Specific PABP effect on translation of<i>YB-1</i>mRNA is neutralized by polyadenylation through a “mini-loop” at 3′ UTR

Eliseeva, Irina A.; Ovchinnikov, Lev P.; Lyabin, Dmitry N.

doi:10.4161/rna.22711

Cited by 9 publications

(9 citation statements)

References 56 publications

(63 reference statements)

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“…Hence, we hypothesize that RALY exerts a transcriptional control of these targets. Since the 3΄UTRs act as a scaffold where many proteins and microRNAs form complexes for post-transcriptional and/or translational regulation (81,82), RALY might compete or cooperate with one or more of these factors in regulating the level of these specific transcripts. RNA binding proteins can be recruited to promoter regions during transcription and they can interact with RNA polymerase II as well as with transcription factors and then bind to the nascent RNA (83).…”

Section: Discussionmentioning

confidence: 99%

Identification and dynamic changes of RNAs isolated from RALY-containing ribonucleoprotein complexes

Rossi

Moro

Tebaldi

et al. 2017

Nucleic Acids Research

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RALY is a member of the heterogeneous nuclear ribonucleoprotein family (hnRNP), a large family of RNA-binding proteins involved in many aspects of RNA metabolism. Although RALY interactome has been recently characterized, a comprehensive global analysis of RALY-associated RNAs is lacking and the biological function of RALY remains elusive. Here, we performed RIP-seq analysis to identify RALY interacting RNAs and assessed the role of RALY in gene expression. We demonstrate that RALY binds specific coding and non-coding RNAs and associates with translating mRNAs of mammalian cells. Among the identified transcripts, we focused on ANXA1 and H1FX mRNAs, encoding for Annexin A1 and for the linker variant of the histone H1X, respectively. Both proteins are differentially expressed by proliferating cells and are considered as markers for tumorigenesis. We demonstrate that cells lacking RALY expression exhibit changes in the levels of H1FX and ANXA1 mRNAs and proteins in an opposite manner. We also provide evidence for a direct binding of RALY to the U-rich elements present within the 3΄UTR of both transcripts. Thus, our results identify RALY as a poly-U binding protein and as a regulator of H1FX and ANXA1 in mammalian cells.

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Section: Discussionmentioning

confidence: 99%

Identification and dynamic changes of RNAs isolated from RALY-containing ribonucleoprotein complexes

Rossi

Moro

Tebaldi

et al. 2017

Nucleic Acids Research

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“…Importantly, this effect was observed for unpolyadenylated YB‐1 mRNA only. In the case of poly(A) + YB‐1 mRNA, the poly(A) tail interacts with the RE and prevents the positive effect of PABP . In contrast, another poly(A)‐binding protein, hnRNPQ, competes with PABP and either promotes YB‐1 binding or does not preclude from it, which, in turn, results in translation inhibition …”

Section: Yb‐1 Synthesis Regulationmentioning

confidence: 99%

“…In the case of poly(A) + YB-1 mRNA, the poly(A) tail interacts with the RE and prevents the positive effect of PABP. 110 In contrast, another poly(A)-binding protein, hnRNPQ, competes with PABP and either promotes YB-1 binding or does not preclude from it, which, in turn, results in translation inhibition. 111 The YB-1 mRNA 5 UTR contains a sequence(s) ensuring translational sensitivity to the mTORC1 signaling pathway.…”

Section: Yb-1 Synthesis Regulationmentioning

confidence: 99%

YB‐1 protein: functions and regulation

2013

Self Cite

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The Y-box binding protein 1 (YB-1, YBX1) is a member of the family of DNA- and RNA-binding proteins with an evolutionarily ancient and conserved cold shock domain. It falls into a group of intrinsically disordered proteins that do not follow the classical rule 'one protein-one function' but introduce a novel principle stating that a disordered structure suggests many functions. YB-1 participates in a wide variety of DNA/RNA-dependent events, including DNA reparation, pre-mRNA transcription and splicing, mRNA packaging, and regulation of mRNA stability and translation. At the cell level, the multiple activities of YB-1 are manifested as its involvement in cell proliferation and differentiation, stress response, and malignant cell transformation. WIREs RNA 2014, 5:95-110. doi: 10.1002/wrna.1200 CONFLICT OF INTEREST: The authors have declared no conflicts of interest for this article. For further resources related to this article, please visit the WIREs website.

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“…Through an unbiased RNAi screen, we have identified pAbp, Drosophila ortholog of the cytoplasmic Poly(A)-binding protein (PABP-C) as an RBP that is required for Wnd-induced upregulation of Dscam expression as well as for Wnd-induced axon arborization. Although PABP-C is considered as a general activator of protein translation through poly(A) tail interaction (Munroe and Jacobson, 1990); it also performs gene-specific posttranscriptional regulations (Wu and Bag, 1998;Lyabin et al, 2011;Vazquez-Pianzola et al, 2011;Eliseeva et al, 2012;Iwakawa et al, 2012;Smith et al, 2017). We identified an adenine nucleotide rich (A-rich) region in the 39UTR of Dscam that mediates pAbp interaction.…”

Section: Introductionmentioning

confidence: 99%

Dual Leucine Zipper Kinase Regulates Dscam Expression through a Noncanonical Function of the Cytoplasmic Poly(A)-Binding Protein

Singh

Kim

2022

J. Neurosci.

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Dual leucine zipper kinase (DLK) plays a pivotal role in the development, degeneration, and regeneration of neurons. DLK can regulate gene expression post-transcriptionally, but the underlying mechanism remains poorly understood. The Drosophila DLK, Wallenda (Wnd), regulates the expression of Down syndrome cell adhesion molecule (Dscam) to control presynaptic arbor growth. This regulation is mediated by the 39 untranslated region (39UTR) of Dscam mRNA, which suggests that RNA binding proteins (RBPs) mediate DLK function. We performed a genome-wide cell-based RNAi screen of RBPs and identified the cytoplasmic poly(A)-binding protein, pAbp, as an RBP that mediates Wnd-induced increase in Dscam expression. Genetic analysis shows that Wnd requires pAbp for promoting presynaptic arbor growth and for enhancing Dscam expression. Our analysis revealed that Dscam mRNAs harbor short poly(A) tails. We identified a region in Dscam 39UTR that specifically interacts with pAbp. Removing this region significantly reduced Wnd-induced increase in Dscam expression. These suggest that a noncanonical interaction of PABP with the 39UTR of target transcripts is essential for DLK functions.

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Specific PABP effect on translation ofYB-1mRNA is neutralized by polyadenylation through a “mini-loop” at 3′ UTR

Cited by 9 publications

References 56 publications

Identification and dynamic changes of RNAs isolated from RALY-containing ribonucleoprotein complexes

Identification and dynamic changes of RNAs isolated from RALY-containing ribonucleoprotein complexes

YB‐1 protein: functions and regulation

Dual Leucine Zipper Kinase Regulates Dscam Expression through a Noncanonical Function of the Cytoplasmic Poly(A)-Binding Protein

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