RETRACTED: The RasGAP-associated endoribonuclease G3BP assembles stress granules

Tourrière, Hélène; Chébli, Karim; Zekri, Latifa; Courselaud, Brice; Blanchard, Jean Marie; Bertrand, Édouard; Tazi, Jamal

doi:10.1083/jcb.200212128

Cited by 816 publications

(1,104 citation statements)

References 22 publications

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“…Thus, both CDDP and OXP lead to a similar perturbation in energy metabolism. However, OXP and CDDP were rather different in their capacity to elicit the redistribution of G3BP-GFP (Tourriere et al, 2003) or GFP-LC3 (Kabeya et al, 2000) from a diffuse to a punctiform distribution, which indicates the formation of stress granules (Figures 4a and b) or autophagosomes (Figures 4c and d), respectively. This difference was particularly remarkable at early time points.…”

Section: Thapsigargin Restores Immunogenic Cancer Cell Death I Martinmentioning

confidence: 97%

Restoration of the immunogenicity of cisplatin-induced cancer cell death by endoplasmic reticulum stress

et al. 2010

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In contrast to other cytotoxic agents including anthracyclins and oxaliplatin (OXP), cisplatin (CDDP) fails to induce immunogenic tumor cell death that would allow to stimulate an anticancer immune response and hence to amplify its therapeutic efficacy. This failure to induce immunogenic cell death can be attributed to CDDP's incapacity to elicit the translocation of calreticulin (CRT) from the lumen of the endoplasmic reticulum (ER) to the cell surface. Here, we show that, in contrast to OXP, CDDP is unable to activate the protein kinase-like ER kinase (PERK)-dependent phosphorylation of the eukaryotic translation initiation factor 2a (eIF2a). Accordingly, CDDP also failed to stimulate the formation of stress granules and macroautophagy, two processes that only occur after eIF2a phosphorylation. Using a screening method that monitors the voyage of CRT from the ER lumen to the cell surface, we identified thapsigargin (THAPS), an inhibitor of the sarco/ER Ca 2 þ -ATPase as a molecule that on its own does not stimulate CRT exposure, yet endows CDDP with the capacity to do so. The combination of ER stress inducers (such as THAPS or tunicamycin) and CDDP effectively induced the translocation of CRT to the plasma membrane, as well as immunogenic cell death, although ER stress or CDDP alone was insufficient to induce CRT exposure and immunogenic cell death. Altogether, our results underscore the contribution of the ER stress response to the immunogenicity of cell death.

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Section: Thapsigargin Restores Immunogenic Cancer Cell Death I Martinmentioning

confidence: 97%

Restoration of the immunogenicity of cisplatin-induced cancer cell death by endoplasmic reticulum stress

et al. 2010

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“…We subjected HeLa cells to oxidative stress (through arsenite treatment), osmotic stress (through sorbitol treatment) or heat-shock stress and visualized SGs and PBs by staining for RasGAP SH3 domain binding protein (G3BP) 24 and DCP1A, respectively. ERG independently colocalized with both DCP1A and G3BP, thus indicating that it belongs to the set of common components shared between PBs and SGs (Fig.…”

Section: Erg Localizes To Pbs and Promotes Cytoplasmic Mrna Decaymentioning

confidence: 99%

The transcription factor ERG recruits CCR4–NOT to control mRNA decay and mitotic progression

