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Proximity labeling proteins differences between TRIM25 and G3BP1 interactions or not, and Proximity labeling proteins differences between G3BP1 and TRIM25 in the presence or absence of poly(I:C) stimulation

ABSTRACT: This project investigates G3BP1 proximity proteins by constructing a G3BP1-BirA* fusion protein using G3BP1 as a decoy protein and BirA* as a biotin ligase. The changes in G3BP1 proximity proteins were studied in the presence or absence of poly(I:C) stimulation conditions, using poly(I:C) stimulation as a variable. This project investigated the TRIM25 proximity protein by constructing a TRIM25-BirA* fusion protein with TRIM25 as the decoy protein and BirA* as the biotin ligase. The changes of TRIM25 proximity proteins under the conditions of TRIM25 interacting with or without G3BP1 were studied by performing PTFG sequence deletion on TRIM25; the changes in TRIM25 proximity proteins were studied in the presence or absence of poly(I:C) stimulation conditions, using poly(I:C) stimulation as a variable.

ORGANISM(S): Homo Sapiens

SUBMITTER: Da Jia

PROVIDER: PXD043603 | iProX | Fri Jul 07 00:00:00 BST 2023

REPOSITORIES: iProX

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G3BP1 proximity labeling proteins under poly(I:C)

Project description:This project investigates G3BP1 proximity proteins by constructing a G3BP1-BirA* fusion protein using G3BP1 as a decoy protein and BirA* as a biotin ligase. The changes in G3BP1 proximity proteins were studied in the presence or absence of poly(I:C) stimulation conditions, using poly(I:C) stimulation as a variable.

2023-07-07 | PXD043602 |

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

G3BP1 Binds to Guanine Quadruplexes in mRNAs

Project description:we identify G3BP1 as a novel rG4-binding protein, and reveal that G3BP1 can modulate mRNA stability through its binding with rG4 structures

2021-03-16 | GSE168943 | GEO

ChIP-seq analysis of G3BP1 in KGN cells

Project description:To investigate whether G3BP1 binds to telomeric DNA, we performed the ChIP-seq analysis of G3BP1 in KGN cells.

2024-04-14 | GSE263539 | GEO

G3BP1 inhibits Cul3SPOP to amplify AR signaling and promote prostate tumorigenesis

Project description:Speckle-type POZ protein (SPOP), an E3 ubiquitin ligase, acts as a tumor suppressor. We identified G3BP1 as non-substrate interactor of SPOP. G3BP1 is a well-known oncogene in many cancer types, but its role in prostate cancer (PCa) remains largely elusive. We showed that G3BP1 functions as an upstream regulator and potent endogenous inhibitor of Cul3SPOP, suggesting a distinctive Cul3SPOP inactivation independent of SPOP mutations. Transcriptomic analysis together with functional studies revealed that the G3BP1-SPOP ubiquitin signaling axis is involved in PCa progression through activating AR signaling. Further, AR upregulates G3BP1 to potentiate feed-forward amplification of signaling through G3BP1-SPOP axis. Overall, we show G3BP1high PCa tumors constitute a new subset where G3BP1 inhibits Cul3SPOP function to upregulate AR signaling, and promotes tumorigenesis.

2021-09-26 | GSE138612 | GEO

G3bp1-miR-1 axis regulates cardiomyocyte hypertrophy

Project description:We examine the role of G3bp1, a RNA binding protein and site specific endoribonuclease in gene expression in isolated neonatal cardiomyocytes. RNAseq data from cardiomyocytes were infected with adenoviruses expressing shRNA against G3bp1 (ad-siG3bp1) or Luciferase (ad-siLUC, control) showed significant decrease in transcript abudnnace of cardiac-enriched genes involved in Calcium handling, contraction, action potential and sacromere function. On the other hand increase was observed in genes that regulate Hippo, TNF and TGFb signaling. Knockdown of G3bp1 inhibited endothelin-1 induced cardiomyocyte hypertrophy.

2022-01-14 | GSE184441 | GEO

G3BP1 translocates into mitochondria to impair MCU complex function and promotes NASH progression

2023-12-13 | GSE249869 | GEO

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]

2024-04-20 | GSE246499 | GEO

RAN directly binds and stabilizes G3BP1 mRNA in the nucleus to facilitate proliferation and metastasis of nasopharyngeal carcinoma (si-G3BP1 RNA-seq)

Project description:RNA binding proteins (RBPs) play a critical role in tumor progression by participating in the post-transcriptional regulation of RNA. However, the expression and function of RBPs in nasopharyngeal carcinoma (NPC) remain elusive. This study identified 5 RBPs (RAN, EZH2, RDM1, HRSP12, and ALYREF) that were up-regulated in NPC and could promote NPC cells migration or proliferation. RAN was first investigated because of its most significant effect on NPC cells. Functionally, RAN facilitated NPC proliferation, migration, and invasion in vitro and in vivo. High expression of RAN was associated with poor prognosis of NPC patients and could be performed as a prognostic biomarker. Mechanistically, RAN mediated the nucleus import of TDP43 and enhanced TDP43 nuclear distribution. On the other hand, RAN was directly bound to the coding sequence of G3BP1 mRNA and served as an adapter to facilitate TDP43 interacting with G3BP1 mRNA 3’untranslated region. Thereby increased G3BP1 mRNA stability in the nucleus and led to up-regulation of G3BP1, which further enhanced ATK/ERK phosphorylation and ultimately promoted NPC proliferation and metastasis.

2024-10-31 | GSE262032 | GEO

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