Fig. 5: FBXO9 docks on a phosphodegron 132TxxxS within PRMT4. | Cell Death & Disease

Fig. 5: FBXO9 docks on a phosphodegron 132TxxxS within PRMT4.

From: Endotoxin stabilizes protein arginine methyltransferase 4 (PRMT4) protein triggering death of lung epithelia

Fig. 5

A BEAS-2B cells were ectopically expressed with various deletion V5-PRMT4 plasmid constructs and lysates subjected to FBXO9 immunoprecipitation from MLE12 cell lysates and subsequent V5 immunoblotting to assess FBXO9:V5 interaction. Pull-down assays suggest that aa100–150 of PRMT4 is important for FBXO9 binding. B, C Fine mapping the FBXO9-binding sites with pull-down assays indicate that a phosphodegron 132TxxxS is critical for FBXO9 binding. D, E Pull-down assays with phosphorylation/dephosphorylation mimics indicate that T132 dephosphorylation and S136 phosphorylation promote the degron binding to FBXO9. F T132 dephosphorylation and S136 phosphorylation accelerate PRMT4 degradation using cycloheximide (CHX). G Densitometric results of F were plotted. Experiments n = 3.

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