK-STAT pathway. |
