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A PARP14/TARG1-Regulated RACK1 MARylation Cycle Drives Stress Granule Dynamics in Cancer Cells [RNA-seq]

ABSTRACT: A PARP14/TARG1-Regulated RACK1 MARylation Cycle Drives Stress Granule Dynamics in Cancer Cells [RNA-seq]

PROVIDER: PRJNA1028613 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR26400258.fastq.gz	Fastqsanger.gz
	SRR26400259.fastq.gz	Fastqsanger.gz
	SRR26400260.fastq.gz	Fastqsanger.gz
	SRR26400261.fastq.gz	Fastqsanger.gz
	SRR26400262.fastq.gz	Fastqsanger.gz

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A PARP14/TARG1-Regulated RACK1 MARylation Cycle Drives Stress Granule Dynamics in Cancer Cells

Project description:A PARP14/TARG1-Regulated RACK1 MARylation Cycle Drives Stress Granule Dynamics in Cancer Cells

| PRJNA1028614 | ENA

A PARP14/TARG1-Regulated RACK1 MARylation Cycle Drives Stress Granule Dynamics in Cancer Cells [Ribo-seq]

Project description:In this study we examine the role of RACK1 MARylation in stress granule assembly and translational regulation in ovarian cancer cells. In addition, we describe the role of TARG1, an ADPR hydrolase enzyme in stress granule assembly and translation.

2025-01-02 | GSE245503 | GEO

A PARP14/TARG1-Regulated RACK1 MARylation Cycle Drives Stress Granule Dynamics in Cancer Cells [RNA-seq]

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A PARP14/TARG1-Regulated RACK1 MARylation Cycle Drives Stress Granule Dynamics in Cancer Cells [Ribo-seq]

Project description:A PARP14/TARG1-Regulated RACK1 MARylation Cycle Drives Stress Granule Dynamics in Cancer Cells [Ribo-seq]

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A PARP14/TARG1-Regulated RACK1 MARylation Cycle Drives Stress Granule Dynamics in Ovarian Cancer Cells.

Project description:Mono(ADP-ribosyl)ation (MARylation), a post-translational modification (PTM) of proteins, is emerging as a critical regulator of ribosome function and translation. Herein, we demonstrate that RACK1, a member of the tryptophan-aspartate repeat (WD-repeat) family of proteins and an integral component of the ribosome, is MARylated by the mono(ADP-ribosyl) transferase (MART) PARP14 in ovarian cancer cells. We mapped and confirmed the sites of MARylation, which occur on three acidic residues within blades 4 and 5 of β-propeller domain of RACK1, a chaperone that shuttles and anchors proteins where needed. Site-specific MARylation of RACK1 is required for stress granule formation and promotes the colocalization of RACK1 to stress granules with key components, such as G3BP1, eIF3η, and 40S ribosomal proteins. In parallel, we observed reduced translation of a subset of mRNAs, including those encoding key cancer regulators (e.g., AKT). Treatment with a PARP14 inhibitor or mutation of the sites of MARylation on RACK1 blocks these outcomes. To re-set the system after prolonged stress and recovery, the ADP-ribosyl hydrolase TARG1 deMARylates RACK1 to dissociate the stress granules and return RACK1 and the 40S ribosomal subunit to the cytoplasm, allowing for a restoration of translation. Collectively, our results highlight the discovery of a PARP14/TARG1-regulated RACK1 MARylation cycle that controls stress granule assembly and disassembly in ovarian cancer cells.

| S-EPMC10592810 | biostudies-literature

A PARP14/TARG1-Regulated RACK1 MARylation Cycle Drives Stress Granule Dynamics in Cancer Cells

Project description:This SuperSeries is composed of the SubSeries listed below.

2025-01-01 | GSE245504 | GEO

Polysome purified mRNA in control and RACK1 silenced in human hepatocarcinoma cells

Project description:Fighting viral infections is hampered by the scarcity of viral targets and their variability resulting in development of resistance. Viruses depend on cellular molecules for their life cycle, which are attractive alternative targets, provided that they are dispensable for normal cell functions. Using the model organism Drosophila melanogaster, we identify the ribosomal protein RACK1 as a cellular factor required for infection by internal ribosome entry site (IRES)-containing viruses. We further show that RACK1 is an essential determinant for hepatitis C virus translation and infection indicating that its function is conserved among distantly related human and fly viruses. Inhibition of RACK1 does not affect Drosophila or human cell viability and proliferation, and RACK1-silenced adult flies are viable, indicating that this protein is not essential for general translation. Our findings demonstrate a specific function for RACK1 in selective mRNA translation and uncover a new target for the development of broad antiviral intervention. 4 Controls 4 RACK1 silenced cells

2015-05-14 | E-GEOD-60374 | biostudies-arrayexpress

Polysome purified mRNA in control and RACK1 silenced in human hepatocarcinoma cells

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Project description:MicroRNAs (miRNAs) regulate plant development by post-transcriptional regulation of target genes. In Arabidopsis thaliana, DCL1 processes precursors (pri-miRNAs) to miRNA duplexes, which associate with AGO1. Additional proteins act in concert with DCL1 (e.g. HYL1 and SERRATE) or AGO1, respectively, to facilitate efficient and precise pri-miRNA processing and miRNA loading. In this study, we show that the accumulation of plant microRNAs depends on RECEPTOR FOR ACTIVATED C KINASE 1 (RACK1), a scaffold protein found in all higher eukaryotes. miRNA levels are reduced in rack1 mutants and our data suggest that RACK1 affects the microRNA pathway via several distinct mechanisms involving direct interactions with known microRNA factors: RACK1 ensures the accumulation and processing of some pri-miRNAs, directly interacts with SERRATE and is part of an AGO1 complex. As a result, mutations in RACK1 lead to misregulation of miRNA target genes, which is important for ABA responses and phyllotaxy. In conclusion, our study discovered complex functioning of RACK1 proteins in the Arabidopsis miRNA pathway, which are important for miRNA production and therefore plant development.

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AGS-RACK1

Project description:MicroRNA microarray profiling analysis was performed on human gastric cancer AGS cells after RACK1 silenced or not

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