Fig. 7: As-induced RIP140 degradation is triggered by Syk-mediated Tyr-phosphorylation | Cell Death & Disease

Fig. 7: As-induced RIP140 degradation is triggered by Syk-mediated Tyr-phosphorylation

From: Receptor-interacting protein 140 as a co-repressor of Heat Shock Factor 1 regulates neuronal stress response

Fig. 7

a Immunoblot showing that HSF1 agonist GA fails to induce RIP140 degradation. b Immunoblot showing that HSF1 inhibitor KRIBB11 and transcription inhibitor Act-D both fail to block RIP140 degradation. c Immunoblot showing that HSF1 knockdown fails to block RIP140 degradation. d Immunoblot showing that the proteasome inhibitor (MG132), but not autophagy inhibitor (CQ and NH4Cl), attenuates RIP140 degradation. e Immunoblot showing that Syk inhibitor KN-62 attenuates As-induced RIP140 degradation. f Immunoblot showing Syk targeting sites-mutated RI140 (Y3F, Tyr 364, 418, 436) is not degraded following As stress. K3R is a negative control with substitution of Lys 662, 678, and 686 with Arg. Quantified and normalized expression level of RIP140 is shown under the corresponding blots

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