2020
DOI: 10.1186/s40170-020-00233-6
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Protein synthesis inhibitors stimulate MondoA transcriptional activity by driving an accumulation of glucose 6-phosphate

Abstract: Background Protein synthesis is regulated by the availability of amino acids, the engagement of growth factor signaling pathways, and adenosine triphosphate (ATP) levels sufficient to support translation. Crosstalk between these inputs is extensive, yet other regulatory mechanisms remain to be characterized. For example, the translation initiation inhibitor rocaglamide A (RocA) induces thioredoxin-interacting protein (TXNIP). TXNIP is a negative regulator of glucose uptake; thus, its induction … Show more

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Cited by 10 publications
(9 citation statements)
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“…[81,82] This process, in turn, increases the lipophilic nature of the central metal atom, which favors its permeation more efficiently through the lipid layers of the microorganism, thus destroying them more aggressively. [83] The selected copper(II) complexes for anticancer investigation are believed to possess the ability of cleavage of DNA through oxidative and hydrolytic pathways, cell apoptosis via intrinsic reactive oxygen species (ROS)-mediated mitochondrial pathway due to excessive production of ROS. The flexible behavior of Cu(I/II) redox advantage prompts the formation of more potent derivatives.…”
Section: Anticancer Activitymentioning
confidence: 99%
“…[81,82] This process, in turn, increases the lipophilic nature of the central metal atom, which favors its permeation more efficiently through the lipid layers of the microorganism, thus destroying them more aggressively. [83] The selected copper(II) complexes for anticancer investigation are believed to possess the ability of cleavage of DNA through oxidative and hydrolytic pathways, cell apoptosis via intrinsic reactive oxygen species (ROS)-mediated mitochondrial pathway due to excessive production of ROS. The flexible behavior of Cu(I/II) redox advantage prompts the formation of more potent derivatives.…”
Section: Anticancer Activitymentioning
confidence: 99%
“…This “Mlx Network”, also comprised of bHLH-ZIP factors, contained the Myc-like proteins ChREBP (“carbohydrate response element binding protein”) and MondoA and their own dedicated heterodimerization partner, the Max-related Mlx, which together formed the Network’s positively-acting arm [ 31 , 56 , 57 , 58 ] ( Figure 1 ). Unlike Myc and Max, which are nuclear proteins, ChREBP, MondoA and Mlx are “conditionally nuclear” in that they translocate to the nucleus only upon binding metabolites such as glucose, glucose-6-phosphate, fructose 2,6-bisphosphate, lactate and adenosine [ 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 40 , 42 , 56 , 59 , 60 , 61 , 62 , 63 , 64 , 65 , 66 , 67 , 68 ]. The cytosolic location of MondoA and ChREBP is also not random; rather, amphipathic helical domains in the C-termini of these factors allow them to interact with intracytoplasmic lipid droplets and presumably serve as sensors of intracellular lipid content [ 69 ].…”
Section: Introductionmentioning
confidence: 99%
“…They tend to encode enzymes involved in carbohydrate and lipid metabolism; mitochondrial and ribosomal proteins and factors that regulate translational initiation, elongation and termination [ 31 , 39 , 41 , 42 , 46 , 70 , 71 , 72 , 73 , 76 , 78 , 79 , 80 , 81 , 82 , 83 , 84 , 85 , 86 , 87 , 88 , 89 ]. Together, these findings indicate that, via selective, cytoplasmic-nuclear partitioning, sharing of Mxd1,4 and Mnt and binding to both common and unique target genes, this “Extended Myc Network” cross-talks, while simultaneously communicating with and responding to the metabolic cues and reservoirs needed to support energy-intensive processes such as translation and proliferation [ 36 , 42 , 64 , 65 , 69 , 88 , 89 , 90 , 91 , 92 , 93 , 94 , 95 , 96 ].…”
Section: Introductionmentioning
confidence: 99%
“…They tend to encode enzymes involved in carbohydrate and lipid metabolism; mitochondrial and ribosomal proteins and factors that regulate translational initiation, elongation and termination [21,33,50,[57][58][59][60]63,[65][66][67][68][69][70][71][72][73][74][75][76][77][78]. Together these findings indicate that, via selective, cytoplasmic-nuclear partitioning, sharing of Mxd1,4 and Mnt and binding to both common and unique target genes, this "Extended Myc Network" cross-talks, while simultaneously communicating with and responding to the metabolic cues needed to support energy-intensive processes such as translation and proliferation [43,[50][51][52]56,[77][78][79][80][81][82][83][84][85].…”
Section: Introductionmentioning
confidence: 86%
“…1). Unlike Myc and Max, which are nuclear proteins, ChREBP, MondoA and Mlx are cytoplasmic but translocate to the nucleus in response to the binding of metabolites such as glucose, glucose-6-phosphate, fructose 2,6-bisphosphate, lactate and adenosine [33,34,[37][38][39][40][41][42][43][44][45][46][47][48][49][50][51][52][53][54][55]. In fact, the cytosolic location of MondoA and ChREBP is not random; rather amphipathic helical domains in the C-termini of these factors allow them to interact with intracytoplasmic lipid droplets and presumably serve as sensors of intracellular lipid content [56].…”
Section: Introductionmentioning
confidence: 99%