About: Alphavirus nsP3 ADP-ribosylhydrolase Activity Disrupts Stress Granule Formation

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Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Alphavirus nsP3 ADP-ribosylhydrolase Activity Disrupts Stress Granule Formation
Creator	Griffin, Diane Leung, Anthony Kumar, Aravinth
Source	BioRxiv; MedRxiv
abstract	Formation of stress granules (SGs), cytoplasmic condensates of stalled translation initiation complexes, is regulated by post-translational protein modification. Alphaviruses interfere with SG formation in response to inhibition of host protein synthesis through the activities of nonstructural protein 3 (nsP3). nsP3 has a conserved N-terminal macrodomain that binds and can remove ADP-ribose from ADP-ribosylated proteins and a C-terminal hypervariable domain that binds essential SG component G3BP1. We showed that the hydrolase activity of chikungunya virus nsP3 macrodomain removed ADP-ribosylation of G3BP1 and suppressed SG formation. ADP-ribosylhydrolase-deficient nsP3 mutants allowed stress-induced cytoplasmic condensation of translation initiation factors. nsP3 also disassembled SG-like aggregates enriched with translation initiation factors that are induced by the expression of FUS mutant R495X linked to amyotrophic lateral sclerosis. Therefore, our data indicate that regulation of ADP-ribosylation controls the localization of translation initiation factors during virus infection and other pathological conditions.
has issue date	2019-06-20(xsd:dateTime)
bibo:doi	10.1101/629881
has license	biorxiv
sha1sum (hex)	00e490bccc20b370f5d9334b722ef405d53c5eda
schema:url	https://doi.org/10.1101/629881
resource representing a document's title	Alphavirus nsP3 ADP-ribosylhydrolase Activity Disrupts Stress Granule Formation
schema:publication	bioRxiv
resource representing a document's body	covid:00e490bccc20b370f5d9334b722ef405d53c5eda#body_text
is schema:about of	named entity 'G3BP1' named entity 'PROTEINS' named entity 'binds' named entity 'complexes' named entity 'initiation' named entity 'Granule' named entity 'protein synthesis' named entity 'Stress Granule' named entity 'nsP3' named entity 'chikungunya virus' named entity 'stress granule' named entity 'nsP3' named entity 'endoplasmic reticulum' named entity 'FUS' named entity 'eIF3b' named entity 'GFP' named entity 'nsP3' named entity 'ADP' named entity 'G3BP1' named entity 'nsP3' named entity 'pathological conditions' named entity 'frontotemporal dementia' named entity 'TIA1' named entity 'viruses' named entity 'pharmacological' named entity 'ADP-ribosylation' named entity 'molecular weight' named entity 'G3BP' named entity 'G3BP1' named entity 'infection' named entity 'ALS' named entity 'thapsigargin' named entity 'nsP3' named entity 'pathogenesis' named entity 'neddylation' named entity 'arsenite' named entity 'C-terminal' named entity 'PARG' named entity 'G3BP1' named entity 'ADP' named entity 'hydrolysis' named entity 'mitochondrial' named entity 'wild-type' named entity 'transfection' named entity 'nsP3' named entity 'RNA-binding proteins' named entity 'physiological' named entity 'mosquito' named entity 'eIF3b' named entity 'nsP3' named entity 'mitochondrial' named entity 'eIF3b' named entity 'nsP3' named entity 'enzymatic activity' named entity 'lysed' named entity 'transfection' named entity 'SDS-PAGE' named entity 'transfection' named entity 'paralog' named entity 'infection' named entity 'clotrimazole' named entity 'G3BP1' named entity 'neurotoxicity' named entity 'proximal' named entity 'viral protein' named entity 'dynamic equilibrium' named entity 'nsP3' named entity 'G3BP1' named entity 'nsP3' named entity 'lysates' named entity 'amyotrophic lateral sclerosis' named entity 'infection' named entity 'transfected' named entity 'methanol' named entity 'eIF3b' named entity 'protein expression' named entity 'N-terminal' named entity 'nsP3' named entity 'C-terminal' named entity 'transfected' named entity 'Precipitates' named entity 'eIF3b'

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