G3BP1 Depletion Increases Radiosensitisation by Inducing Oxidative Stress in Response to DNA Damage

Cho, Eugene; Than, Thoa Thi; Kim, Su-Hyeon; Park, Eun‐Ran; Kim, Mi‐Yeon; Lee, Kee Ho; Shin, Hyun Jin

doi:10.21873/anticanres.13816

Cited by 19 publications

(19 citation statements)

References 30 publications

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“…MS-based protein interactome studies demonstrated that SLU7 interacts with components of the SGs in unstressed conditions, both in vivo and in vitro. Moreover, we found that SLU7 is necessary to secure SG formation upon stress induction, as SLU7 is required to maintain the expression of the SG core components G3BP1 and USP10 (28), which in turn also have antioxidant capacity (30,31). While the specific mechanisms involved in the stabilization of SG components by SLU7 remain to be fully elucidated, we revealed that USP10 antioxidant function controls HNF4 stability, and that upon liver damage SLU7 haploinsufficiency results in USP10 downregulation.…”

Section: Accepted Articlementioning

confidence: 86%

Splicing Factor SLU7 Prevents Oxidative Stress‐Mediated Hepatocyte Nuclear Factor 4α Degradation, Preserving Hepatic Differentiation and Protecting From Liver Damage

et al. 2021

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Section: Accepted Articlementioning

confidence: 86%

Splicing Factor SLU7 Prevents Oxidative Stress‐Mediated Hepatocyte Nuclear Factor 4α Degradation, Preserving Hepatic Differentiation and Protecting From Liver Damage

et al. 2021

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“…G3BP1 enhances the resistance of sunitinibresistance RCC (128). This suggests that targeting G3BP1 may prove to be an effective therapeutic strategy for RCC (129).…”

Section: G3bp Regulates Kidney Cancermentioning

confidence: 98%

Research Progress on the Structure and Function of G3BP

et al. 2021

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Ras-GTPase-activating protein (SH3 domain)-binding protein (G3BP) is an RNA binding protein. G3BP is a key component of stress granules (SGs) and can interact with many host proteins to regulate the expression of SGs. As an antiviral factor, G3BP can interact with viral proteins to regulate the assembly of SGs and thus exert antiviral effects. However, many viruses can also use G3BP as a proximal factor and recruit translation initiation factors to promote viral proliferation. G3BP regulates mRNA translation and attenuation to regulate gene expression; therefore, it is closely related to diseases, such as cancer, embryonic death, arteriosclerosis, and neurodevelopmental disorders. This review discusses the important discoveries and developments related G3BP in the biological field over the past 20 years, which includes the formation of SGs, interaction with viruses, stability of RNA, and disease progression.

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“…G3BP1 depletion increases Bax protein levels and consequently cell apoptosis, therefore identifying G3BP1 as a potential target for sensitizing cancer cells to chemotherapy. Moreover, G3BP1 depletion sensitizes human NSCLC cell lines to radiationinduced cell death by impairing both ROS scavenging and DNA repair [68].…”

Section: Open Accessmentioning

confidence: 99%

Cancer cell adaptability: turning ribonucleoprotein granules into targets

et al. 2021

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Stress granules (SGs) and processing bodies (P-bodies) are membraneless cytoplasmic condensates of ribonucleoproteins (RNPs). They both regulate RNA fate under physiological and pathological conditions, and are thereby involved in the regulation and maintenance of cellular integrity. During tumorigenesis, cancer cells use these granules to thrive, to adapt to the harsh conditions of the tumor microenvironment (TME), and to protect themselves from anticancer treatments. This ability to provide multiple outcomes not only makes RNP granules promising targets for cancer therapy but also emphasizes the need for more knowledge about the biology of these granules to achieve clinical use. In this review we focus on the role of RNP granules in cancer, and on how their composition and regulation might be used to elaborate therapeutic strategies. RNP granules between stress and translationRegulating the expression of the genomic information is crucial to ensure cell identity and functionality. During transformation into cancer cells and throughout tumor progression, cells dynamically modulate the expression of their genomic information to adapt to environmental cues. Control of mRNA translation ensures the spatiotemporal adjustment of protein synthesis, and is often dysregulated in cancer cells to favor their adaptability [1]. In particular, regulation of translation initiation allows cancer cells to reprogram this activity towards essential mRNAs, such as those encoding oncogenes, to facilitate cell growth, proliferation, and survival [2]. Moreover, cancer cells must adapt to stress conditions in the TME, mainly through activation of the integrated stress response (ISR) [3,4] (Figure 1). This pathway controls translation initiation through eukaryotic initiation factor 2 (eIF2), which, once phosphorylated on its α subunit, prevents the formation of the ternary complex (eIF2:GTP: methionyl-initiator-tRNA) and consequently blocks translation initiation [5]. Four stress-sensor kinases can induce eIF2α phosphorylation, namely the PKR-like endoplasmic reticulum kinase (PERK), general control nonrepressible 2 (GCN2), heme-regulated inhibitor (HRI), and protein kinase R (PKR). The outcome of ISR activation is a global decrease in protein synthesis, while sparing the translation of some specific mRNAs such as that of transcription factor ATF4 [4]. Activation of this pathway, and the resulting selective translation, favor tumor progression following endoplasmic reticulum stress caused for instance by the hypoxic TME [6]. Furthermore, ISR activation by aberrant MYC expression enables cancer cells to adapt to this intrinsic stress by reprogramming translational programs. Consequently, the ISR prevents cancer cells from entering apoptosis and promotes both tumor progression [7,8] and escape from antitumor immunity [9,10].

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G3BP1 Depletion Increases Radiosensitisation by Inducing Oxidative Stress in Response to DNA Damage

Cited by 19 publications

References 30 publications

Splicing Factor SLU7 Prevents Oxidative Stress‐Mediated Hepatocyte Nuclear Factor 4α Degradation, Preserving Hepatic Differentiation and Protecting From Liver Damage

Splicing Factor SLU7 Prevents Oxidative Stress‐Mediated Hepatocyte Nuclear Factor 4α Degradation, Preserving Hepatic Differentiation and Protecting From Liver Damage

Research Progress on the Structure and Function of G3BP

Cancer cell adaptability: turning ribonucleoprotein granules into targets

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