SUMOylation of nuclear actin
Copyright policy )SUMOylation of nuclear actin
Actin, a major component of the cytoplasm, is also abundant in the nucleus. Nuclear actin is involved in a variety of nuclear processes including transcription, chromatin remodeling, and intranuclear transport. Nevertheless, the regulation of nuclear actin by posttranslational modifications has not been investigated. We now show that nuclear actin is modified by SUMO2 and SUMO3 and that computational modeling and site-directed mutagenesis identified K68 and K284 as critical sites for SUMOylating actin. We also present a model for the actin–SUMO complex and show that SUMOylation is required for the nuclear localization of actin.
- State University of New York at Potsdam United States
- University of Pittsburgh United States
- University of Illinois at Chicago United States
- State University of New York United States
- University of Dundee United Kingdom
Models, Molecular, 570, Recombinant Fusion Proteins, RNA-POLYMERASE-II, BINDING, Chlorocebus aethiops, Animals, Humans, Computer Simulation, CELL, TRANSCRIPTION, Ubiquitins, Research Articles, Cell Nucleus, IN-VITRO, PROTEIN DOCKING, Actins, Protein Structure, Tertiary, BETA-ACTIN, SUMO, COS Cells, Fatty Acids, Unsaturated, Mutagenesis, Site-Directed, Small Ubiquitin-Related Modifier Proteins, COMPLEXES, MYOSIN, Protein Processing, Post-Translational, HeLa Cells
Models, Molecular, 570, Recombinant Fusion Proteins, RNA-POLYMERASE-II, BINDING, Chlorocebus aethiops, Animals, Humans, Computer Simulation, CELL, TRANSCRIPTION, Ubiquitins, Research Articles, Cell Nucleus, IN-VITRO, PROTEIN DOCKING, Actins, Protein Structure, Tertiary, BETA-ACTIN, SUMO, COS Cells, Fatty Acids, Unsaturated, Mutagenesis, Site-Directed, Small Ubiquitin-Related Modifier Proteins, COMPLEXES, MYOSIN, Protein Processing, Post-Translational, HeLa Cells
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