AXenopus laevisHomologue of the La Autoantigen Binds the Pyrimidine Tract of the 5′ UTR of Ribosomal Protein mRNAsin Vitro: Implication of a Protein Factor in Complex Formation

Pellizzoni, Livio; Cardinali, Beatrice; Lin-Marq, Nathalie; Mercanti, Delio; Pierandrei-Amaldi, Paola

doi:10.1006/jmbi.1996.0368

Cited by 71 publications

(49 citation statements)

References 49 publications

(57 reference statements)

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“…1). Enhanced 59TOP mRNA association could instead be mediated by starvation-stimulated cooperative binding with other factors associated with the 59 end of 59TOP mRNAs, such as, for example, La, ZNF9, or AUF1 (Pellizzoni et al 1996(Pellizzoni et al , 1997(Pellizzoni et al , 1998Crosio et al 2000;Cardinali et al 2003;Intine et al 2003;Schwartz et al 2004;Kakegawa et al 2007). Alternatively, starvation could trigger the release of factors from the 59TOP, such as translation initiation complexes, which under conditions stimulatory to cell growth may prevent the binding of TIA-1/TIAR to the 59TOP.…”

Section: Discussionmentioning

confidence: 99%

“…Several candidates for such an activity have been proposed through their reported association with 59TOP elements and immediate downstream regions. These include the abundant La antigen (La) (Pellizzoni et al 1996;Crosio et al 2000;Cardinali et al 2003;Intine et al 2003;Schwartz et al 2004), ZNF9 (Pellizzoni et al 1997(Pellizzoni et al , 1998, and AUF1 (Kakegawa et al 2007). However, definitive evidence for regulatory roles of these proteins in 59TOP mRNA translation is lacking.…”

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confidence: 99%

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Translational coregulation of 5′TOP mRNAs by TIA-1 and TIAR

Damgaard¹,

2011

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The response of cells to changes in their environment often requires coregulation of gene networks, but little is known about how this can occur at the post-transcriptional level. An important example of post-transcriptional coregulation is the selective translational regulation in response to growth conditions of mammalian mRNAs that encode protein biosynthesis factors and contain hallmark 59-terminal oligopyrimidine tracts (59TOP). However, the responsible trans-factors and the mechanism by which they coregulate 59TOP mRNAs have remained elusive. Here we identify stress granule-associated TIA-1 and TIAR proteins as key factors in human 59TOP mRNA regulation, which upon amino acid starvation assemble onto the 59 end of 59TOP mRNAs and arrest translation at the initiation step, as evidenced by TIA-1/TIAR-dependent 59TOP mRNA translation repression, polysome release, and accumulation in stress granules. This requires starvation-mediated activation of the GCN2 (general control nonderepressible 2) kinase and inactivation of the mTOR (mammalian target of rapamycin) signaling pathway. Our findings provide a mechanistic explanation to the long-standing question of how the network of 59TOP mRNAs are coregulated according to amino acid availability, thereby allowing redirection of limited resources to mount a nutrient deprivation response. This presents a fundamental example of how a group of mRNAs can be translationally coregulated in response to changes in the cellular environment.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Translational coregulation of 5′TOP mRNAs by TIA-1 and TIAR

Damgaard¹,

2011

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“…65 Several candidate proteins have been proposed over the years as potential modulators of TOP mRNAs, including the abundant La antigen (also known as La-related protein 3 [LARP3]). [67][68][69] LARP3 was shown to directly interact with mRNAs containing a 5'TOP motif within actively translating polysomes, suggesting that it plays a positive role in TOP mRNA translation. 67 The RNA-binding protein AUF1 (AU-rich element RNA-binding protein 1) was also found to interact with the 5'TOP sequence, but in this case AUF1 binding correlated with translational repression of TOP mRNAs.…”

Section: Translational Control Of Top Mrnasmentioning

confidence: 99%

Regulation of global and specific mRNA translation by the mTOR signaling pathway

2015

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“…However, the final effector(s) that directly affect TOP mRNAs have not been clearly identified. Some putative TOP mRNA translational regulators have been proposed: the autoantigen La, which binds the TOP sequence (Pellizzoni et al 1996;Crosio et al 2000;Zhu et al 2001;Cardinali et al 2003;Schwartz et al 2004), and the cellular nucleic acid binding protein (CNBP), which binds a downstream region (Pellizzoni et al 1997). The precise role of these proteins in TOP mRNA translational regulation as well as their relation with PI3K signaling pathways is still to be defined.…”

Section: Introductionmentioning

confidence: 99%

All translation elongation factors and the e, f, and h subunits of translation initiation factor 3 are encoded by 5′-terminal oligopyrimidine (TOP) mRNAs

Iadevaia¹,

Caldarola²,

Tino³

et al. 2008

RNA

103

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Terminal oligopyrimidine (TOP) mRNAs (encoded by the TOP genes) are identified by a sequence of 6-12 pyrimidines at the 59 end and by a growth-associated translational regulation. All vertebrate genes for the 80 ribosomal proteins and some other genes involved, directly or indirectly, in translation, are TOP genes. Among the numerous translation factors, only eEF1A and eEF2 are known to be encoded by TOP genes, most of the others having not been analyzed. Here, we report a systematic analysis of the human genes for translation factors. Our results show that: (1) all five elongation factors are encoded by TOP genes; and (2) among the initiation and termination factors analyzed, only eIF3e, eIF3f, and eIF3h exhibit the characteristics of TOP genes. Interestingly, these three polypeptides have been recently shown to constitute a specific subgroup among eIF3 subunits. In fact, eIF3e, eIF3f, and eIF3h are the part of the functional core of eIF3 that is not conserved in Saccharomyces cerevisiae. It has been hypothesized that they are regulatory subunits, and the fact that they are encoded by TOP genes may be relevant for their function.

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AXenopus laevisHomologue of the La Autoantigen Binds the Pyrimidine Tract of the 5′ UTR of Ribosomal Protein mRNAsin Vitro: Implication of a Protein Factor in Complex Formation

Cited by 71 publications

References 49 publications

Translational coregulation of 5′TOP mRNAs by TIA-1 and TIAR

Translational coregulation of 5′TOP mRNAs by TIA-1 and TIAR

Regulation of global and specific mRNA translation by the mTOR signaling pathway

All translation elongation factors and the e, f, and h subunits of translation initiation factor 3 are encoded by 5′-terminal oligopyrimidine (TOP) mRNAs

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