Abstract
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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Actins / metabolism*
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Animals
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COS Cells
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Cell Nucleus / metabolism*
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Chlorocebus aethiops
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Computer Simulation
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Fatty Acids, Unsaturated / metabolism
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HeLa Cells
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Humans
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Models, Molecular
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Mutagenesis, Site-Directed
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Protein Processing, Post-Translational*
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Protein Structure, Tertiary
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Small Ubiquitin-Related Modifier Proteins / genetics
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Small Ubiquitin-Related Modifier Proteins / metabolism*
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Ubiquitins / genetics
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Ubiquitins / metabolism*
Substances
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Actins
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Fatty Acids, Unsaturated
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Recombinant Fusion Proteins
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SUMO2 protein, human
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SUMO3 protein, human
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Small Ubiquitin-Related Modifier Proteins
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Ubiquitins
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leptomycin B