Ube1L and protein ISGylation are not essential for alpha/beta interferon signaling
- Authors
- Keun Il Kim; Ming Yan; Oxana Malakohva; Luo, Jiann-Kae; Mei-Feng Shen; Weiguo Zou; Juan Carlos de la Torre; Dong-Er Zhang
- Issue Date
- Jan-2006
- Publisher
- American Society for Microbiology
- Citation
- Molecular and Cellular Biology, v.26, no.2, pp 472 - 479
- Pages
- 8
- Journal Title
- Molecular and Cellular Biology
- Volume
- 26
- Number
- 2
- Start Page
- 472
- End Page
- 479
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/15400
- DOI
- 10.1128/MCB.26.2.472-479.2006
- ISSN
- 0270-7306
1098-5549
- Abstract
- The expression of ubiquitin-Iike modifier ISG15 and its conjugation to target proteins are highly induced by interferon (IFN) stimulation and during viral and bacterial infections. However, the biological significance of this modification has not been clearly understood. To investigate the function of protein modification by ISG15, we generated a mouse model deficient in UBE1L, an ISG15-activating enzyme. Ube1L-/- mice did not produce ISG15 conjugates but expressed free ISG15 normally. ISGylation lias been implicated in the reproduction and innate immunity. However, Ube1L-/- mice were fertile and exhibited normal antiviral responses against vesicular stomatitis virus and lymphocytic choriomeningitis virus infection. Our results indicate that UBE1L and protein ISGylation are not critical for IFN-α/β signaling via JAK/STAT activation. Moreover, using Ube1L/Ubp43 double-deficient mice, we showed that lack of UBP43, but not the increase of protein ISGylation, is related to the increased IFN signaling in Ubp43-deficient mice. Copyright © 2006, American Society for Microbiology. All Rights Reserved.
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