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• W2903483323 endingPage "815" @default.
• W2903483323 startingPage "805" @default.
• W2903483323 abstract "5-Aminoimidazole-4-carboxamide 1-β-d-ribofuranoside (AICAR, or acadesine) is a precursor of the monophosphate derivative 5-amino-4-imidazole carboxamide ribonucleoside 5'-phosphate (ZMP), an intermediate in de novo purine biosynthesis. AICAR proved to have promising anti-proliferative properties, although the molecular basis of its toxicity is poorly understood. To exert cytotoxicity, AICAR needs to be metabolized, but the AICAR-derived toxic metabolite was not identified. Here, we show that ZMP is the major toxic derivative of AICAR in yeast and establish that its metabolization to succinyl-ZMP, ZDP, or ZTP (di- and triphosphate derivatives of AICAR) strongly reduced its toxicity. Affinity chromatography identified 74 ZMP-binding proteins, including 41 that were found neither as AMP nor as AICAR or succinyl-ZMP binders. Overexpression of karyopherin-β Kap123, one of the ZMP-specific binders, partially rescued AICAR toxicity. Quantitative proteomic analyses revealed 57 proteins significantly less abundant on nuclei-enriched fractions from AICAR-fed cells, this effect being compensated by overexpression of KAP123 for 15 of them. These results reveal nuclear protein trafficking as a function affected by AICAR." @default.
• W2903483323 created "2018-12-11" @default.
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• W2903483323 date "2019-01-01" @default.
• W2903483323 modified "2023-10-11" @default.
• W2903483323 title "Metabolomics and proteomics identify the toxic form and the associated cellular binding targets of the anti-proliferative drug AICAR" @default.
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• W2903483323 doi "https://doi.org/10.1074/jbc.ra118.004964" @default.
• W2903483323 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6341394" @default.
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