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In mammalian cells, there are three isoforms of malic enzymes (MEs): a cytosolic nicotinamide adenine dinucleotide phosphate + (NADP + )-dependent isoform (ME1), a mitochondrial NAD(P) + -dependent isoform (ME2),… Click to show full abstract
In mammalian cells, there are three isoforms of malic enzymes (MEs): a cytosolic nicotinamide adenine dinucleotide phosphate + (NADP + )-dependent isoform (ME1), a mitochondrial NAD(P) + -dependent isoform (ME2), and a mitochondrial NADP + -dependent isoform (ME3), of which ME1 and ME2 are the major isoforms. As essential modulators of metabolism and aging, MEs have been reported to be targets for wild-type p53 (wtp53), which can transcriptionally repress their expression. Reciprocally, downregulation of ME1 and ME2 leads to wtp53 activation via distinct mechanisms (Jiang The TP53 most frequently mutated in with more than of this of p53 much in many cells, and high levels of mutp53 usually an increased oncogenic capacity. it is crucial to determine the mechanisms by which mutp53 stabilization/degradation is regulated, to identify therapeutic strategies that destabilize
Journal Title: Journal of Molecular Cell Biology
Year Published: 2022
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