Regulation of cap-dependent translation by eIF4E inhibitory proteins

By Joel D. Richter, Nahum Sonenberg. Nature, 2005

1,028 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/7abd355eabdfd11442ab411ccb0ed1c37e673ca5

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Citations in the corpus

Large-scale mapping of human protein–protein interactions by mass spectrometry (2007, background): “For translation to proceed, binding of an initiation factor, EIF4E, to the cap structure is required (Richter and Sonenberg, 2005).”
Activation of Akt and eIF4E survival pathways by rapamycin-mediated mammalian target of rapamycin inhibition. (2005, background): “eIF4E plays a critical role in the regulation of cap-dependentprotein translation and thus its activity is integral in determining global translation rates (32).”
The autistic neuron: troubled translation? (2008, background): “Recognition of the 5′ mRNA cap by eIF4E, which leads to recruitment of eIF4G and the small ribosomal subunit, is the key regulatory step in translation initiation (Richter and Sonenberg, 2005).”
RNA‐binding proteins and post‐transcriptional gene regulation (2008, positive): “ing protein (PABP) binds the poly(A) tail and interacts directly with eIF4G to abrogate maskin s interaction with eIF4E, allowing the mRNA to be translated [130,132].”
Systems biology approach predicts immunogenicity of the yellow fever vaccine in humans (2008, background): “EIF2AK4 (also known as mammalian general control non-derepressible-2 (GCN2)) regulates protein synthesis in response to environmental stresses by phosphorylating the α -subunit of initiation factor 2 (eIF2 α ) 19 .”
Protein Synthesis Initiation in Eukaryotic Cells. (2018, background): “2003) and is a site of translational control via a series of eIF4E-binding proteins (4E-BPs) that limit eIF4E access to eIF4G (Richter and Sonenberg 2005).”
The Molecular Bases of Training Adaptation (2007, background): “mTOR-raptor also regulates and suppresses 4E-BP1 (also known as phosphorylated heat and acid soluble protein stimulated by insulin, PHAS-1) via hyper-phosphorylation to derepress 4E-BP1 inhibition of translation initiation cap binding protein eIF4E (Richter and Sonenberg 2005; Sarbassov et al. 2005a”
Toward a Kinetic Understanding of Eukaryotic Translation. (2018, background): “The regulation of eIF4F availability is controlled by eIF4E-binding proteins (4E-BPs) acting as competitive inhibitors to prevent eIF4E binding to eIF4G (Richter and Sonenberg 2005).”
mTOR signaling at a glance (2009, methodology): “The phosphorylation of 4E-BP1 prevents its binding to eIF4E, enabling eIF4E to promote cap-dependent translation (reviewed by Richter and Sonenberg, 2005 ).”
The fragile X syndrome protein represses activity-dependent translation through CYFIP1, a new 4E-BP. (2008, methodology): “In some cases, synaptic activity and/or developmental transitions can alleviate translational repression (Gebauer and Hentze, 2004; Richter and Sonenberg, 2005); con- 1048 Cell 134, 1042–1054, September 19, 2008 ª2008 Elsevier Inc. sequently, we investigated whether BDNF stimulation caused release…”
P bodies and the control of mRNA translation and degradation. (2007, background): “…repression involves the sequestration of the cap structure by the cap-binding protein eIF4E in a complex with an eIF4E-binding protein, such as CUP in Drosophila or 4E-T in mammalian cells, which blocks eIF4G recruitment and thereby inhibits translation initiation (Richter and Sonenberg, 2005).”
p53 target genes sestrin1 and sestrin2 connect genotoxic stress and mTOR signaling. (2008, positive): “Phosphorylated 4E-BP1 cannot interact with eIF-4E and does not inhibit eIF-4F formation (Richter and Sonenberg, 2005).”
Control of translation and mRNA degradation by miRNAs and siRNAs. (2006, background): “First, translation initiation can be regulated on specific mRNAs by affecting the ability of the mRNA to complete a step in the initiation process (for review, see Richter and Sonenberg 2005).”
mTOR regulates MAPKAPK2 translation to control the senescence-associated secretory phenotype (2015, neutral): “19).”