Author: Aravinth Kumar Jayabalan; Diane E. Griffin; Anthony K. L. Leung
Title: Alphavirus nsP3 ADP-ribosylhydrolase Activity Disrupts Stress Granule Formation Document date: 2019_6_20
ID: n8sjpcbs_3
Snippet: Recently, we and others have reported that the viral MD possesses enzymatic activity for removal of single ADP-ribose groups, and possibly PAR, from ADP-ribosylated proteins [38, [45] [46] [47] . Given that the structural integrity of SGs is dependent on ADP-ribosylation [19] , we hypothesized, and identified, that the MD ADP-ribosylhydrolase activity is required for suppressing the formation of SGs induced by stress, with G3BP1 as one of the tar.....
Document: Recently, we and others have reported that the viral MD possesses enzymatic activity for removal of single ADP-ribose groups, and possibly PAR, from ADP-ribosylated proteins [38, [45] [46] [47] . Given that the structural integrity of SGs is dependent on ADP-ribosylation [19] , we hypothesized, and identified, that the MD ADP-ribosylhydrolase activity is required for suppressing the formation of SGs induced by stress, with G3BP1 as one of the target substrates. This enzymatic activity is required for alteration of SG composition by releasing translation factors from a condensated state in nsP3-expressing cells.
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