Control of the Translational Efficiency of β-ATPase mRNA Depends on the Regulation of a Protein That Binds the 3′ Untranslated Region of the mRNA

Izquierdo, José María; Cuezva, J M

doi:10.1128/mcb.17.9.5255

Cited by 89 publications

(170 citation statements)

References 72 publications

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“…5). Post-transcriptional regulation is not limited to changes in message stability, and sequences within the 3Ј-UTR of mRNAs have also been shown to be important for enhancing message translation as well as for translational silencing (45,75,76). Because the 3Ј-UTR of murine cox-2 also contains multiple regulatory elements that alter message stability and translational efficiency (45), results from the assay system we employed for the present study collectively reflect post-transcriptional regulatory mechanisms but do not differentiate translational efficiency or translational silencing from message stabilization.…”

Section: Discussionmentioning

confidence: 99%

Myeloid Differentiation Factor 88-dependent Post-transcriptional Regulation of Cyclooxygenase-2 Expression by CpG DNA

Yeo

Yoon

2003

Journal of Biological Chemistry

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The immune stimulatory unmethylated CpG motifs present in bacterial DNA (CpG DNA) induce expression of cyclooxygenase-2 (cox-2). The present study demonstrates that CpG DNA can up-regulate cox-2 expression by post-transcriptional mechanisms in RAW264.7 cells. To determine the CpG DNA-mediated signaling pathway that post-transcriptionally regulates cox-2 expression, a cox-2 translational reporter (COX2-3-UTR-luciferase) was generated by inserting sequences within the 3-untranslated region (UTR) of cox-2 to the 3 end of the luciferase gene under control of the SV40 promoter. CpG DNA-induced COX2-3-UTR-luciferase activity was completely inhibited by an endosomal acidification inhibitor chloroquine, a Toll-like receptor 9 antagonist inhibitory CpG DNA, or overexpression of a dominant negative (DN) form of MyD88. However, overexpression of DN-IRAK-1 or DN-TRAF6 resulted in substantial, but not complete, inhibition of the CpG DNA-induced COX2-3-UTR-luciferase activity. Activation of all three MAPKs (ERK, p38, and JNK) was required for optimal COX2-3-UTR-luciferase activity induced by CpG DNA.

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Section: Discussionmentioning

confidence: 99%

Myeloid Differentiation Factor 88-dependent Post-transcriptional Regulation of Cyclooxygenase-2 Expression by CpG DNA

Yeo

Yoon

2003

Journal of Biological Chemistry

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“…The localization of mRNAs also exerts a fundamental role in the regulation of gene expression (Martin and Ephrussi, 2009). Mechanisms that control the localization (Lithgow et al, 1997;Marc et al, 2002) and translation (de Heredia et al, 2000;Izquierdo and Cuezva, 1997;Martinez-Diez et al, 2006) of nucleus-encoded mRNAs of mitochondria have been shown to define the bioenergetic phenotype of the cell. The sorting of mRNAs to the vicinity of mitochondria is a conserved feature in both yeast and mammalian cells (Lithgow et al, 1997;Sylvestre et al, 2003b) affecting those mRNAs that encode core components of mitochondrial complexes Marc et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Human G3BP1 interacts with β-F1-ATPase mRNA and inhibits its translation

Ortega

Willers

Sala

et al. 2010

Journal of Cell Science

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SummaryThe post-transcriptional regulation of nuclear mRNAs that encode core components of mitochondria has relevant implications in cell physiology. The mRNA that encodes the catalytic subunit of the mitochondrial H + -ATP synthase subunit (ATP5B, -F1-ATPase) is localized in a large ribonucleoprotein (RNP) complex (-F1-RNP), which is subjected to stringent translational control during development and the cell cycle, and in carcinogenesis. Because downregulation of -F1-ATPase is a conserved feature of most prevalent human carcinomas, we have investigated the molecular composition of the human -F1-RNP. By means of an improved affinity-chromatography procedure and protein sequencing we have identified nine RNA-binding proteins (RNABPs) of the -F1-RNP. Immunoprecipitation assays of Ras-GAP SH3 binding protein 1 (G3BP1) and fluorescent in-situ hybridization of mRNA indicate a direct interaction of the endogenous G3BP1 with mRNA of -F1-ATPase (-F1 mRNA). RNA-bridged trimolecular fluorescence complementation (TriFC) assays confirm the interaction of G3BP1 with the 3Ј-UTR of -F1 mRNA in cytoplasmic RNA-granules. Confocal and high-resolution immunoelectron-microscopy experiments suggest that the -F1-RNP is sorted to the periphery of mitochondria. Molecular and functional studies indicate that the interaction of G3BP1 with -F1 mRNA inhibits its translation at the initiation level, supporting a role for G3BP1 in the glycolytic switch that occurs in cancer.

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“…But putatively the di erent HMGA1 3'UTR regions may be involved in post-transcriptional processes regulating the expression of HMGA1. Conceivably they can promote degradation similar to the elements within the 3'UTR of HMGA2 or they can provide target sites for RNA-binding proteins that activate (Fajardo et al, 1997) or inhibit (Izquierdo and Cuezva, 1997) translation. But further experiments will have to be done to ®nd out more about the function of the putative regulatory elements within the 3'UTR of both HMGA genes.…”

Section: Introductionmentioning

confidence: 99%