Viral and cellular proteins containing FGDF motifs bind G3BP to block stress granule formation.
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.
Marc D Panas +6 more
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Separate domains of G3BP promote efficient clustering of alphavirus replication complexes and recruitment of the translation initiation machinery. [PDF]
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 +7 more
doaj +2 more sources
Antibody response in vaccinated pregnant mares to recent G3BP[12] and G14P[12] equine rotaviruses
Background Both the G3P[12] and the G14P[12] type of equine group A rotavirus (RVA) have recently become predominant in many countries, including Japan. G3 types are classified further into G3A and G3B.
Nemoto Manabu +11 more
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Pseudorabies virus IE180 protein hijacks G3BPs into the nucleus to inhibit stress granule formation [PDF]
Pseudorabies 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
Stress granule-related genes during embryogenesis of an invertebrate chordate [PDF]
Controlling 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
Stress-specific 14-3-3–client modules in digestive cancers: an evidence-graded review of adaptive survival and therapy resistance [PDF]
14-3-3 proteins are phosphoserine- and phosphothreonine-binding adaptors that regulate client localization, stability and activity under cellular stress.
Rudong Li, Zhipeng Zhao, Xudong Wang
doaj +2 more sources
Research Progress on the Biological Function, Disease-Driving Mechanism and Clinical Targeting Strategies of G3BP2 [PDF]
G3BP2 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
Perillaldehyde Improves Parkinson‐Like Deficits by Targeting G3BP Mediated Stress Granule Assembly in Preclinical Models [PDF]
Stress granules (SGs) fulfill a pivotal role in host defense mechanisms, by sequestering both mRNA and protein via the process of liquid–liquid phase separation (LLPS).
Minglv Fang +12 more
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The SHFV nsp2 and nucleocapsid proteins recruit G3BP1 to sites of viral replication, but stress granules are not induced by the infection [PDF]
Stress granules (SGs) are dynamic, cytoplasmic foci that form in response to environmental stresses, including viral infections, and function to restore cellular homeostasis by regulating mRNA translation, storage, and decay.
Ayisha A. Lavender +6 more
doaj +2 more sources
Endogenous TDP-43, but not FUS, contributes to stress granule assembly via G3BP
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by the selective loss of upper and lower motor neurons, a cell type that is intrinsically more vulnerable than other cell types to exogenous stress.
Aulas Anaïs +2 more
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