On the Intracellular Trafficking of Mouse S5 Ribosomal Protein from Cytoplasm to Nucleoli

Matragkou, Ch.; Papachristou, Helen; Karetsou, Zoe; Παπαδόπουλος, Γεώργιος; Papamarcaki, Thomais; Vizirianakis, Ioannis S.; Tsiftsoglou, Asterios S.; Choli‐Papadopoulou, Theodora

doi:10.1016/j.jmb.2009.07.049

Cited by 13 publications

(9 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“… 41 , 42 Casein kinase II could phosphorylate RPS5, which plays an important role in protein trafficking from cytoplasm to nucleoli. 43 In this study, we first confirmed the combination of M19 and RPS5 by a DARTS test in RAW264.7 cells. Since M19 displayed a significant inhibitory effect on osteoclastogenesis, probably RPS5 has a role in osteoclastogenesis.…”

Section: Discussionsupporting

confidence: 58%

RETRACTED ARTICLE: Matrine derivate MASM uncovers a novel function for ribosomal protein S5 in osteoclastogenesis and postmenopausal osteoporosis

et al. 2017

View full text Add to dashboard Cite

Postmenopausal osteoporosis (POMP) is a public health problem characterized by decreased bone density and increased fracture risk. Over-activated osteoclastogenesis plays a vital role in POMP. Here we developed a novel bioactive compound MASM (M19) based on sophocarpine. Although it showed no significant effects on osteogenesis and adipogenesis for bone marrow-derived mesenchymal stem cells (BMSCs) in vitro, it could significantly inhibit RANKL/M-CSF induced osteoclastogenesis through suppressing NF-κB, MAPKs and PI3K/Akt pathways in vitro and ameliorate bone loss in ovariectomized mice in vivo. Ribosomal protein s5 (RPS5) has been identified as a target of M19 and regulates PI3K/Akt, NF-κB and MAPKs pathways in osteoclastogenesis. Overexpressions of RPS5 synergistically inhibited osteoclastogenesis with M19 while silencing RPS5 compromised M19 inhibitory effects on osteoclastogenesis in vitro. Among the three pathways, Akt plays a major role in M19 effects. The Akt activator SC79 partially reversed the inhibitory effects on osteoclastogenesis by M19 and RPS5-knocking-down. It indicates that RPS5 serves as a potential candidate target for inhibiting osteoclastogenesis and osteoporosis therapy and M19 is a promising agent for POMP treatment.

show abstract

Section: Discussionsupporting

confidence: 58%

RETRACTED ARTICLE: Matrine derivate MASM uncovers a novel function for ribosomal protein S5 in osteoclastogenesis and postmenopausal osteoporosis

et al. 2017

View full text Add to dashboard Cite

show abstract

“…For example, RPS5 could interact with the hepatitis C virus and cricket paralysis virus internal ribosome entry site . It is phosphorylated by casein kinase II when not assembled into ribosome and the phosphorylation seems to regulate protein trafficking from cytoplasm to nucleoli . Interesting, RPS5 is tightly coupled with murine erythroleukemia cell differentiation .…”

Section: Discussionmentioning

confidence: 99%

Bioactive compound reveals a novel function for ribosomal protein S5 in hepatic stellate cell activation and hepatic fibrosis

Tian

et al. 2014

Hepatology

View full text Add to dashboard Cite

Liver fibrosis and its endstage, cirrhosis, represent a major public health problem worldwide. Activation of hepatic stellate cells (HSCs) is a central event in hepatic fibrosis. However, the proteins that control HSC activation are incompletely understood. Here we show that (6aS, 10S, 11aR, 11bR, 11cS)-10-methylamino-dodecahydro-3a, 7a-diazabenzo [de]anthracene-8-thione (MASM) exhibits potent inhibitory activity against liver fibrosis in vitro and in vivo associated with the reduction of Akt phosphorylation. Furthermore, ribosomal protein S5 (RPS5) was identified as a direct target of MASM, which stabilized RPS5 in cultured HSCs and in the liver of experimental animals after dimethylnitrosamine (DMN) or bile duct ligation (BDL). Functional studies revealed that RPS5 could prevent HSC activation. RPS5 overexpression in HSCs resulted in Akt dephosphorylation at both Ser473 and Thr308, and led to subsequent dephosphorylation of GSK3b or P70S6K. Progression of DMN-and BDL-induced hepatic fibrosis was aggravated by Rps5 knockdown and alleviated by RPS5 overexpression, which correlated with the modulation of Akt phosphorylation and HSC number in the fibrotic livers. Moreover, RPS5 was substantially reduced in the transdifferentiated HSCs, experimental fibrotic livers, and human cirrhosis samples. Conclusion: These results demonstrate that RPS5 is implicated in hepatic fibrogenesis and may represent a promising target for potential therapeutic intervention in liver fibrotic diseases. (HEPATOLOGY 2014;60:648-660)