Rambout

Detiffe

Bruyr

et al. 2016

Nat Struct Mol Biol

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nature structural & molecular biology advance online publication a r t i c l e sAlthough undisputable evidence has clearly demonstrated that the nuclear steps of mRNA processing are mechanistically linked to transcription, a conceptual evolution in gene regulation has come with the realization that transcription might also be functionally connected to more remote processes occurring in the cytoplasm, such as mRNA decay 1,2 . Cytoplasmic mRNA decay is initiated by deadenylation, a rate-limiting event during which the poly(A) tail of the transcript is trimmed off by the CCR4-NOT complex, the main deadenylation machinery in eukaryotes 3 . The degradation of specific mRNAs, a key process in the regulation of eukaryotic gene expression, is achieved through the recruitment of the CCR4-NOT complex by sequence-specific RNA-binding proteins (RBPs) or by the microRNA machinery 3,4 . Poly(A)-shortened mRNAs, along with factors involved in the deadenylation, decapping and mRNA-degradation machineries, accumulate in microscopic mRNA-protein complex (mRNP) aggregates called processing bodies (PBs) 5 .The idea of coupling between mRNA synthesis and degradation has recently emerged. Genome-wide expression studies in yeast have shown that mRNA synthesis and decay are mechanistically and functionally coordinated, thus supporting the existence of common molecular effectors [6][7][8][9] . In particular, the CCR4-NOT deadenylation complex was first described as a transcriptional regulator and has been implicated in initiation and elongation by RNA polymerase II 10,11 . More surprisingly, it has also been shown that degradation of yeast mRNAs is determined by cis-acting sequence elements in promoters 12,13 . These findings have led to the concept of mRNA imprinting, in which sequence-specific DNA-binding factors might orchestrate mRNA synthesis and decay. This decay would occur via loading of factors regulating cytoplasmic mRNA degradation onto the transcribing mRNA 14 . However, the identity of these DNA-binding mRNA coordinators is still obscure, and it remains to be tested whether such coupling between transcription and decay also exists in higher eukaryotes. E26 (Ets) proteins, a family of 28 helix-loop-helix transcription factors (TFs) in metazoans, are characterized by a highly conserved DNA-binding ETS domain 15 . Through this domain, Ets factors bind specific gene promoters and act as key regulators in many biological processes including cellular proliferation, apoptosis, differentiation and survival 16 . ERG, FLI1 and the more structurally divergent FEV compose the Erg subfamily of Ets factors and have been identified as driving factors in prostate cancer, Ewing's tumors and leukemias 15,17 . Using ERG as a paradigm, we sought to investigate the possibility that eukaryotic transcription factors might be directly involved in cytoplasmic mRNA decay. We demonstrate that ERG triggers degradation of mRNAs connected to Aurora signaling by recruiting RBPs and the CCR4-NOT deadenylation complex and that this activity is important fo...

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“…Nucleoli (Brangwynne et al , 2011), P granules (Brangwynne et al , 2009), and stress granules (Molliex et al , 2015; Patel et al , 2015), three membrane‐less organelles, were recently reported to have liquid droplet properties (Brangwynne, 2013), supporting a role for liquid–liquid phase separation in their formation (Li et al , 2012b; Nott et al , 2015; Patel et al , 2015). The recruitment of additional components to these bodies is not well understood but must involve protein/protein interactions (Tourrière et al , 2003). SPOP typically localizes to nuclear speckles (Nagai et al , 1997).…”

Section: Introductionmentioning

confidence: 99%

Higher‐order oligomerization promotes localization of SPOP to liquid nuclear speckles

et al. 2016

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Membrane‐less organelles in cells are large, dynamic protein/protein or protein/RNA assemblies that have been reported in some cases to have liquid droplet properties. However, the molecular interactions underlying the recruitment of components are not well understood. Herein, we study how the ability to form higher‐order assemblies influences the recruitment of the speckle‐type POZ protein (SPOP) to nuclear speckles. SPOP, a cullin‐3‐RING ubiquitin ligase (CRL3) substrate adaptor, self‐associates into higher‐order oligomers; that is, the number of monomers in an oligomer is broadly distributed and can be large. While wild‐type SPOP localizes to liquid nuclear speckles, self‐association‐deficient SPOP mutants have a diffuse distribution in the nucleus. SPOP oligomerizes through its BTB and BACK domains. We show that BTB‐mediated SPOP dimers form linear oligomers via BACK domain dimerization, and we determine the concentration‐dependent populations of the resulting oligomeric species. Higher‐order oligomerization of SPOP stimulates CRL3SPOP ubiquitination efficiency for its physiological substrate Gli3, suggesting that nuclear speckles are hotspots of ubiquitination. Dynamic, higher‐order protein self‐association may be a general mechanism to concentrate functional components in membrane‐less cellular bodies.

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RETRACTED: The RasGAP-associated endoribonuclease G3BP assembles stress granules

Cited by 816 publications

References 22 publications

Restoration of the immunogenicity of cisplatin-induced cancer cell death by endoplasmic reticulum stress

Restoration of the immunogenicity of cisplatin-induced cancer cell death by endoplasmic reticulum stress

The transcription factor ERG recruits CCR4–NOT to control mRNA decay and mitotic progression

Higher‐order oligomerization promotes localization of SPOP to liquid nuclear speckles

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