Fig. 10: Changes in ubiquitination levels on the proteome of Hela cells upon treatment with ACBI1 at 300 nM for 1 h. | Nature Communications

Fig. 10: Changes in ubiquitination levels on the proteome of Hela cells upon treatment with ACBI1 at 300 nM for 1 h.

From: Predicting the structural basis of targeted protein degradation by integrating molecular dynamics simulations with structural mass spectrometry

Fig. 10

a Change in SMARCA2 protein abundance upon treatment with DMSO (cyan circles), ACBI1 (green hexagons), and ACBI1 + MG132 (gray squares). The ACBI1 treatment significantly decreases the SMARCA2 protein abundance compared to the DMSO alone and, upon co-treatment with the proteasomal inhibitor (MG132), the abundance is rescued to levels almost similar to the DMSO alone. The data (n = 3; 2 for ACBI-only) are visualized as the arithmetic mean ± one standard error (for n > 2). Source data are provided as a Source Data file. b Distribution of changes in ubiquitination levels plotted as Log2 fold change in ACBI1 versus DMSO control against the Benjamini-Hochberg corrected p-value for all quantified ubiquitinated sites (n = 12,569) from triplicate measurements. The SMARCA2 sites with significant changes in ubiquitination levels (p-value < 0.05 and Log2 FC(ACBI1/DMSO) ≥ 1) are marked. The sites unique to SMARCA2 are marked as solid orange circles and SMARCA2/4 shared sites are shown as solid blue circles. A pairwise t-test, with Benjamini-Hochberg mutiple comparison, was used for comparing two conditions in triplicate measurements. Source data are provided as Supplementary Data 2. c Location of the two SMARCA2BD lysine residues K1398 and K1416 (shown in blue stick representation) on the SMARCA2BD:ACBI1:VCB crystal structure.

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