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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
  • University of Illinois at Chicago
  • University of Dundee
  • University of Pittsburgh
  • Cincinnati Children's Hospital Medical Center

Research output: Contribution to journalArticlepeer-review

80 Scopus citations

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.

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

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