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Context-dependent and disease-specific diversity in stress granules formed from preexisting protein interactions

ABSTRACT: Affinity-capture proteomics studies using endogenously tagged G3BP1 with APEX2 to capture the stress granule proteome at steady state and upon stress induction. This was done in 293T cells as well as induced pluripotent stem cells differentiated into neuronal progenitor cells.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Eric J. Bennett

PROVIDER: MSV000081554 | MassIVE |

REPOSITORIES: MassIVE

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Context-Dependent and Disease-Specific Diversity in Protein Interactions within Stress Granules.

Markmiller Sebastian S Soltanieh Sahar S Server Kari L KL Mak Raymond R Jin Wenhao W Fang Mark Y MY Luo En-Ching EC Krach Florian F Yang Dejun D Sen Anindya A Fulzele Amit A Wozniak Jacob M JM Gonzalez David J DJ Kankel Mark W MW Gao Fen-Biao FB Bennett Eric J EJ Lécuyer Eric E Yeo Gene W GW

Cell 20180101 3

Stress granules (SGs) are transient ribonucleoprotein (RNP) aggregates that form during cellular stress and are increasingly implicated in human neurodegeneration. To study the proteome and compositional diversity of SGs in different cell types and in the context of neurodegeneration-linked mutations, we used ascorbate peroxidase (APEX) proximity labeling, mass spectrometry, and immunofluorescence to identify ∼150 previously unknown human SG components. A highly integrated, pre-existing SG prote ...[more]

PMID: 29373831

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ECT2 and AURKB Modulate Formation of Stress Granules Containing Transcripts from Diverse Cellular Pathways in Astrocytoma Cells

Project description:Stress granules are small RNA-protein granules that modify the translational landscape during cellular stress to promote survival. The RhoGTPase RhoA is implicated in the formation of RNA stress granules. Our data demonstrate that the cytokinetic proteins ECT2 and AurkB are localized to stress granules in human astrocytoma cells. AurkB and its downstream target histone-3 are phosphorylated during arsenite-induced stress. Chemical (AZD1152-HQPA) and siRNA inhibition of AurkB results in fewer and smaller stress granules when analyzed utilizing high throughput fluorescent based cellomics assays. RNA immunoprecipitation with the known stress granule aggregates TIAR and G3BP1 was performed on astrocytoma cells and subsequent analysis revealed that astrocytoma stress granules harbour unique mRNAs for various cellular pathways including cellular migration, metabolism, translation and transcriptional regulation. Human astrocytoma cell stress granules contain mRNA that are known to be involved in glioma signaling and the mTOR pathway. These data provide evidence that RNA stress granules are a novel form of epigenetic regulation in astrocytoma cells, which may be targetable by chemical inhibitors and enhance astrocytoma susceptiblity to conventional therapy such as radiation and chemotherapy. Astrocytoma cells were either untreated or treated with arsenite to induce stress granule formation and RNA immunoprecipitates were analyzed by exon array analysis. RNA species that were enriched in TIAR RIPs and G3BP1 RIPS, respectively were compared to compared to TIAR and G3BP1 RIPs from untreated cells and input controls. Ingenuity pathway analysis was performed on the stress granule enriched mRNAs from the TIAR and G3BP1 RIPs to identify significant functional biology networks.

2016-02-29 | E-GEOD-76814 | biostudies-arrayexpress

Huntington’s disease mice and human brain tissue exhibit increased G3BP1 granules and TDP43 mislocalization

Project description:We identify cerebrospinal fluid extracellular vesicle miRNAs in Huntington’s Disease that are enriched for targeting G3BP1 and show aberrant G3BP1 granule dynamics in HD mice and human brain tissue.

