Identification and Herc5-mediated ISGylation of novel target proteins

Takeuchi, Tomoharu; Inoue, Satoshi; Yokosawa, Hideyoshi

Biochemical and Biophysical Research Communications, 2006, 348(2), 473-477

Permalink : https://hdl.handle.net/2115/14737

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アクセス権
open access
URI
https://hdl.handle.net/2115/14737
タイトル
Identification and Herc5-mediated ISGylation of novel target proteins
著者
Takeuchi, Tomoharu ; Inoue, Satoshi ; Yokosawa, Hideyoshi
著者名
Takeuchi, Tomoharu
著者名
Inoue, Satoshi
著者名
Yokosawa, Hideyoshi
言語
英語
キーワード
ISG15
Interferon
Ubiquitin
Herc5
発行日
2006-09-22
出版者
Elsevier Inc.
収録物名
Biochemical and Biophysical Research Communications
巻(号)
348(2)
ページ
473-477
抄録
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.
資源タイプ
学術雑誌論文
出版タイプ
Accepted Manuscript
PISSN
0006-291X
EISSN
1090-2104
関連情報
PMID
16884686
URI
http://www.sciencedirect.com/science/journal/0006291X
関連情報 (isVersionOf)
出版社版DOI
https://doi.org/10.1016/j.bbrc.2006.07.076