show abstract

“…These results imply that EvpP might exert an influence on host macrophages by means of interaction with RPS5. RPS5, as an important component of ribosomes, forms part of the exit site on the small ribosomal subunit and cross-links to the exitsite tRNA (Matragkou et al, 2009). RPS5 is known for its involvement in ribosome biogenesis function, however its functions remain largely unknown.…”

Section: Discussionmentioning

confidence: 99%

“…The increasingly accumulated evidence suggests that ribosomal proteins has extra-ribosomal functions associated with cell differentiation, apoptosis, regulation of signal pathway, and DNA repair (LindstrÖm, 2009;Warner and Mcintosh, 2009). RPS5 was also found to participate in extra-ribosomal activities such as cell differentiation (Matragkou et al, 2008;Vizirianakis et al, 2015), intracellular trafficking (Matragkou et al, 2009), and hepatic fibrosis (Xu et al, 2016).…”

Section: Discussionmentioning

confidence: 99%

Roles of EvpP in Edwardsiella piscicida-Macrophage Interactions

Qin¹,

Wang²,

Gao³

et al. 2020

Front. Cell. Infect. Microbiol.

View full text Add to dashboard Cite

Edwardsiella piscicida is found to be an important facultative intracellular pathogen with a broad host range. These organisms can replicate and survive within host macrophages to escape from the subversion of the immune defense. E. piscicida-macrophage interaction is very important in determining the outcome of edwardsiellasis. As an effector protein of E. piscicida T6SS, EvpP has been determined to be a very important virulence factor for E. piscicida, although its precise role in E. piscicida-macrophage interactions is not yet clear. In this study, the roles of EvpP in E. piscicida-macrophage interactions were characterized. Here, we constructed the deletion mutants of evpP (evpP) and complementation (evpP-C) by the allelic exchange method. Compared to wild type strain (WT), evpP was found to be attenuated for growth within macrophages. In line with this observation, we found its survival capacity was lower than WT under oxidative and acid stress in vitro, which simulate conditions encountered in host macrophages. Attenuation of evpP also correlated with enhanced activation of macrophages, as reflected by augmented NO production in evpP-treated macrophages. Moreover, compared to WT, evpP induced markedly increased apoptosis of macrophages, characterized by increased Annexin V binding and the activation of cleaved caspase-3. These findings provided strong evidence that EvpP is involved in the process of E. piscicida-macrophage interactions and is required for its survival and replication in macrophages. Thus, we propose that EvpP might be an important factor that controlling the fate of E. piscicida inside macrophages. To further exploring the underlying mechanism of EvpP action, the cDNA library was constructed from E. piscicida-infected macrophages and a yeast two-hybrid screen was performed to search for cellular proteins interacting with EvpP. Ribosomal protein S5 (RPS5) was identified as a target of EvpP. Furthermore, the interaction was validated with co-immunoprecipitation assay. This result implies that the observed effect of EvpP on macrophages might be related to RPS5-mediated regulation, contributing to a better understanding of the mechanisms of EvpP involved in E. piscicida-macrophage interactions.

show abstract

On the Intracellular Trafficking of Mouse S5 Ribosomal Protein from Cytoplasm to Nucleoli

Cited by 13 publications

References 49 publications

RETRACTED ARTICLE: Matrine derivate MASM uncovers a novel function for ribosomal protein S5 in osteoclastogenesis and postmenopausal osteoporosis

RETRACTED ARTICLE: Matrine derivate MASM uncovers a novel function for ribosomal protein S5 in osteoclastogenesis and postmenopausal osteoporosis

Bioactive compound reveals a novel function for ribosomal protein S5 in hepatic stellate cell activation and hepatic fibrosis

Roles of EvpP in Edwardsiella piscicida-Macrophage Interactions

Contact Info

Product

Resources

About