Involvement of hGLD-2 in cytoplasmic polyadenylation of human p53 mRNA

Glahder, Jacob; Norrild, Bodil

doi:10.1111/j.1600-0463.2011.02804.x

Cited by 10 publications

(9 citation statements)

References 30 publications

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“…PAPD1 was also reported to uridylate histone mRNA along with PAPD5 to target it for degradation [123] although the actual PAP that uridylates histone mRNA is somewhat controversial [124]. hGLD2 (PAPD4) is a cytoplasmic PAP that polyadenylates short (A)‐tailed mRNAs in the cytoplasm [125,126] and is involved in diverse functions such as embryonic development, cell cycle, germline maturation, synaptic plasticity, learning and memory [126–131]. hGLD2 also polyadenylates p53 mRNA in the cytoplasm [128,132].…”

Section: Poly(a) Polymerase (Pap)mentioning

confidence: 99%

“…hGLD2 (PAPD4) is a cytoplasmic PAP that polyadenylates short (A)‐tailed mRNAs in the cytoplasm [125,126] and is involved in diverse functions such as embryonic development, cell cycle, germline maturation, synaptic plasticity, learning and memory [126–131]. hGLD2 also polyadenylates p53 mRNA in the cytoplasm [128,132]. hGLD2 targets mRNAs containing a cytoplasmic polyadenylation element (CPE) at the 3′‐UTR that is recognised by the regulatory protein CPEB (CPE binding protein).…”

Section: Poly(a) Polymerase (Pap)mentioning

confidence: 99%

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Poly(A) polymerase (PAP) diversity in gene expression – Star‐PAP vs canonical PAP

Laishram

2014

FEBS Letters

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Almost all eukaryotic mRNAs acquire a poly(A) tail at the 3′‐end by a concerted RNA processing event: cleavage and polyadenylation. The canonical PAP, PAPα, was considered the only nuclear PAP involved in general polyadenylation of mRNAs. A phosphoinositide‐modulated nuclear PAP, Star‐PAP, was then reported to regulate a select set of mRNAs in the cell. In addition, several non‐canonical PAPs have been identified with diverse cellular functions. Further, canonical PAP itself exists in multiple isoforms thus illustrating the diversity of PAPs. In this review, we compare two nuclear PAPs, Star‐PAP and PAPα with a general overview of PAP diversity in the cell. Emerging evidence suggests distinct niches of target pre‐mRNAs for the two PAPs and that modulation of these PAPs regulates distinct cellular functions.

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Section: Poly(a) Polymerase (Pap)mentioning

confidence: 99%

Section: Poly(a) Polymerase (Pap)mentioning

confidence: 99%

Poly(A) polymerase (PAP) diversity in gene expression – Star‐PAP vs canonical PAP

Laishram

2014

FEBS Letters

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“…MTPAP is a mitochondorial PAP, which regulates stability of mitochondrial mRNAs ( Tomecki et al, 2004 ; Nagaike et al, 2005 ). TENT2 adenylates selected mRNAs and miRNAs in cytoplasm ( Kwak et al, 2004 ; Nagaike et al, 2005 ; Katoh et al, 2009 ; Glahder and Norrild, 2011 ; D’Ambrogio et al, 2012 ), while TENT4A and TENT4B add poly(A) to various classes of nuclear RNAs and involve in RNA degradation as a subunit of a TRAMP-like complex ( Berndt et al, 2012 ; Ogami et al, 2013 ; Sudo et al, 2016 ). TENT4A and TENT4B have also recently been shown to be responsible for mRNA guanylylation ( Lim et al, 2018 ).…”

Section: Introductionmentioning

confidence: 99%

Function and Regulation of Human Terminal Uridylyltransferases

Yashiro

Tomita

2018

Front. Genet.

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RNA uridylylation plays a pivotal role in the biogenesis and metabolism of functional RNAs, and regulates cellular gene expression. RNA uridylylation is catalyzed by a subset of proteins from the non-canonical terminal nucleotidyltransferase family. In human, three proteins (TUT1, TUT4, and TUT7) have been shown to exhibit template-independent uridylylation activity at 3′-end of specific RNAs. TUT1 catalyzes oligo-uridylylation of U6 small nuclear (sn) RNA, which catalyzes mRNA splicing. Oligo-uridylylation of U6 snRNA is required for U6 snRNA maturation, U4/U6-di-snRNP formation, and U6 snRNA recycling during mRNA splicing. TUT4 and TUT7 catalyze mono- or oligo-uridylylation of precursor let-7 (pre–let-7). Let-7 RNA is broadly expressed in somatic cells and regulates cellular proliferation and differentiation. Mono-uridylylation of pre–let-7 by TUT4/7 promotes subsequent Dicer processing to up-regulate let-7 biogenesis. Oligo-uridylylation of pre–let-7 by TUT4/7 is dependent on an RNA-binding protein, Lin28. Oligo-uridylylated pre–let-7 is less responsive to processing by Dicer and degraded by an exonuclease DIS3L2. As a result, let-7 expression is repressed. Uridylylation of pre–let-7 depends on the context of the 3′-region of pre–let-7 and cell type. In this review, we focus on the 3′ uridylylation of U6 snRNA and pre-let-7, and describe the current understanding of mechanism of activity and regulation of human TUT1 and TUT4/7, based on their crystal structures that have been recently solved.

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“…Gld2 enzymes acquire substrate specificity by interacting with RNA-binding proteins and are recruited to only a subset of mRNAs [20]. Previous studies have mostly focused on the effect of Gld2 on mRNA.…”

Section: Introductionmentioning

confidence: 99%

HBx Down-Regulated Gld2 Plays a Critical Role in HBV-Related Dysregulation of miR-122

et al. 2014

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miR-122 is a liver-rich-specific microRNA that plays an important role in hepatic gene expression via post-transcription regulation, and it is potentially associated with the development of hepatocellular carcinoma. It has been confirmed that miR-122 is down-regulated during HBV infection; however, how HBV affects miR-122 is still debated. One research provided evidence that HBx could reduce the miR-122 transcription level, but the other insisted that HBV had no significant effect on miR-122 transcription level but reduce miR-122 level via binding and sequestering endogenous miR-122. It is determinate that Gld2 could increase the specific miRNA stabilization by monoadenylation which was a post-transcription regulation. In this study, we aimed to investigate the mechanism of HBV-induced reduction of miR-122 and examine whether Gld2 is involved in it. According to the results of a microRNA microarray, we found miR-122 was the most down-regulated microRNA in HepG2.2.15 compared to HepG2. As revealed by qRT-PCR and western blotting analyses, both miR-122 and Gld2 levels were reduced in hepatic cell lines with expression of HBV or HBx but not other proteins of HBV, and over-expression of Gld2 could abolish the effect of HBV and HBx on the miR-122 level. What's more, both HBV and HBx have no significant effect on pre-miR-122 levels. And the dual-luciferase assay implicated that HBx could reduce the Gld2 promoter activity but had no significant effect on miR-122 promoter activity. In conclusion, HBx is a critical protein derived from HBV, which regulates miR-122 via down-regulating Gld2.

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Involvement of hGLD-2 in cytoplasmic polyadenylation of human p53 mRNA

Cited by 10 publications

References 30 publications

Poly(A) polymerase (PAP) diversity in gene expression – Star‐PAP vs canonical PAP

Poly(A) polymerase (PAP) diversity in gene expression – Star‐PAP vs canonical PAP

Function and Regulation of Human Terminal Uridylyltransferases

HBx Down-Regulated Gld2 Plays a Critical Role in HBV-Related Dysregulation of miR-122

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