Genetic and genomic approaches to explore roles for the conserved 3′-5′ exoribonuclease EXOSC10 in normal and malignant cells

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FIGURE 1.
FIGURE 1.

EXOSC10 structure, protein network, and sumoylation. (A) A cartoon structure from the AlphaFold database (https://alphafold.ebi.ac.uk) for human EXOSC10 (AF-Q01780-F1) is shown, and N-terminal, internal, and C-terminal regions are highlighted in yellow, red, and green, respectively. (B) An experimentally verified physical subnetwork of EXOSC10, RNA-exosome core subunits, and cofactors as provided by the String database (https://string-db.org) is shown. (C) A lollipop plot of posttranslational modifications referenced by PhosphoSitePlus (https://www.phosphosite.org) generated with cBioPortal's mutation mapper (https://www.cbioportal.org/mutation_mapper) is shown. The positions of amino acids undergoing PTMs (x-axis) are plotted against the number of PTMs for any given residue (y-axis). Three lysines (K) that are sumoylated in response to stress are indicated. The location of functional domains is indicated by colored bars. Amino acid coordinates are given at the bottom.

This Article

  1. RNA 32: 789-801