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Identification and Herc5-mediated ISGylation of novel target proteins
| Title: | Identification and Herc5-mediated ISGylation of novel target proteins |
| Authors: | Takeuchi, Tomoharu Browse this author | | Inoue, Satoshi Browse this author | | Yokosawa, Hideyoshi Browse this author |
| Keywords: | ISG15 | | Interferon | | Ubiquitin | | Herc5 |
| Issue Date: | 22-Sep-2006 |
| Publisher: | Elsevier Inc. |
| Journal Title: | Biochemical and Biophysical Research Communications |
| Volume: | 348 |
| Issue: | 2 |
| Start Page: | 473 |
| End Page: | 477 |
| Publisher DOI: | 10.1016/j.bbrc.2006.07.076 |
| PMID: | 16884686 |
| Abstract: | ISG15, a protein containing two ubiquitin-like domains, is an interferon-stimulated gene product that functions in antiviral response and is conjugated to various cellular proteins (ISGylation) upon interferon stimulation. ISGylation occurs via a pathway similar to the pathway for ubiquitination that requires the sequential action of E1/E2/E3: the E1 (UBE1L), E2 (UbcH8), and E3 (Efp/Herc5) enzymes for ISGylation have been hitherto identified. In this study, we identified six novel candidate target proteins for ISGylation by a proteomic approach. Four candidate target proteins were demonstrated to be ISGylated in UBE1L- and UbcH8-dependent manners, and ISGylation of the respective target proteins was stimulated by Herc5. In addition, Herc5 was capable of binding with the respective target proteins. Thus, these results suggest that Herc5 functions as a general E3 ligase for protein ISGylation. |
| Relation: | http://www.sciencedirect.com/science/journal/0006291X |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/14737 |
| Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 横沢 英良
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