Protein Phosphorylation in Translational Control

Proud, Christopher G.

doi:10.1016/b978-0-12-152832-4.50008-2

Cited by 183 publications

(72 citation statements)

References 651 publications

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“…The optimal temperature for the assays was 27 mC (not shown), the same temperature at which the S. frugiperda cells are grown in culture. The addition of an eIF2α kinase inhibitor, 2-aminopurine (Proud, 1992), had no effect on the incorporation of [$&S]methionine (not shown). Apparently, eIF2α kinases were not active in the in vitro translation assays.…”

Section: Resultsmentioning

confidence: 99%

Translational properties of the untranslated regions of the p10 messenger RNA of Autographa californica multicapsid nucleopolyhedrovirus.

Scheper

Vries²,

Broere³

et al. 1997

Journal of General Virology

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Protein yields in the baculovirus expression system do not always correlate with the presence of abundant amounts of corresponding mRNAs. Therefore, a novel aspect of the baculovirus expression system was studied : initiation of translation of very late mRNAs of Autographa californica multicapsid nucleopolyhedrovirus. The untranslated regions (UTRs) of the p10 mRNA of this baculovirus were studied by in vitro translation and after transfection into Spodoptera frugiperda insect cells. Lysates from insect cells were optimized for translation of in vitro transcripts containing p10 sequences. The lysates were used to measure the effects of various deletions in either the 5h or 3hUTR on protein synthesis. Transcripts containing the p10 5hUTR were translated efficiently. Large deletions in the 5hUTR severely decreased this efficiency. Deletions

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Section: Resultsmentioning

confidence: 99%

Translational properties of the untranslated regions of the p10 messenger RNA of Autographa californica multicapsid nucleopolyhedrovirus.

Scheper

Vries²,

Broere³

et al. 1997

Journal of General Virology

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“…mTOR-mediated activation of p70 s6k results in the phosphorylation of ribosomal protein S6, which correlates with the translation of mRNAs that encode both ribosomal proteins and translational elongation factors (8,9). The phosphorylation of PHAS-I through mTOR facilitates the release of eIF-4E and allows its participation in translation initiation, especially of mRNAs with high 5Ј-UTR secondary structures (10)(11)(12)(13). In support of this mechanism, rapamycin, a potent inhibitor of mTOR, blocks the phosphorylation of PHAS-I and p70…”

Section: Metabolic Regulation By Leucine Of Translationmentioning

confidence: 99%

Metabolic Regulation by Leucine of Translation Initiation Through the mTOR-Signaling Pathway by Pancreatic β-Cells

Kwon²,

Cruz³

et al. 2001

Diabetes

200

157

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Recent findings have demonstrated that the branchedchain amino acid leucine can activate the translational regulators, phosphorylated heat-and acid-stable protein regulated by insulin (PHAS-I) and p70 S6 kinase (p70 s6k ), in an insulin-independent and rapamycin-sensitive manner through mammalian target of rapamycin (mTOR), although the mechanism for this activation is undefined. It has been previously established that leucine-induced insulin secretion by ␤-cells involves increased mitochondrial metabolism by oxidative decarboxylation and allosteric activation of glutamate dehydrogenase (GDH). We now show that these same intramitochondrial events that generate signals for leucine-induced insulin exocytosis are required to activate the mTOR mitogenic signaling pathway by ␤-cells. Thus, a minimal model consisting of leucine and glutamine as substrates for oxidative decarboxylation and an activator of GDH, respectively, confirmed the requirement for these two metabolic components and mimicked closely the synergistic interactions achieved by a complete complement of amino acids to activate p70 s6k in a rapamycinsensitive manner. Studies using various leucine analogs also confirmed the close association of mitochondrial metabolism and the ability of leucine analogs to activate p70 s6k . Furthermore, selective inhibitors of mitochondrial function blocked this activation in a reversible manner, which was not associated with a global reduction in ATP levels. These findings indicate that leucine at physiological concentrations stimulates p70 s6k phosphorylation via the mTOR pathway, in part, by serving both as a mitochondrial fuel and an allosteric activator of GDH. Leucine-mediated activation of protein translation through mTOR may contribute to enhanced ␤-cell function by stimulating growth-related protein synthesis and proliferation associated with the maintenance of ␤-cell mass. Diabetes 50:353-360, 2001

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“…It phosphorylates and inactivates eEF-2, thereby reducing the rate of peptide chain elongation. 16,17 It is suggested that the PI3-K/ Akt/mTOR signaling pathway plays an important role in the regulation of mRNA translation. 18,19 As shown in Figure 2f and g, phosphorylated 4E-BP1 levels were significantly increased, whereas phosphorylated eEF2 levels were decreased in the hippocampus of rats immediately after the training on day 8, suggesting that the radial arm maze training results in an activation of translational processes in the hippocampus.…”

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confidence: 99%

Phosphatidylinositol 3-kinase: a molecule mediating BDNF-dependent spatial memory formation

et al. 2003

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Brain-derived neurotrophic factor (BDNF) plays a critical role in synaptic plasticity such as long-term potentiation (LTP), a form of synaptic correlate of learning and memory. BDNF is also implicated in learning and memory. We have demonstrated that radial arm maze training in rats for spatial learning and memory results in a significant increase in the BDNF mRNA expression in the hippocampus. Moreover, antisense BDNF oligonucleotide treatment impaired not only acquisition, but also maintenance and/or recall of spatial memory in the maze. Although these results suggest a role of BDNF for spatial memory processes, the signal transduction mechanisms that mediate the actions of BDNF remain unknown. Here we show that phosphorylation of BDNF receptor tyrosine kinase B (TrkB), phosphatidylinositol 3-kinase (PI3-K) and Akt, a target of PI3-K, in the hippocampus increased in parallel with spatial memory formation. Moreover, an activation of translational processes was suggested in the hippocampus after the maze training. When spatial learning was inhibited by antisense BDNF oligodeoxynucleotide, the activation was diminished. Chronic treatment with PI3-K inhibitor wortmannin impaired spatial learning. Our findings suggested that activation of TrkB/PI3-K and protein synthesis signaling pathway by BDNF in the hippocampus is important for spatial memory.

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Protein Phosphorylation in Translational Control

Cited by 183 publications

References 651 publications

Translational properties of the untranslated regions of the p10 messenger RNA of Autographa californica multicapsid nucleopolyhedrovirus.

Translational properties of the untranslated regions of the p10 messenger RNA of Autographa californica multicapsid nucleopolyhedrovirus.

Metabolic Regulation by Leucine of Translation Initiation Through the mTOR-Signaling Pathway by Pancreatic β-Cells

Phosphatidylinositol 3-kinase: a molecule mediating BDNF-dependent spatial memory formation

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