FIGURE SUMMARY
Title

The BTB-Containing Protein Kctd15 Is SUMOylated In Vivo

Authors
Zarelli, V.E., and Dawid, I.B.
Source
Full text @ PLoS One

KR mutants repress AP-2α function

(A) AP-2α activity in a reporter assay [19] was inhibited by the K252R and 4xKR mutants with similar efficacy as the WT protein, although inhibition was reduced at low concentration. Immunoblots with anti-Kctd15, anti-AP-2 and anti-Tubulin antibodies control for protein expression. (B) AP2-Luc reporter assay using human KCTD15 and K278R mutant, both of which inhibit activity. (C) Kctd15 and K252R mRNAs were injected into zebrafish embryos. ISH with foxD3 probe at the 1 somite stage shows that the K252R mutant inhibits NC formation as effectively as WT Kctd15. Embryo images define normal expression, total inhibition and partial inhibition. Quantification is shown in the histogram, numbers of embryos listed on the bars. (D) Luciferase assay using AP-2γ illustrates that zebrafish WT and K252R mutant are equally effective in inhibiting reporter activity.

Kctd15 conjugated to SUMO1 is less competent in inhibiting AP-2α activity and NC formation.

(A) Diagram of the fusion protein between Kctd15 and SUMO1. (B) Kctd15-SUMO1 conjugated protein was less effective than WT in repressing AP-27alpha; dependent reporter activation. (C) Injection into zebrafish embryos of Kctd15-SUMO1 failed to abolish NC formation.

Acknowledgments
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