Fig. 4: Interaction between Parkin and RIPK1 promotes the recruitment of components in complex I under TNFα stimulation. | Cell Death & Disease

Fig. 4: Interaction between Parkin and RIPK1 promotes the recruitment of components in complex I under TNFα stimulation.

From: Parkin regulates NF-κB by mediating site-specific ubiquitination of RIPK1

Fig. 4: Interaction between Parkin and RIPK1 promotes the recruitment of components in complex I under TNFα stimulation.The alternative text for this image may have been generated using AI.

a The expression vectors of HA-tagged RIPK1 with or without FLAG-tagged Parkin were transfected into 293 T cells for 24 h. HA-RIPK1 was immunoprecipitated with anti-HA. The binding proteins of RIPK1 were identified by mass spectrometry and quantified with LFQ module implemented in MaxQuant. b 661 W cells stably expressing GFP or Parkin were treated with TNFα 10 ng/mL for 0, 5, 15 and 30 min. The cell lysates were immunoprecipitated with anti-TNFR1. The immunoprecipitates and cell lysates were analyzed by western blotting with indicated antibodies. c 661 W cells stably expressing Parkin or K150E Parkin were treated with TNFα 10 ng/mL for 0, 5 and 15 min. The cell lysates were immunoprecipitated with anti-TNFR1. The immunoprecipitates and cell lysates were analyzed by western blotting with indicated antibodies

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