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Vol. 17, No. 4, pp. 455-460, February 15, 2003
1 Department of Molecular and Experimental Medicine, The
Scripps Research Institute, La Jolla, California 92037, USA;
2 Division of Hematology/Oncology, University of California at
Los Angeles, School of Medicine, Los Angeles, California 90095, USA
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-
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.
[Keywords: ISG15; UBP43; knockout; interferon; STAT; JAK]
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