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- W3100708325 abstract "Abstract NUP98-fusion proteins cause acute myeloid leukemia via unknown molecular mechanisms. All NUP98-fusion proteins share an intrinsically disordered region (IDR) featuring >35 repeats of Phenylalanine-Glycine (FG) in the NUP98 N-terminus. Conversely, different C-terminal NUP98-fusion partners are often transcriptional and epigenetic regulators. Given these structural features we hypothesized that mechanisms of oncogenic transformation by NUP98-fusion proteins are hard-wired in their protein interactomes. Affinity purification coupled to mass spectrometry of five distinct NUP98-fusion proteins revealed a conserved set of interactors that was highly enriched for proteins involved in biomolecular condensation. We developed biotinylated isoxazole-mediated condensome mass spectrometry (biCon-MS) to show that NUP98-fusion proteins alter the global composition of biomolecular condensates. In addition, an artificial FG-repeat containing fusion protein was able to phenocopy the induction of leukemic gene expression as mediated by NUP98-KDM5A. Thus, we propose that IDR-containing fusion proteins have evolved to uniquely combine biomolecular condensation with gene control to induce cancer. AML, NUP98, fusion protein, AP-MS, LLPS, biCon-MS, condensate" @default.
- W3100708325 created "2020-11-23" @default.
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- W3100708325 date "2020-11-16" @default.
- W3100708325 modified "2023-09-26" @default.
- W3100708325 title "Biomolecular Condensation Drives Leukemia Caused by NUP98-Fusion Proteins" @default.
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- W3100708325 doi "https://doi.org/10.1101/2020.11.16.384271" @default.
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