SUMOylation of nuclear actin

Wilma A. Hofmann, Alessandro Arduini, Samantha M. Nicol, Carlos J. Camacho, James L. Lessard, Frances V. Fuller-Pace, Primal de Lanerolle

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    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.

    © 2009 Hofmann et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

    Original languageEnglish
    Pages (from-to)193-200
    Number of pages8
    JournalJournal of Cell Biology
    Volume186
    Issue number2
    DOIs
    Publication statusPublished - 27 Jul 2009

    Keywords

    • RNA-POLYMERASE-II
    • PROTEIN DOCKING
    • BETA-ACTIN
    • IN-VITRO
    • SUMO
    • CELL
    • TRANSCRIPTION
    • COMPLEXES
    • BINDING
    • MYOSIN

    Cite this

    Hofmann, W. A., Arduini, A., Nicol, S. M., Camacho, C. J., Lessard, J. L., Fuller-Pace, F. V., & de Lanerolle, P. (2009). SUMOylation of nuclear actin. Journal of Cell Biology, 186(2), 193-200. https://doi.org/10.1083/jcb.200905016