Identification of a non-canonical G3BP-binding sequence in a Mayaro virus nsP3 hypervariable domain
Ras-GTPase-activating SH3 domain-binding-proteins 1 (G3BP1) and 2 (G3BP2) are multifunctional RNA-binding proteins involved in stress granule nucleation, previously identified as essential cofactors of Old World alphaviruses.
Aymeric Neyret +6 more
doaj +4 more sources
Endogenous TDP-43, but not FUS, contributes to stress granule assembly via G3BP [PDF]
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
doaj +4 more sources
The RasGAP-associated endoribonuclease G3BP assembles stress granules. [PDF]
Stress granules (SGs) are formed in the cytoplasm in response to various toxic agents, and are believed to play a critical role in the regulation of mRNA metabolism during stress. In SGs, mRNAs are stored in an abortive translation initiation complex that can be routed to either translation initiation or degradation.
Tourrière, Hélène +6 more
openaire +3 more sources
The miR‐669a‐5p/G3BP/HDAC6/AKAP12 Axis Regulates Primary Cilia Length [PDF]
Primary cilia are conserved organelles in most mammalian cells, acting as “antennae” to sense external signals. Maintaining a physiological cilium length is required for cilium function.
Weina Wang +6 more
doaj +4 more sources
The RasGAP-associated endoribonuclease G3BP mediates stress granule assembly
Stress granules (SGs) are formed in the cytoplasm in response to various toxic agents and are believed to play a critical role in the regulation of mRNA metabolism during stress. In SGs, mRNAs are stored in an abortive translation initiation complex that can be routed to either translation initiation or degradation.
Hélène Tourrière +6 more
openaire +3 more sources
Comprehensive evolutionary analysis and nomenclature of plant G3BPs
A thorough phylogenetic analysis of eukaryotic G3BPs (Rasputins) with a focus on plant G3BP proteins, classification into two subfamilies and a proposed systematic nomenclature.
Aala A Abulfaraj +6 more
doaj +4 more sources
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
doaj +2 more sources
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
Analysis of subcellular G3BP redistribution during rubella virus infection
Rubella virus (RUBV) replicates slowly and to low titre in vertebrate cultured cells, with minimal cytopathology. To determine whether a cellular stress response is induced during such an infection, the formation of Ras-GAP-SH3 domain-binding protein (G3BP)-containing stress granules (SGs) in RUBV-infected cells was examined.
Jason D, Matthews, Teryl K, Frey
openaire +3 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
doaj +2 more sources

