c-Jun ARE Targets mRNA Deadenylation by an EDEN-BP (Embryo Deadenylation Element-binding Protein)-dependent Pathway

Paillard, Luc; Legagneux, Vincent; Maniey, Dominique; Osborne, Howard Beverley

doi:10.1074/jbc.m109362200

Cited by 54 publications

(42 citation statements)

References 33 publications

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“…We have shown above that this peptide has no effect on the slow default-type deadenylation (see Figure 4B). We also observed that it did not inhibit the AUUUA-dependent deadenylation, a rapid mechanism in Xenopus embryos that does not require active EDEN-BP (Voeltz and Steitz, 1998;Paillard et al, 2002) (data not shown). Hence, peptide 183-210 specifically inhibits the deadenylation of EDEN-containing transcripts in Xenopus embryos or extracts, but not other types of deadenylation.…”

Section: Figure 4 Peptide 183-210 Inhibits Eden-bp Oligomerization Anmentioning

confidence: 72%

“…Accordingly, two additional transcripts were used, the synthetic GbORF (globin open reading frame) and GbORFjun (GbORF containing the c-Jun ARE in the 3 -UTR) . The GbORF mRNA is a substrate for default deadenylation, whereas the GbORFjun mRNA is deadenylated by the EDEN-dependent process Paillard et al, 2002). As shown in Figure 5 (middle panel) the slow deadenylation of the GbORF mRNA injected into embryos was not affected by the co-injection of 200 ng of the 183-210 peptide.…”

Section: Figure 4 Peptide 183-210 Inhibits Eden-bp Oligomerization Anmentioning

confidence: 90%

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Oligomerization of EDEN‐BP is required for specific mRNA deadenylation and binding

Cosson

Gautier-Courteille

Maniey

et al. 2006

Biology of the Cell

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Background information. mRNA deadenylation [shortening of the poly(A) tail] is often triggered by specific sequence elements present within mRNA 3 untranslated regions and generally causes rapid degradation of the mRNA. In vertebrates, many of these deadenylation elements are called AREs (AU-rich elements). The EDEN (embryo deadenylation element) sequence is a Xenopus class III ARE. EDEN acts by binding a specific factor, EDEN-BP (EDEN-binding protein), which in turn stimulates deadenylation.Results. We show here that EDEN-BP is able to oligomerize. A 27-amino-acid region of EDEN-BP was identified as a key domain for oligomerization. A mutant of EDEN-BP lacking this region was unable to oligomerize, and a peptide corresponding to this region competitively inhibited the oligomerization of full-length EDEN-BP. Impairing oligomerization by either of these two methods specifically abolished EDEN-dependent deadenylation. Furthermore, impairing oligomerization inhibited the binding of EDEN-BP to its target RNA, demonstrating a strong coupling between EDEN-BP oligomerization and RNA binding.Conclusions. These data, showing that the oligomerization of EDEN-BP is required for binding of the protein on its target RNA and for EDEN-dependent deadenylation in Xenopus embryos, will be important for the identification of cofactors required for the deadenylation process.

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Section: Figure 4 Peptide 183-210 Inhibits Eden-bp Oligomerization Anmentioning

confidence: 72%

Section: Figure 4 Peptide 183-210 Inhibits Eden-bp Oligomerization Anmentioning

confidence: 90%

Oligomerization of EDEN‐BP is required for specific mRNA deadenylation and binding

Cosson

Gautier-Courteille

Maniey

et al. 2006

Biology of the Cell

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“…Maternal mRNAs encoding cell cycle proteins such as cdc25A (Kim et al, 1999) and XChk1 (Kappas et al, 2000) and other proteins such as c-mos and aurora A (Eg2) are also destabilized after the MBT. c-mos and aurora A mRNA are deadenylated before the MBT in an EDEN-BP-dependent manner (Paillard et al, 1998(Paillard et al, , 2002) that does not require zygotic transcription. The adenylation behavior of cdc25A and XChk1 has not been studied in Xenopus, thus they remain potential targets for zygote-mediated deadenylation.…”

