G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits

By N. Kedersha, M. Panas, Christopher A. Achorn, Shawn Lyons, Sarah Tisdale, T. Hickman, Marshall P. Thomas, J. Lieberman, G. McInerney, P. Ivanov and 1 more. Journal of Cell Biology, 2016

603 citations recorded by the source corpus.

Stress granule condensation (SGC) of translationally arrested mRNAs requires G3BP, and G3BP-mediated SGC is inhibited by serine 149 phosphorylation, regulated by mutually exclusive binding of Caprin1 and USP10, and requires its RGG region for SGC and for interactions with 40S ribosomal subunits.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/33ec1f6b975195a207a518a56de6ed7e9b1f49c3

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Citations in the corpus

Liquid-Liquid Phase Separation in Disease. (2019, background): “G3BP is an RNA-binding protein that is absolutely required for SG formation (146); it promotes the assembly of SGs by binding to free RNA that accumulates upon stress and viral infections (84).”
Composition dependent thermodynamics of intracellular phase separation (2020, background): “U2OS G3BP1/2 KO cells were previously described (Kedersha et al., 2016).”
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., 2007), G3BP1 and G3BP2 (Kedersha et al., 2016), PRRC2C (Youn et al., 2018), CSDE1 (Youn et al., 2018), and UBAP2L (Markmiller et al., 2018).”
Principles and Properties of Stress granules (2016, background): “However, during osmotic stress G3BP1/2 and caprin are not required for stress granule formation [30].”
Competing protein-RNA interaction networks control multiphase intracellular organization (2020, positive): “Studies show that G3BP is dimeric, as is its isolated NTF2like domain (hereafter, NTF2) (Figures 1B and 2D; Guillén-Boixet et al., 2020; Kedersha et al., 2016; Kristensen, 2015; Panas et al., 2015; Yang et al., 2020; Tourrière et al., 2003; Vognsen et al., 2013).”
Intrinsically disordered regions contribute promiscuous interactions to RNP granule assembly (2017, background): “Some of the interactions that drive RNP granule assembly are well defined interactions between folded proteins, or folded protein domains and short linear motifs (SLiMs) (Decker et al., 2007; Jonas and Izaurralde, 2013; Kedersha et al., 2016; Ling et al., 2008; Mitrea et al., 2016; Tourriere, 2003).”
The stress granule transcriptome reveals principles of mRNA accumulation in stress granules (2017, positive): “Moreover, in DD G3BP1/2 U-2 OS cells, which fail to form SGs under arsenite treatment (Kedersha et al., 2016), we no longer observe the clustering of SG-enriched mRNAs by smFISH (Figure S2B).”