Research Progress on the Structure and Function of G3BP [PDF]
Frontiers in Immunology, 2021 Ras-GTPase-activating protein (SH3 domain)-binding protein (G3BP) is an RNA binding protein. G3BP is a key component of stress granules (SGs) and can interact with many host proteins to regulate the expression of SGs.
Haixue Zheng, Dan Li
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SARS-CoV-2 N protein recruits G3BP to double membrane vesicles to promote translation of viral mRNAs [PDF]
Nature CommunicationsRas-GTPase-activating protein SH3-domain-binding proteins (G3BP) are critical for the formation of stress granules (SGs) through their RNA- and ribosome-binding properties. SARS-CoV-2 nucleocapsid (N) protein exhibits strong binding affinity for G3BP and
Adnane Achour +2 more
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The RNA-Binding Protein Rasputin/G3BP Enhances the Stability and Translation of Its Target mRNAs [PDF]
Cell Reports, 2020 Summary: G3BP RNA-binding proteins are important components of stress granules (SGs). Here, we analyze the role of the Drosophila G3BP Rasputin (RIN) in unstressed cells, where RIN is not SG associated. Immunoprecipitation followed by microarray analysis
Angelo Karaiskakis +2 more
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Viral and Cellular Proteins Containing FGDF Motifs Bind G3BP to Block Stress Granule Formation
PLoS Pathogens, 2015 The Ras-GAP SH3 domain-binding proteins (G3BP) are essential regulators of the formation of stress granules (SG), cytosolic aggregates of proteins and RNA that are induced upon cellular stress, such as virus infection.
Tatyana Sandalova +2 more
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Genome-Wide Identification of G3BP Family in U’s Triangle Brassica Species and Analysis of Its Expression in B. napus [PDF]
PlantsThe RasGAP SH3 domain binding protein (G3BP) is a highly conserved family of proteins in eukaryotic organisms that coordinates signal transduction and post-transcriptional gene regulation and functions in the formation of stress granules.
Alain Tseke Inkabanga +13 more
doaj +2 more sources
Pharmacological modulation of stress granules via G3BP1/2: A pathway to treat cancer, inflammatory disease, and neurodegeneration [PDF]
Frontiers in PharmacologyStress granules (SGs) are membraneless ribonucleoprotein condensates formed by liquid–liquid phase separation of non-translating mRNAs under stress, acting as dynamic platforms for translational reprogramming and cytoprotection.
Jinhua Yang, Fenfei Gao
doaj +2 more sources
Pseudorabies virus IE180 protein hijacks G3BPs into the nucleus to inhibit stress granule formation [PDF]
Journal of VirologyPseudorabies virus (PRV) is a porcine alphaherpesvirus that can infect different animal species and cause pruritus and lethal encephalitis. Stress granules (SGs) are membrane-free cytoplasmic structures formed by liquid-liquid phase separation of G3BP ...
Ruihan Zhao +6 more
doaj +2 more sources
PLoS Pathogens, 2019 G3BP-1 and -2 (hereafter referred to as G3BP) are multifunctional RNA-binding proteins involved in stress granule (SG) assembly. Viruses from diverse families target G3BP for recruitment to replication or transcription complexes in order to block SG ...
Benjamin Götte +2 more
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Stress granule-related genes during embryogenesis of an invertebrate chordate [PDF]
Frontiers in Cell and Developmental BiologyControlling global protein synthesis through the assembly of stress granules represents a strategy adopted by eukaryotic cells to face various stress conditions.
Laura Drago +7 more
doaj +2 more sources
Research Progress on the Biological Function, Disease-Driving Mechanism and Clinical Targeting Strategies of G3BP2 [PDF]
MoleculesG3BP2 is an important RNA-binding protein that belongs to the mammalian Ras-GAP SH3 domain-binding protein (G3BP) family. Its structure enables it to bind to RNA or proteins, regulate nuclear–cytoplasmic shuttling, and participate in various functions ...
Yao Chen +6 more
doaj +2 more sources