Interferon-inducible ubiquitin E2, Ubc8, is a conjugating enzyme for protein ISGylation
- Authors
- Kim KI; Giannakopoulos NV; Virgin HW; Zhang DE
- Issue Date
- Nov-2004
- Publisher
- AMER SOC MICROBIOLOGY
- Citation
- MOLECULAR AND CELLULAR BIOLOGY, v.24, no.21, pp 9592 - 9600
- Pages
- 9
- Journal Title
- MOLECULAR AND CELLULAR BIOLOGY
- Volume
- 24
- Number
- 21
- Start Page
- 9592
- End Page
- 9600
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/148880
- DOI
- 10.1128/MCB.24.21.9592-9600.2004
- ISSN
- 0270-7306
1098-5549
- Abstract
- Protein ISGylation is unique among ubiquitin-like conjugation systems in that the expression and conjugation processes are induced by specific stimuli, mainly via the alpha/beta interferon signaling pathway. It has been suggested that protein ISGylation plays a special role in the immune response, because of its interferonsignal dependency and its appearance only in higher eukaryotic organisms. Here, we report the identification of an ISG15-conjugating enzyme, Ubc8. Like other components of the protein ISGylation system (ISG15, UBE1L, and UBP43), Ubc8 is an interferon-inducible protein. Ubc8 clearly mediates protein ISGylation in transfection assays. The reduction of Ubc8 expression by small interfering RNA causes a decrease in protein ISGylation in HeLa cells upon interferon treatment. Neither UbcH7/UbcM4, the closest homologue of Ubc8 among known ubiquitin E2s, nor the small ubiquitin-like modifier E2 Ubc9 supports protein ISGylation. These findings strongly suggest that Ubc8 is a major ISG15-conjugating enzyme responsible for protein ISGylation upon interferon stimulation. Furthermore, we established an assay system to detect ISGylated target proteins by cotransfection of ISG15, UBE1L, and Ubc8 together with a target protein to be analyzed. This method provides an easy and effective way to identify new target
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