Regulation of cytoplasmic mRNA decay

Schoenberg, Daniel R.; Maquat, Lynne E.

doi:10.1038/nrg3160

Cited by 550 publications

(608 citation statements)

References 119 publications

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“…It is known that phosphorylation regulates the binding and function of RNA-Bps (12). For example, TTP phosphorylation by MK2 downstream of p38 MAPK signaling facilitates TTP to degrade mRNA through inhibition of deadenylase (28).…”

Section: Discussionmentioning

confidence: 99%

“…It has been reported that the activity of RNA-Bps is regulated by the activation of mitogen-activated protein kinases (MAPKs), such as p38 MAPK downstream of various stimuli, including IL-1β and lipopolysaccharide (LPS) (11,12). The regulation of cytokine mRNA stability by RNA-Bps is particularly important because of their essential roles (such as for IL-6) in human disease.…”

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confidence: 99%

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Arid5a controls IL-6 mRNA stability, which contributes to elevation of IL-6 level in vivo

Masuda

Ripley

Nishimura

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

189

254

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Posttranscriptional regulation of IL-6 has been largely uncharacterized, with the exception of the ribonuclease Regnase-1, which prevents autoimmunity by destabilizing IL-6 mRNA. Here, we identified AT-rich interactive domain-containing protein 5A (Arid5a) as a unique RNA binding protein, which stabilizes IL-6 but not TNF-α mRNA through binding to the 3′ untranslated region of IL-6 mRNA. Arid5a was enhanced in macrophages in response to LPS, IL-1β, and IL-6. Arid5a deficiency inhibited elevation of IL-6 serum level in LPStreated mice and suppressed IL-6 levels and the development of T H 17 cells in experimental autoimmune encephalomyelitis. Importantly, Arid5a inhibited the destabilizing effect of Regnase-1 on IL-6 mRNA. These results indicate that Arid5a plays an important role in promotion of inflammatory processes and autoimmune diseases.immune regulation | RNA-protein complex

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Arid5a controls IL-6 mRNA stability, which contributes to elevation of IL-6 level in vivo

Masuda

Ripley

Nishimura

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

189

254

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“…This includes nanoparticlebased bio-barcode assay that detects protein and DNA with ultrahigh sensitivity [11][12][13][14][15] , and although shown highly sensitive and versatile, this method is yet to be widely used partly because of the use of a non-conventional light-scattering assay platform. Further, it is very difficult to reliably and sensitively detect 19-to 25-nucleotide-long miRNA targets because miRNA is easily degradable by RNase 16 . In this regard, the bio-barcode approach that detects a barcode DNA that is a surrogate for a miRNA target could be beneficial.…”

mentioning

confidence: 99%

Bio-barcode gel assay for microRNA

2014

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MicroRNA has been identified as a potential biomarker because expression level of microRNA is correlated with various cancers. Its detection at low concentrations would be highly beneficial for cancer diagnosis. Here, we develop a new type of a DNA-modified gold nanoparticle-based bio-barcode assay that uses a conventional gel electrophoresis platform and potassium cyanide chemistry and show this assay can detect microRNA at aM levels without enzymatic amplification. It is also shown that single-base-mismatched microRNA can be differentiated from perfectly matched microRNA and the multiplexed detection of various combinations of microRNA sequences is possible with this approach. Finally, differently expressed microRNA levels are selectively detected from cancer cells using the bio-barcode gel assay, and the results are compared with conventional polymerase chain reaction-based results. The method and results shown herein pave the way for practical use of a conventional gel electrophoresis for detecting biomolecules of interest even at aM level without polymerase chain reaction amplification.

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“…It has long been thought that nonsense-mediated mRNA decay (NMD), which drives selective destruction of aberrant or physiological mRNAs containing a premature termination codon (9)(10)(11), occurs during the first round of translation driven by the CBC (1). The above view, however, was recently challenged by two reports showing that NMD occurs in the cytoplasm, regardless of whether the CBC or eIF4E drives the first round of translation (12,13).…”

mentioning

confidence: 99%

eIF4AIII enhances translation of nuclear cap-binding complex–bound mRNAs by promoting disruption of secondary structures in 5′UTR

Choe

Ryu

Park

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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It has long been considered that intron-containing (spliced) mRNAs are translationally more active than intronless mRNAs (identical mRNA not produced by splicing). The splicing-dependent translational enhancement is mediated, in part, by the exon junction complex (EJC). Nonetheless, the molecular mechanism by which each EJC component contributes to the translational enhancement remains unclear. Here, we demonstrate the previously unappreciated role of eukaryotic translation initiation factor 4AIII (eIF4AIII), a component of EJC, in the translation of mRNAs bound by the nuclear cap-binding complex (CBC), a heterodimer of cap-binding protein 80 (CBP80) and CBP20. eIF4AIII is recruited to the 5′-end of mRNAs bound by the CBC by direct interaction with the CBCdependent translation initiation factor (CTIF); this recruitment of eIF4AIII is independent of the presence of introns (deposited EJCs after splicing). Polysome fractionation, tethering experiments, and in vitro reconstitution experiments using recombinant proteins show that eIF4AIII promotes efficient unwinding of secondary structures in 5′UTR, and consequently enhances CBC-dependent translation in vivo and in vitro. Therefore, our data provide evidence that eIF4AIII is a specific translation initiation factor for CBC-dependent translation.eIF4AIII | cap-binding complex | translation | CTIF | nonsense-mediated mRNA decay I n mammalian cells, translation initiation is driven by two major cap-binding proteins (CBPs). One is the nuclear cap-binding complex (CBC), which is a heterodimer of nuclear CBP80 and CBP20 (CBP80/20) (1), and the other is the eukaryotic translation initiation factor (eIF) 4E, which is a major cytoplasmic CBP (2). The CBC binds the 5′-cap structure of a newly synthesized mRNA in the nucleus and then directly interacts with an eIF4G-like scaffold protein called CBP80/20-dependent translation initiation factor (CTIF) (3). Because CTIF is mostly present on the cytoplasmic side of the nuclear envelope and is found in the nucleus (3), the interaction between the CBC and CTIF may occur either in the nucleus or during mRNA export through the nuclear pore complex. In the cytoplasm, at the 5′-end of mRNA, the CBC-CTIF complex recruits the eIF3 complex (4) and then the 40S small subunit of the ribosome, thereby directing the socalled "first" (or pioneer) round of translation (1).Translation of a CBC-bound mRNA precedes that of the eIF4E-bound mRNA, because the CBC-bound mRNA is a precursor form of the eIF4E-bound mRNA (5). The timing of the replacement of the CBC by eIF4E has not yet been elucidated; however, it is known that the replacement is mediated by the action of importin α/β in a translation-independent manner (6). The replaced eIF4E at the 5′-end of mRNA recruits a scaffold protein, eIF4GI or eIF4GII, which recruits eIF3 and eIF4AI/II and, eventually, the 40S ribosomal subunit. Then, the recruited 40S subunit scans the mRNA until it reaches the authentic translation initiation codon AUG. Efficient ribosome scanning requires either eIF4AI or e...

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Regulation of cytoplasmic mRNA decay

Cited by 550 publications

References 119 publications

Arid5a controls IL-6 mRNA stability, which contributes to elevation of IL-6 level in vivo

Arid5a controls IL-6 mRNA stability, which contributes to elevation of IL-6 level in vivo

Bio-barcode gel assay for microRNA

eIF4AIII enhances translation of nuclear cap-binding complex–bound mRNAs by promoting disruption of secondary structures in 5′UTR

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