IRAK4 autophosphorylation functions as a molecular switch to regulate death domain assembly and Myddosome maturation - Supplementary Data (Fig. S4)
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Original and analyzed data for Supplementary Figure 4, from the following manuscript: IRAK4 autophosphorylation functions as a molecular switch to regulate death domain assembly and Myddosome maturation Niranjan Srikanth1,2, Rafael Deliz-Aguirre1,3, Deepika Kumari Gola1, Margaux Bilay1, Elke Ziska1, Ian Kelsall4, Yogesh Kulathu4, and Marcus J. Taylor1* Max Planck Institute for Infection Biology, Chariteplatz 1, Berlin D-10117 Germany Department of Biology, Chemistry and Pharmacy, Freie Universität Berlin, Berlin 14195, Germany. Humboldt University of Berlin, Unter den Linden 6, Berlin 10117, Germany MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom * Corresponding author: taylor@mpiib-berlin.mpg.de Supplementary Figure 4A Original Kymographs used in figure SupplementaryFigure_4B Proportion of MyD88–IRAK4 colocalized puncta with lifetimes ≤30 s or >30 s for IRAK4-WT versus IRAK4-K213A/K214A paired with MyD88-WT SupplementaryFigure_4C Percentage of total MyD88 puncta stably colocalized with IRAK4-WT versus IRAK4-K213A/K214A SupplementaryFigure_4D Original, full-length Western blots. SupplementaryFigure_4E Percentage of total MyD88 puncta stably colocalized with IRAK4-WT when treated with either DMSO or kinase inhibitor SupplementaryFigure_4G IL-2 ELISA data for EL4-MyD88-GFP+IRAK4-mScarlet cells treated with varying doses of IRAK4 kinase inhibitor