Section: Discussionmentioning

confidence: 99%

“…C-rich elements have been shown recently to control poly(A) addition of the maternal mRNA encoding the phosphatase PP2A (Paillard et al, 2000), whereas BMP-7 mRNA is polyadenylated and translated in early embryos even though its 3ЈUTR does not contain known polyadenylation elements (Fritz and Sheets, 2001). The embryonic deadenylation element (EDEN), an UG/UA rich sequence, and its binding protein EDEN-BP trigger the deadenylation of several maternal mRNAs immediately after fertilization, including c-mos and c-jun (Paillard et al, 1998(Paillard et al, , 2002. AU-rich elements (AREs), which destabilize cytokine mRNAs in somatic cells, also act as deadenylation elements in early frog embryos (Voeltz and Steitz, 1998).…”

Section: Introductionmentioning

confidence: 99%

Zygotic control of maternal cyclin A1 translation and mRNA stability

Audic

Garbrecht

Fritz

et al. 2002

Developmental Dynamics

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Cyclin mRNAs are unstable in the adult cell cycle yet are stable during the first 12 cell divisions in Xenopus laevis. We recently reported that cyclin A1 and B2 maternal mRNAs are deadenylated upon completion of the 12th division (Audic et al. [2001] Mol. Cell Biol. 21: 1662-1671). Deadenylation is mediated by the 3 untranslated region (UTR) of the mRNA and precedes the terminal disappearance of the cyclin proteins, with both processes requiring zygotic transcription. The purpose of the current study was (1) to ask whether deadenylation leads to translational repression and/or destabilization of endogenous cyclin A1 and B2 mRNAs, and (2) to further characterize the regulatory sequences required. We show that zygote-driven deadenylation leads to translational repression and mRNA destabilization. A 99-nucleotide region of the 3UTR of the cyclin A1 mRNA mediates both deadenylation and destabilization. Surprisingly, two AU-rich consensus elements within this region are dispensable for this activity. These results suggest that zygote-dependent deadenylation, translational repression, and mRNA destabilization by means of novel 3UTR elements contribute to the disappearance of maternal cyclins. They also suggest that translational control of cyclins may play a role in the transition to the adult cell cycle. These data concur with previous studies in Drosophila showing that zygote-mediated degradation of maternal cdc25 mRNA may be a general mechanism whereby transition to the adult cell cycle proceeds.

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“…CUG-BP is localized to both the nucleus and the cytoplasm (Mukhopadhyay et al, 2003;Roberts et at., 1997) and can functionally replace EDEN-BP to promote deadenylation in Xenopus embryo extracts (Paillard et al, 2003). Furthermore, the human c-jun mRNA can be rapidly deadenylated by an EDEN-BP specific pathway upon injection into Xenopus embryos (Paillard et al, 2002). This conservation of key sequence elements and protein domains, therefore, makes it very likely that CUG-BP regulates poly(A) tail shortening in mammalian cells.…”

Section: Introductionmentioning

confidence: 99%

CUG-BP and 3'UTR sequences influence PARN-mediated deadenylation in mammalian cell extracts

Moraes

Wilusz

2007

Genet. Mol. Biol.

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Several mRNAs have been shown to exhibit distinct patterns of poly(A) shortening prior to their decay in vivo. In this study, we show that individual transcripts also demonstrate distinct patterns of deadenylation in in vitro systems derived from HeLa and Jurkat T cell cytoplasmic extracts. The major patterns observed were slow/synchronous and fast/asynchronous poly(A) tail shortening. For all RNA substrates tested, PARN was shown to be the enzyme responsible for the deadenylation patterns that were observed. Sequences in the 3' untranslated regions influenced the deadenylation pattern. Using a fragment of the 3'UTR of the c-fos mRNA as a model, the interaction of CUG-BP, the human homolog of EDEN-BP -a protein previously implicated in regulated deadenylation in Xenopus oocyteswas shown to be associated with changes in PARN-mediated deadenylation patterns. Our results suggest that association of CUG-BP with 3'UTR sequences can modulate the activity of the PARN deadenylase in mammalian cell extracts.

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c-Jun ARE Targets mRNA Deadenylation by an EDEN-BP (Embryo Deadenylation Element-binding Protein)-dependent Pathway

Cited by 54 publications

References 33 publications

Oligomerization of EDEN‐BP is required for specific mRNA deadenylation and binding

Oligomerization of EDEN‐BP is required for specific mRNA deadenylation and binding

Zygotic control of maternal cyclin A1 translation and mRNA stability

CUG-BP and 3'UTR sequences influence PARN-mediated deadenylation in mammalian cell extracts

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