Drosophila sex-lethal inhibits the stable association of the 40S ribosomal subunit with msl-2 mRNA.
TLDR
It is demonstrated that SXL inhibits translation initiation and prevents the stable association of the 40S ribosomal subunit with the mRNA in a manner that does not require the presence of a cap structure at the 5' end of the mRNA.About:
This article is published in Molecular Cell.The article was published on 2003-05-01 and is currently open access. It has received 75 citations till now. The article focuses on the topics: Five prime untranslated region & Untranslated region.read more
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Molecular mechanisms of translational control
TL;DR: Translational control is widely used to regulate gene expression and is especially relevant in situations where transcription is silent or when local control over protein accumulation is required as mentioned in this paper. But only a few examples of translational regulation are mechanistically understood.
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Drosophila miR2 induces pseudo-polysomes and inhibits translation initiation
Rolf Thermann,Matthias W. Hentze +1 more
TL;DR: Results directly show the inhibition of m7GpppG cap-mediated translation initiation as the mechanism of miR2 function, and uncover pseudo-polysomal messenger ribonucleoprotein assemblies that may help to explain earlier findings.
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Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control.
Barsanjit Mazumder,Prabha Sampath,Prabha Sampath,Vasudevan Seshadri,Ratan K. Maitra,Paul E. DiCorleto,Paul E. DiCorleto,Paul L. Fox,Paul L. Fox +8 more
TL;DR: A model in which the ribosome functions not only as a protein synthesis machine, but also as a depot for regulatory proteins that modulate translation is proposed.
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Mechanisms of translational control by the 3' UTR in development and differentiation.
TL;DR: This review focuses on the four main mechanisms of translational control by 3' untranslated regions: Cytoplasmic polyadenylation and deadenylation, recruitment of 4E binding proteins, Regulation of ribosomal subunit binding, Post-initiation repression by microRNAs and translational regulation of mRNAs.
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The Splicing Factor SF2/ASF Regulates Translation Initiation by Enhancing Phosphorylation of 4E-BP1
TL;DR: It is demonstrated that SF2/ASF promotes translation initiation of bound mRNAs and that this activity requires the presence of the cytoplasmic cap-binding protein eIF4E, which suggests a novel mechanism for the activation oftranslation initiation of a subset of m RNAs bound by the shuttling protein SF2/.
References
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eIF4 Initiation Factors: Effectors of mRNA Recruitment to Ribosomes and Regulators of Translation
TL;DR: The recent determination of the structure of eIF4E at atomic resolution has provided insight about how translation is initiated and regulated and suggests that eif4F is also implicated in malignancy and apoptosis.
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Gene-Specific Regulation by General Translation Factors
TL;DR: This work has helped elucidate how modifications of the general translational machinery regulate gene-specific protein production and enables cells to rapidly manipulate protein production without new mRNA synthesis, processing, or export.
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Two genetic circuits repress the Caenorhabditis elegans heterochronic gene lin-28 after translation initiation.
TL;DR: It is shown that lin-28 is repressed during normal development by a mechanism that acts on its mRNA after translation initiation, and that a parallel lin-4-independent regulatory mechanism regulates the expression of lin-14, which encodes a nuclear hormone receptor.
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Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons
TL;DR: EIF1 and eIF1A are also both essential for translation initiation, and act synergistically to mediate assembly of ribosomal initiation complexes at the initiation codon and dissociate aberrant complexes from the mRNA.
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Maskin Is a CPEB-Associated Factor that Transiently Interacts with eIF-4E
TL;DR: It is reported that CPEB, which binds the CPE and stimulates polyadenylation, interacts with a new factor the authors term maskin, which contains a peptide sequence that is conserved among elF-4E-binding proteins.