Recruitment of the human TREX complex to mRNA during splicing

Masuda, Seiji; Das, Rita; Cheng, Hong; Hurt, Ed; Dorman, N.; Reed, Robin

doi:10.1101/gad.1302205

Cited by 402 publications

(557 citation statements)

References 35 publications

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“…The gH and gL genes of RRV, like most other RRV genes, do not have introns that are spliced out during mRNA processing. It has been shown that TREX and the exon-junction complex (EJC) binds onto mRNA in a splicing-dependent manner to facilitate the efficient nuclear export of spliced mRNAs in eukaryotic cells (19,23,31). We asked whether the lack of appropriate ribonucleoprotein (RNP), due to a lack of splicing, was responsible for the poor expression of gH and gL mRNAs.…”

Section: Resultsmentioning

confidence: 99%

Rhesus Monkey Rhadinovirus ORF57 Induces gH and gL Glycoprotein Expression through Posttranscriptional Accumulation of Target mRNAs

Shin

Desrosiers

2011

J Virol

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Open reading frame 57 (ORF57) of gamma-2 herpesviruses is a key regulator of viral gene expression. It has been reported to enhance the expression of viral genes by transcriptional, posttranscriptional, or translational activation mechanisms. Previously we have shown that the expression of gH and gL of rhesus monkey rhadinovirus (RRV), a close relative of the human Kaposi's sarcoma-associated herpesvirus (KSHV), could be dramatically rescued by codon optimization as well as by ORF57 coexpression (J. P. Bilello, J. S. Morgan, and R. C. Desrosiers, J. Virol. 82:7231-7237, 2008). We show here that ORF57 coexpression and codon optimization had similar effects, except that the rescue of expression by codon optimization was temporally delayed relative to that of ORF57 coexpression. The transfection of gL mRNA directly into cells with or without ORF57 coexpression and with or without codon optimization recapitulated the effects of these modes of induction on transfected DNA. These findings suggested an important role for the enhancement of mRNA stability and/or the translation of mRNA for these very different modes of induced expression. This conclusion was confirmed by several different measures of gH and gL mRNA stability and accumulation with or without ORF57 coexpression and with or without codon optimization. Our results indicate that RRV gH and gL expression is severely limited by the stability of the mRNA and that ORF57 coexpression and codon optimization independently induce gH and gL expression principally by allowing accumulation and translation of these mRNAs.

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Section: Resultsmentioning

confidence: 99%

Rhesus Monkey Rhadinovirus ORF57 Induces gH and gL Glycoprotein Expression through Posttranscriptional Accumulation of Target mRNAs

Shin

Desrosiers

2011

J Virol

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“…In mammals, the TREX complex is recruited primarily to the 5 0 end of transcripts through cooperative action of the nuclear cap-binding complex and the spliceosome [16,17]. Once bound to the mRNA, the TREX complex promotes nuclear export of fully processed transcripts through the nuclear pore by direct interactions between the TREX component, Aly, and the nuclear export factor, TAP-p15 [18,19].…”

Section: Splicing Directs Mrnp Formationmentioning

confidence: 99%

“…Whereas genes with regulatory functions are enriched for 5UIs, genes encoding proteins targeted to the endoplasmic reticulum (ER) or mitochondria are significantly depleted of such introns [3,24]. When 5UIs are present, they are necessarily the most 5 0 proximal introns in a transcript, and 5 0 proximal introns have a disproportionate role in regulating transcription, mRNA export, and translation [16,[25][26][27][28]. However, 5 0 proximity alone cannot explain the functional distribution of transcripts that do or do not contain 5UIs.…”

Section: Splicing Directs Mrnp Formationmentioning

confidence: 99%

Introns in UTRs: Why we should stop ignoring them

et al. 2012

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Although introns in 5 0 -and 3 0 -untranslated regions (UTRs) are found in many protein coding genes, rarely are they considered distinctive entities with specific functions. Indeed, mammalian transcripts with 3 0 -UTR introns are often assumed nonfunctional because they are subject to elimination by nonsense-mediated decay (NMD). Nonetheless, recent findings indicate that 5 0 -and 3 0 -UTR intron status is of significant functional consequence for the regulation of mammalian genes. Therefore these features should be ignored no longer.

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“…On the other hand, in agreement with data obtained from morphological experiments (Figure 3), in FMIP knockdown cells, C/EBPalpha is expressed even in the presence of muscle differentiation medium (Figure 4c), suggesting that FMIP downmodulates polyadenylated C/EBPalpha mRNA expression under these conditions. C/EBPalpha counteracts the effect of FMIP on adipocyte/myocyte differentiation Recently, a mammalian homologue of THOC5 in Drosophila melanogaster which is a member of the nuclear export complex (Rehwinkel et al, 2004), was identified as fSAP79 (Masuda et al, 2005). The aminoacid sequence of fSAP79 is identical to FMIP.…”

Section: Fmip Influences the Expression Of C/ebpalpha Gene During Adimentioning

confidence: 99%

FMIP controls the adipocyte lineage commitment of C2C12 cells by downmodulation of C/EBPalpha

et al. 2006

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Fms interacting protein (FMIP) is a substrate for Fms tyrosine kinase, and a nuclear/cytoplasm shuttling protein with a leucine zipper. As the phosphorylation of FMIP is observed in insulin-stimulated preadipocytes, we examined the role of FMIP in adipocyte differentiation, using the mesenchymal multipotent stem cells, C2C12 cells, that can differentiate into adipocytes, muscle cells and osteoblasts. Ectopic expression of FMIP in C2C12 impairs the adipocyte differentiation induced by treatment with insulin, dexamethasone and 3-isobutyl-1-methylxanthine. These cells exhibit muscle phenotype with multinuclear morphology. Furthermore, knockdown of endogenous FMIP expression by small interfering RNA improves adipocytic lineage commitment of C2C12 cells, while impairing muscle differentiation. Upon stimulation with insulin, CCAAT/enhancer binding protein (C/EBP)-beta, but not C/EBPalpha, is upregulated in cells expressing ectopic FMIP, whereas in FMIP knockdown cells, C/EBPalpha is constitutively expressed. Ectopic expression of C/EBPalpha counteracts the effects of FMIP, whereas C/EBPalpha knockdown partially mimics the effects of FMIP in this system. Northern blot analysis and reverse transcriptase-polymerase chain reaction study reveal that ectopic FMIP-expressing cells do not contain the polyadenylated C/EBPalpha mRNA, but contain the C/EBPalpha pre-mRNA, suggesting that FMIP plays a role in RNA processing and/or export. Indeed, a member of the THO complex that plays a role in mRNA export, THOC1, is co-precipitated with FMIP. The data we have acquired on FMIP suggest that it is a target for tyrosine kinase receptors that potentiate mRNA export.

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Recruitment of the human TREX complex to mRNA during splicing

Cited by 402 publications

References 35 publications

Rhesus Monkey Rhadinovirus ORF57 Induces gH and gL Glycoprotein Expression through Posttranscriptional Accumulation of Target mRNAs

Rhesus Monkey Rhadinovirus ORF57 Induces gH and gL Glycoprotein Expression through Posttranscriptional Accumulation of Target mRNAs

Introns in UTRs: Why we should stop ignoring them

FMIP controls the adipocyte lineage commitment of C2C12 cells by downmodulation of C/EBPalpha

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