ArticleOpen biology2023
Caprin-1 binding to the critical stress granule protein G3BP1 is influenced by pH.
Article in Open biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Review
- High expression of G3BP1 is associated with poor prognosis in breast invasive carcinoma.Oncology letters · 2026Article
- Targeting G3BP1 Condensate Topology Promotes Stress Granule Assembly via mAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Pharmacological modulation of stress granulesFrontiers in pharmacology · 2026Review
- Review
- Defining short linear motif binding determinants by phage display-based deep mutational scanning.Protein science : a publication of the Protein Society · 2025Article
- Protein aggregates and biomolecular condensates: implications for human health and disease.Frontiers in molecular biosciences · 2025Review
- SARS-CoV-2 N protein recruits G3BP to double membrane vesicles to promote translation of viral mRNAs.Nature communications · 2024Article
- G3BP isoforms differentially affect stress granule assembly and gene expression during cellular stress.Molecular biology of the cell · 2024Article
- Review
- Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replication and pathogenicity.Cell reports · 2024Article
- Review
- Tryptophan mutations in G3BP1 tune the stability of a cellular signaling hub by weakening transient interactions with Caprin1 and USP10.The Journal of biological chemistry · 2022Article
- SARS-CoV-2 Nucleocapsid Protein Targets a Conserved Surface Groove of the NTF2-like Domain of G3BP1.Journal of molecular biology · 2022Article
- Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities.Nature communications · 2021Article
- Two Birds With One Stone: RNA Virus Strategies to Manipulate G3BP1 and Other Stress Granule Components.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
17 authors at 5 institutions in 2 countries.
Funding
Abstract
G3BP is the central node within stress-induced protein-RNA interaction networks known as stress granules (SGs). The SG-associated proteins Caprin-1 and USP10 bind mutually exclusively to the NTF2 domain of G3BP1, promoting and inhibiting SG formation, respectively. Herein, we present the crystal structure of G3BP1-NTF2 in complex with a Caprin-1-derived short linear motif (SLiM). Caprin-1 interacts with His-31 and His-62 within a third NTF2-binding site outside those covered by USP10, as confirmed using biochemical and biophysical-binding assays. Nano-differential scanning fluorimetry revealed reduced thermal stability of G3BP1-NTF2 at acidic pH. This destabilization was counterbalanced significantly better by bound USP10 than Caprin-1. The G3BP1/USP10 complex immunoprecipated from human U2OS cells was more resistant to acidic buffer washes than G3BP1/Caprin-1. Acidification of cellular condensates by approximately 0.5 units relative to the cytosol was detected by ratiometric fluorescence analysis of pHluorin2 fused to G3BP1. Cells expressing a Caprin-1/FGDF chimera with higher G3BP1-binding affinity had reduced Caprin-1 levels and slightly reduced condensate sizes. This unexpected finding may suggest that binding of the USP10-derived SLiM to NTF2 reduces the propensity of G3BP1 to enter condensates.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.