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Figure 3

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Publication: Kerek et al., 2020 - A conserved acetylation switch enables pharmacological control of tubby-like protein stability
All Figures: Figures for Kerek et al., 2020

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Figure 3

Modification of K316, K320, and K389 each influences TULP3 stability.A, schematic outlining key functional domains in TULP3 and the location of acetylation sites. IFT-A ID denotes Intraflagellar Transport Complex A interacting domain. Western blots representing cycloheximide pulse-chase experiments for stably expressed (B) FLAG-TULP3 wild-type protein or (C) K316Q, (D) K316R, (E) K389Q, (F) K389R, (G) K316Q/K389Q, (H) K316R/K389R mutants in 293T cells. I, plot corresponding to experiments in (B–H) quantifying relative TULP3 protein levels versus time; n = 3 biological replicates, Mean ± S.D. shown. J, protein levels of FLAG-TULP3, FLAG-TULP3 K316Q/K389Q, and K316R/K389R mutants stably expressed in 293T cells following treatment with DMSO or 30 μM C646 for 9 h.

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