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. 2010 Jan 25;188(2):191–198. doi: 10.1083/jcb.200911102

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© 2010 Holland 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 2. — Phosphorylation of the β-TrCP–binding motif has a minor effect on the stability of mouse Plk4. (A) Cells were treated with or without the proteasome inhibitor MG132 for 8 h and immunoblotted to determine the expression level of Plk4^WT and Plk4^KD. (B) Expression of Plk4^WT-EYFP or Plk4^KD-EYFP was induced for 24 h in cells constitutively expressing Plk4^KD-Myc. The expression level of the Myc and EYFP-tagged Plk4 transgenes was subsequently determined by immunoblotting. (C) The Plk4^AA mutant possesses two mutations that prevent phosphorylation of the β-TrCP–binding motif (highlighted in green). (D) Immunoblot shows a modest increase in the stability of Plk4^AA. (E) HEK 293 cells were cotransfected with Plk4-EYFP and Myc–β-TrCP and treated with MG132 for 4 h. Plk4-EYFP was purified using GBP-coupled beads or beads alone, and protein complexes were analyzed by immunoblotting. (F) HEK 293 cells were cotransfected with Plk4-EYFP and HA-ubiquitin and treated with MG132 for 4 h. Plk4-EYFP was purified using GBP-coupled beads or beads alone, and protein complexes were analyzed by immunoblotting.