Stress granule assembly is mediated by prion-like aggregation of TIA-1.

By Natalie Gilks, N. Kedersha, M. Ayodele, Lily Shen, G. Stoecklin, L. Dember, Paul Anderson. Molecular Biology of the Cell, 2004

1,027 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/a1e549a017b3e9f57ed306881b7b19152c4bee01

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Citations in the corpus

Mammalian stress granules and processing bodies. (2007, methodology): “Such proteins include TIA-1/TIAR (Gilks et al., 2004), Fragile X Mental Retardation Protein (FMRP/FXR1; Mazroui et al.”
P bodies and the control of mRNA translation and degradation. (2007, background): “repression and decay machinery to specific transcripts (Goldstrohm et al., 2006).”
Eukaryotic stress granules: the ins and outs of translation. (2009, background): “Moreover, TIA-1 lacking its QN-rich domain cannot support stress granule formation, though fusion of the yeast SUP35 prion domain in its place recovers TIA-1 stress granule assembly function (Gilks et al., 2004).”
G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits (2016, background): “Their formation is regulated by two related parameters: (a) SG-nucleating proteins, aggregating in response to overexpression (Gilks et al., 2004; Anderson and Kedersha, 2008), de-naturing stresses (heat shock), or molecular crowding (osmotic stress), independent of phospho-eIF2 α (p-eIF2 α ;…”
Protein Phase Separation: A New Phase in Cell Biology (2018, background): “In contrast, many RNA-protein (RNP) granules are dynamic and liquid-like, and genetic experiments have demonstrated that IDRs can aid in their assembly [40-42].”
The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease (2012, background): “This is certainly a function of the TIA-1 prion-like domain, which ranks 11 among human RRM-bearing prion candidates (Table 1) (Gilks et al., 2004).”
Stress granules and processing bodies are dynamically linked sites of mRNP remodeling (2005, methodology): “DU145 and HT1080 cells were transfected with control or Lsm4 siRNA, untreated or treated with arsenite, fixed and stained for PBs, scored microscopically, and counted.”
RNA granules: post-transcriptional and epigenetic modulators of gene expression (2009, background): “The translational silencers TIA1 and TIAR (among others) contribute to stress-induced translational arrest, polysome disassembly and aggregation of client mRNP”
Tar DNA Binding Protein-43 (TDP-43) Associates with Stress Granules: Analysis of Cultured Cells and Pathological Brain Tissue (2010, background): “SG nucleation occurs via reversible protein aggregation mechanism that is based on prion domains present in TIA-1, TIAR and G3BP [8].”
Formation and Maturation of Phase Separated Liquid Droplets by RNA Binding Proteins (2015, background): “These sequences were originally identified by their similarity to those of the known prions, human prion protein and Sup35p (Gilks et al., 2004; Reijns et al., 2008; Decker et al., 2007), but also include those containing repeated G/S-F/Y-G/S motifs (Kato et al., 2012; Nott et al., 2015; Updike et a”
Intrinsically disordered regions contribute promiscuous interactions to RNP granule assembly (2017, background): “However, since there are cases wherein one IDR can functionally substitute for another in RNP granule assembly (Decker et al., 2007; Gilks et al., 2004), a more generic role for IDRs in RNP granule assembly is also likely.”
G3BP1 is a tunable switch that triggers phase separation to assemble stress granules (2020, positive): “Several studies have implicated various RBPs as “essential” to SG assembly, including TIA1 (Gilks et al., 2004), HDAC6 (Kwon et al.”