Human mRNA Export Machinery Recruited to the 5′ End of mRNA

Cheng, Hong; Dufu, Kobina; Lee, Chung-Sheng; Hsu, Jeanne L.; Dias, Anusha P.; Reed, Robin

doi:10.1016/j.cell.2006.10.044

Cited by 415 publications

(531 citation statements)

References 63 publications

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“…), this hypothesis remains to be tested in planta. In addition, our speculation is supported by the finding that the human transcription/export (TREX) complex, which is comprised of the core THO complex, is recruited to a region near the 59 end of the mRNA and that TREX recruitment requires the 59 cap (Sträßer et al 2002;Cheng et al 2006).…”

Section: Discussionmentioning

confidence: 51%

“…SE encodes a zinc finger protein that has been implicated in mRNA splicing (Prigge and Wagner 2001;Laubinger et al 2008). Interestingly, some functions of the THO complex are dependent on splicing, and studies in animals have indicated that the THO complex interacts with the spliceosome (Rappsilber et al 2002;Zhou et al 2002;Masuda et al 2005;Cheng et al 2006). To determine whether EMU as well as SE are involved in mRNA splicing, we characterized the splicing patterns in emu mutant plants by examining transcripts of genes encoding serine/arginine-rich (SR) proteins, which belong to a conserved family of splicing regulators in eukaryotes and are extensively alternatively spliced (Reddy 2007;Long and Caceres 2009).…”

Section: Splicing Defects In Emumentioning

confidence: 99%

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Characterization of EMU, the Arabidopsis homolog of the yeast THO complex member HPR1

Furumizu¹,

Tsukaya²,

Komeda³

2010

RNA

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Diverse and precise control is essential for eukaryotic gene expression. This is accomplished through the recruitment of a myriad of proteins to a nascent messenger RNA (mRNA) to mediate modifications, such as capping, splicing, 39-end processing, and export. Despite being important for every cell, however, the mechanism by which the formation of diverse messenger ribonucleoprotein (mRNP) particles contributes to maintaining intricate systems in the multicellular organism remains incompletely defined. We identified and characterized a mutant gene named erecta mRNA under-expressed (emu) that leads to the defective mRNA accumulation of ERECTA, a developmental regulator in the model plant Arabidopsis thaliana. EMU encodes a protein homologous to a component of the THO complex that is required for the generation of functional mRNPs. Further analysis suggested that EMU is genetically associated with SERRATE, HYPONASTIC LEAVES1, and ARGONAUTE1, which are required for proper RNA maturation or action. Furthermore, mutations in another THO-related gene led to embryonic lethality. These findings support the presence and importance of the THO-related complex in plants as well as yeast and vertebrates.

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Section: Discussionmentioning

confidence: 51%

Section: Splicing Defects In Emumentioning

confidence: 99%

Characterization of EMU, the Arabidopsis homolog of the yeast THO complex member HPR1

Furumizu¹,

Tsukaya²,

Komeda³

2010

RNA

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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%

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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“…In addition to genes of unknown biochemical function, known FLC regulators include chromatin modifying enzymes, transcription factors, and a number of RNA-associated proteins, including ABSCISIC ACID HYPERSENSITIVE1 (ABH1; Hugouvieux et al, 2001;Bezerra et al, 2004). ABH1 encodes the plant homolog of CAP-BINDING PROTEIN80, a component of the nuclear cap-binding complex that has been implicated in pre-mRNA processing and nuclear export via the nuclear pore complex (NPC; Cheng et al, 2006).…”

mentioning

confidence: 99%

The Nuclear Pore Protein AtTPR Is Required for RNA Homeostasis, Flowering Time, and Auxin Signaling

et al. 2007

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Nuclear pore complexes (NPCs) mediate the transport of RNA and other cargo between the nucleus and the cytoplasm. In vertebrates, the NPC protein TRANSLOCATED PROMOTER REGION (TPR) is associated with the inner filaments of the nuclear basket and is thought to serve as a scaffold for the assembly of transport machinery. In a screen for mutants that suppress the expression of the floral inhibitor FLOWERING LOCUS C, we identified lesions in the Arabidopsis (Arabidopsis thaliana) homolog of TPR (AtTPR). attpr mutants exhibit early-flowering and other pleiotropic phenotypes. A possible explanation for these developmental defects is that attpr mutants exhibit an approximately 8-fold increase in nuclear polyA RNA. Thus AtTPR is required for the efficient export of RNA from the nucleus. Microarray analysis shows that, in wild type, transcript abundance in the nuclear and total RNA pools are highly correlated; whereas, in attpr mutants, a significantly larger fraction of transcripts is enriched in either the nuclear or total pool. Thus AtTPR is required for homeostasis between nuclear and cytoplasmic RNA. We also show that the effects of AtTPR on small RNA abundance and auxin signaling are similar to that of two other NPC-associated proteins, HASTY (HST) and SUPPRESSOR OF AUXIN RESISTANCE3 (SAR3). This suggests that AtTPR, HST, and SAR3 may play related roles in the function of the nuclear pore.

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Human mRNA Export Machinery Recruited to the 5′ End of mRNA

Cited by 415 publications

References 63 publications

Characterization of EMU, the Arabidopsis homolog of the yeast THO complex member HPR1

Characterization of EMU, the Arabidopsis homolog of the yeast THO complex member HPR1

Introns in UTRs: Why we should stop ignoring them

The Nuclear Pore Protein AtTPR Is Required for RNA Homeostasis, Flowering Time, and Auxin Signaling

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