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G3BP1 Ribonucleoprotein Complexes Regulate Focal Adhesion Protein Mobility and Cell Migration [Ribo-Seq]

ABSTRACT: G3BP1 Ribonucleoprotein Complexes Regulate Focal Adhesion Protein Mobility and Cell Migration [Ribo-Seq]

PROVIDER: PRJNA1035318 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR26662537_1.fastq.gz	Fastqsanger.gz
	SRR26662537_2.fastq.gz	Fastqsanger.gz
	SRR26662538_1.fastq.gz	Fastqsanger.gz
	SRR26662538_2.fastq.gz	Fastqsanger.gz
	SRR26662539.fastq.gz	Fastqsanger.gz

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G3BP1 Ribonucleoprotein Complexes Regulate Focal Adhesion Protein Mobility and Cell Migration [Ribo-Seq]

Project description:The subcellular localization of mRNAs plays a pivotal role in biological processes, including cell migration. For instance, β-actin mRNA and its associated RNA binding protein (RBP), ZBP1/IGF2BP1, are recruited to focal adhesions (FAs), to support localized β-actin synthesis, crucial for cell migration. However, whether other mRNAs and RBPs also localize at FAs remains unclear. Here, we identify hundreds of mRNAs that are enriched at FAs (FA-mRNAs). FA-mRNAs share characteristics with stress granule (SG) mRNAs and are found in ribonucleoprotein (RNP) complexes with the SG RBP. Mechanistically, G3BP1 binds to FA proteins in an RNA-dependent manner, and its RNA-binding and dimerization domains, essential for G3BP1 to form RNPs in SG, are required for FA localization and cell migration. We find that G3BP1 RNPs promote cell speed by enhancing FA protein mobility and FA size. These findings suggest a previously unappreciated role for G3BP1 RNPs in regulating FA function under non-stress conditions.

2024-04-20 | GSE246955 | GEO

G3BP1 Ribonucleoprotein Complexes Regulate Focal Adhesion Protein Mobility and Cell Migration [RNA-seq]

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G3BP1 Ribonucleoprotein Complexes Regulate Focal Adhesion Protein Mobility and Cell Migration

Project description:G3BP1 Ribonucleoprotein Complexes Regulate Focal Adhesion Protein Mobility and Cell Migration

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G3BP1 Ribonucleoprotein Complexes Regulate Focal Adhesion Protein Mobility and Cell Migration

Project description:The subcellular localization of mRNAs plays a pivotal role in biological processes, including cell migration1-6. For instance, β-actin mRNA and its associated RNA binding protein (RBP), ZBP1/IGF2BP1, are recruited to focal adhesions (FAs), to support localized β-actin synthesis, crucial for cell migration7-9. However, whether other mRNAs and RBPs also localize at FAs remains unclear. Here, we identify hundreds of mRNAs that are enriched at FAs (FA-mRNAs). FA-mRNAs share characteristics with stress granule (SG) mRNAs and are found in ribonucleoprotein (RNP) complexes with the SG RBP. Mechanistically, G3BP1 binds to FA proteins in an RNA-dependent manner, and its RNA-binding and dimerization domains, essential for G3BP1 to form RNPs in SG10, are required for FA localization and cell migration. We find that G3BP1 RNPs promote cell speed by enhancing FA protein mobility and FA size. These findings suggest a previously unappreciated role for G3BP1 RNPs in regulating FA function under non-stress conditions.

2025-01-22 | PXD059392 | Pride

G3BP1 Ribonucleoprotein Complexes Regulate Focal Adhesion Protein Mobility and Cell Migration [RNA-seq]

Project description:G3BP1 Ribonucleoprotein Complexes Regulate Focal Adhesion Protein Mobility and Cell Migration [RNA-seq]

| PRJNA1033345 | ENA

G3BP1 Ribonucleoprotein Complexes Regulate Focal Adhesion Protein Mobility and Cell Migration

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

2024-04-20 | GSE246956 | GEO

G3BP1 ribonucleoprotein complexes regulate focal adhesion protein mobility and cell migration.

Project description:The subcellular localization of mRNAs plays a pivotal role in biological processes, including cell migration. For instance, β-actin mRNA and its associated RNA-binding protein (RBP), ZBP1/IGF2BP1, are recruited to focal adhesions (FAs) to support localized β-actin synthesis, crucial for cell migration. However, whether other mRNAs and RBPs also localize at FAs remains unclear. Here, we identify hundreds of mRNAs that are enriched at FAs (FA-mRNAs). FA-mRNAs share characteristics with stress granule (SG) mRNAs and are found in ribonucleoprotein (RNP) complexes with the SG RBP. Mechanistically, G3BP1 binds to FA proteins in an RNA-dependent manner, and its RNA-binding and dimerization domains, essential for G3BP1 to form RNPs in SG, are required for FA localization and cell migration. We find that G3BP1 RNPs promote cell speed by enhancing FA protein mobility and FA size. These findings suggest a previously unappreciated role for G3BP1 RNPs in regulating FA function under non-stress conditions.

| S-EPMC11923778 | biostudies-literature

Focal Adhesion Kinase Dependent Expression

Project description:The goal of this study was to identify transcripts, which are differentially regulatulated in the presence and absence of Focal Adhesion Kinase. As Focal Adhesion Kinase activity can depend upon cell density (Snijder et al. Nature 2009), biological replicates where cells, were seeded very sparsely or confluently, were used. Focal Adhesion Kinase Knockout (ATCC CRL-2644) and Rescue Cells (Sieg et al. 1998, clone DA2) were seeded at two different concentrations. Replicas refer to biological replicates, performed on different days. Only one single technical replicate has been done per biological replicate.

2013-09-17 | E-GEOD-43873 | biostudies-arrayexpress

Focal Adhesion Kinase Dependent Expression

2013-09-17 | GSE43873 | GEO

G3BP1 translocates into mitochondria to impair MCU complex function and promotes NASH progression [G3bp1-HKO and G3bp1-Flox mice with BSA or PA treatment]

Project description:Mitochondrial calcium signaling plays a critical role in mitochondrial homeostasis during non-alcoholic steatohepatitis (NASH) progression. Here, we report Ras‐GTPase activating protein SH3 domain‐binding protein 1 (G3BP1), a core protein of stress granule (SG), significantly upregulated in NAFLD/NASH patients, mouse models and palmitic acid-stimulated hepatocytes. Hepatocyte-specific G3BP1 deficiency attenuates NASH in two dietary mouse models. SG and the mitochondrial import protein TOM70 collaboratively mediate the translocation of G3BP1 to the mitochondria. G3BP1 interacts and stabilizes mitochondrial calcium uptake 1 (MICU1) via inhibiting YME1L1-mediated degradation of MICU1, and also impedes MCU complex activity and assembly, leading to mitochondrial calcium overload. Moreover, metabolic stress suppresses TRIM25-mediated K63-ubiquitination of G3BP1 and subsequent SG disassembly. Pharmacological inhibition of G3BP1 impairs the G3BP1-MICU1 interaction and prevents mitochondrial homeostasis imbalance and NASH progression. Collectively, we uncover the significant role of mitochondrial G3BP1 in mitochondrial homeostasis and NASH progression, which provides a potential target for therapeutic interventions.

2024-08-18 | GSE274650 | GEO

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