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G3BP1 Ribonucleoprotein Complexes Regulate Focal Adhesion Protein Mobility and Cell Migration

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Homo sapiens

PROVIDER: GSE246956 | GEO | 2024/04/20

REPOSITORIES: GEO

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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]

2024-04-20 | GSE246499 | 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 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

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

| PRJNA1035314 | ENA

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 [Ribo-Seq]

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

| PRJNA1035318 | ENA

Focal adhesion kinase-dependent focal adhesion recruitment of SH2 domains directs SRC into focal adhesions to regulate cell adhesion and migration.

Project description:Directed cell migration requires dynamical control of the protein complex within focal adhesions (FAs) and this control is regulated by signaling events involving tyrosine phosphorylation. We screened the SH2 domains present in tyrosine-specific kinases and phosphatases found within FAs, including SRC, SHP1 and SHP2, and examined whether these enzymes transiently target FAs via their SH2 domains. We found that the SRC_SH2 domain and the SHP2_N-SH2 domain are associated with FAs, but only the SRC_SH2 domain is able to be regulated by focal adhesion kinase (FAK). The FAK-dependent association of the SRC_SH2 domain is necessary and sufficient for SRC FA targeting. When the targeting of SRC into FAs is inhibited, there is significant suppression of SRC-mediated phosphorylation of paxillin and FAK; this results in an inhibition of FA formation and maturation and a reduction in cell migration. This study reveals an association between FAs and the SRC_SH2 domain as well as between FAs and the SHP2_N-SH2 domains. This supports the hypothesis that the FAK-regulated SRC_SH2 domain plays an important role in directing SRC into FAs and that this SRC-mediated FA signaling drives cell migration.

| S-EPMC4683442 | biostudies-literature

Syndecan-1 controls cell migration by activating Rap1 to regulate focal adhesion disassembly.

Project description:After injury, residual epithelial cells coordinate contextual clues from cell-cell and cell-matrix interactions to polarize and migrate over the wound bed. Protrusion formation, cell body translocation and rear retraction is a repetitive process that allows the cell to move across the substratum. Fundamental to this process is the assembly and disassembly of focal adhesions that facilitate cell adhesion and protrusion formation. Here, we identified syndecan-1 as a regulator of focal adhesion disassembly in migrating lung epithelial cells. Syndecan-1 altered the dynamic exchange of adhesion complex proteins, which in turn regulates migration speed. Moreover, we provide evidence that syndecan-1 controls this entire process through Rap1. Thus, syndecan-1 restrains migration in lung epithelium by activating Rap1 to slow focal adhesion disassembly.

| S-EPMC3533394 | biostudies-literature

miR-29a-3p coordinates the ECM-integrin-adaptor protein axis to regulate focal adhesion in allergic rhinitis

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

2024-10-01 | GSE247295 | GEO

Hax1 regulate focal adhesion dynamics through IQGAP1.

Project description:Cell migration is a highly orchestrated process requiring the coordination between the cytoskeleton, cell membrane and extracellular matrix adhesions. Our previous study demonstrated that Hax1 interacts with EB2, a microtubule end-binding protein, and this interaction regulate cell migration in keratinocytes. However, little is known about the underlying regulatory mechanism. Here, we show that Hax1 links dynamic focal adhesions to regulate cell migration via interacting with IQGAP1, a multidomain scaffolding protein, which was identified by affinity purification coupled with LC-MS/MS. Biochemical characterizations revealed that C-terminal region of Hax1 and RGCT domain of IQGAP1 are the most critical binding determinants for its interaction. IQGAP1/Hax1 interaction is essential for cell migration in MCF7 cells. Knockdown of HAX1 not only stabilizes focal adhesions, but also impairs the accumulation of IQGAP in focal adhesions. Further study indicates that this interaction is critical for maintaining efficient focal adhesion turnover. Perturbation of the IQGAP1/Hax1 interaction in vivo using a membrane-permeable TAT-RGCT peptide results in impaired focal adhesion turnover, thus leading to inhibition of directional cell migration. Together, our findings unravel a novel interaction between IQGAP1 and Hax1, suggesting that IQGAP1 association with Hax1 plays a significant role in focal adhesion turnover and directional cell migration. Video Abstract.

| S-EPMC10364419 | biostudies-literature

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