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. 2009 Jul 27;186(2):193–200. doi: 10.1083/jcb.200905016

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© 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/).

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Figure 3. — Model of the β-actin–SUMO2/3 complex. (A) Predicted model of β-actin (blue) in complex with SUMO2/3 (red). Amino acids involved in complex formation are specified. (B) SUMOylation of actin mutants: myc-tagged wild-type β-actin with an NLS (lane 1) or K68R, K284R, or a K68/284R double mutant β-actin (lanes 2–4), each with a myc tag and NLS, were coexpressed in COS-7 cells with His-SUMO2. His-SUMO2 was purified on a Ni²⁺ column and probed with anti-myc antibodies. COS-7 cells were cotransfected with His-SUMO2 and myc-NLS-actin constructs containing the indicated amino acid substitutions. Molecular mass markers are listed in kD. Asterisk, SUMOylated actin. (C) Schematic representation of the location of the SUMO protein relative to the location of NES-1 of β-actin. Note that the SUMOylation appears to cover NES-1.