Author: Swatek, Kirby N.; Aumayr, Martina; Pruneda, Jonathan N.; Visser, Linda J.; Berryman, Stephen; Kueck, Anja F.; Geurink, Paul P.; Ovaa, Huib; van Kuppeveld, Frank J. M.; Tuthill, Tobias J.; Skern, Tim; Komander, David
Title: Irreversible inactivation of ISG15 by a viral leader protease enables alternative infection detection strategies Document date: 2018_3_6
ID: 3s86w4iw_4
Snippet: Ubiquitination is a key signaling mechanism used by cells to detect and respond to viral infection (8) . Various ubiquitin signals play important roles during the activation of transcriptional programs, such as the NF-κB and IFN response (8, 9) . With the initiation of IFN signaling, the products of roughly 300 IFN stimulated genes (ISGs) mount an antiviral response (10) . Among the ISGs are the ubiquitin-like modifier ISG15 and its assembly mac.....
Document: Ubiquitination is a key signaling mechanism used by cells to detect and respond to viral infection (8) . Various ubiquitin signals play important roles during the activation of transcriptional programs, such as the NF-κB and IFN response (8, 9) . With the initiation of IFN signaling, the products of roughly 300 IFN stimulated genes (ISGs) mount an antiviral response (10) . Among the ISGs are the ubiquitin-like modifier ISG15 and its assembly machinery consisting of UBE1L, UBE2L6/UbcH8, and the HECT E3 ligase HERC5 (11) . ISG15 comprises two ubiquitin fold domains in tandem [an N-terminal ubiquitin-like domain (NTD) and a C-terminal ubiquitin-like domain (CTD)], and like ubiquitin, it is attached to Lys residues on target proteins via its C-terminal Gly-Gly (Gly156-Gly157) motif. Cotranslational attachment of ISG15 to viral capsid proteins inhibits virus assembly (12) , and additional intra-and extracellular roles of ISG15 are also emerging (13, 14) . Together, ubiquitin and ubiquitin-like modifications regulate most antiviral signaling cascades.
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