Identification and Herc5-mediated ISGylation of novel target proteins.

Article Details

Citation

Takeuchi T, Inoue S, Yokosawa H

Identification and Herc5-mediated ISGylation of novel target proteins.

Biochem Biophys Res Commun. 2006 Sep 22;348(2):473-7. Epub 2006 Jul 28.

PubMed ID
16884686 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Serine/threonine-protein kinase 38Q15208Details