2021-05-07 | GSE173546 | GEO

Norovirus infection results in assembly of virus-specific G3BP1 granules and evasion of eIF2 apha signaling

Project description:Proteomic analysis of murine stress granule and G3BP1 granulome in infected cells. BV2 GFP-G3BP1 cells were either treated with 0.1 mM arsenite for 1h to induce SG assembly or infected with MNV for 9h. G3BP1 granules were enriched by sequential centrifugation and purified by immunoprecipitation using antibodies to GFP (to trap GFP-G3BP1) or IgG (as a control) followed by pull down with Protein A-conjugated epoxy Dynabeads as previously described. To characterize the identity of G3BP1 partners within these, Mass Spectrometric analysis was performed.

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G3BP2B stress granules regulate mRNA expression under ER stress [Riboseq_Exp3]

Project description:Stress granules (SGs) are macromolecular assemblies that form under cellular stress. Formation of these condensates is driven by the nucleation of proteins such as G3BPs. G3BPs are RNA-binding proteins that condense into SGs following translation shutoff during the integrated stress response (ISR). Three G3BP paralogs (G3BP1, G3BP2A, and G3BP2B) have been identified in vertebrates. However, the contribution of the different G3BP paralogs to stress granule formation and stress-induced gene expression changes are incompletely understood. Here, we identify a molecular tool to study G3BP condensation into SGs by mutating residue V11 of G3BPs. This conserved amino acid potentiates the G3BP-Caprin-1 complex, hence promoting SG assembly. Ribosome profiling revealed that disruption of G3BP condensation impacts mRNA levels and ribosome engagement during the ISR. Moreover, we found that G3BP2B preferentially condenses and promotes changes in mRNA expression under endoplasmic reticulum (ER) stress. Together, this work suggests that stress granule assembly promotes changes in gene expression under cellular stress, which is differentially regulated by G3BP paralogs.

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G3BP2B stress granules regulate mRNA expression under ER stress [Riboseq_Exp2]

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G3BP2B stress granules regulate mRNA expression under ER stress [Riboseq_Exp1]

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G3BP2B stress granules regulate mRNA expression under ER stress [RNAseq_Exp1]

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G3BP2B stress granules regulate mRNA expression under ER stress [RNAseq_Exp3]

Project description:Stress granules (SGs) are macromolecular assemblies that form under cellular stress. Their function is not completely understood. Formation of these organelles is driven by the nucleation of proteins such as G3BPs. G3BPs are RNA-binding proteins that condense into SGs following translation shutoff during the integrated stress response (ISR). Three G3BP paralogs (G3BP1, G3BP2A, and G3BP2B) have been identified in vertebrates. Here, we found a molecular tool to study G3BP condensation into SGs by mutating residue V11 of G3BPs. This conserved amino acid potentiates the G3BP-Caprin-1 complex, hence promoting SG assembly. Ribosome profiling revealed that disruption of G3BP condensation impacts mRNA expression during the ISR. Moreover, we found that G3BP2B robustly condenses and promotes changes in mRNA expression under endoplasmic reticulum (ER) stress. This indicates that G3BP paralogs differentially regulate SG assembly and gene expression programs. Together, this work suggests that stress granule assembly promotes changes in gene expression to mediate stress-response during the ISR.

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G3BP2B stress granules regulate mRNA expression under ER stress [RNAseq_Exp2]

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SARS-CoV-2 Nucleocapsid protein attenuates stress granule formation and interacts directly with mRNAs to impair host stress response (RNA-Seq)

Project description:Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) nucleocapsid (N) protein is highly expressed upon infection and is essential for viral replication, making it a promising target for antiviral drug and vaccine development. Here, starting from a functional proteomics workflow, we catalogued the protein-protein interactions of 28 SARS-CoV-2 proteins in HEK293 cells, including an evolutionarily conserved specific interaction of N with the stress granule resident proteins G3BP1 and G3BP2. N protein localizes to stress granules and sequesters G3BP1 and G3BP2 away from their normal interaction partners, thus attenuating stress granule formation. N also binds directly to host mRNAs, with a preference for 3´ UTRs, and modulates target mRNA stability. We show that SARS-CoV-2 N protein rewires the G3BP1 mRNA-binding profile, thereby suppressing host gene expression changes induced in response to cellular stress.

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