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Published online
doi:10.1083/jcb.200905016
The Journal of Cell Biology, Vol. 186, No. 2, 193-200
The Rockefeller University Press, 0021-9525 $30.00
© Hofmann et al.
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SUMOylation of nuclear actin



Wilma A. Hofmann1,2, Alessandro Arduini1, Samantha M. Nicol3, Carlos J. Camacho4, James L. Lessard5, Frances V. Fuller-Pace3, and Primal de Lanerolle1

1 Department of Physiology and Biophysics, University of Illinois at Chicago, Chicago, IL 60612
2 Department of Physiology and Biophysics, University at Buffalo, State University of New York, Buffalo, NY 14214
3 Cancer Biology Group, Division of Pathology and Neuroscience, Ninewells Hospital and Medical School, University of Dundee, Dundee DD1 9SY, Scotland, UK
4 Department of Computational Biology, University of Pittsburgh, Pittsburgh, PA 15261
5 Division of Developmental Biology, Cincinnati Children’s Research Foundation, Cincinnati, OH 45229

Correspondence to Primal de Lanerolle: primal{at}uic.edu

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.

Abbreviations used in this paper: LMB, leptomycin B; NES, nuclear export signal; SUMO, small ubiquitin-related modifier.

© 2009 Hofmann et al.
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