Figure 3: Mapping of interacting domains between MARK4 and NLRP3. | Nature Communications

Figure 3: Mapping of interacting domains between MARK4 and NLRP3.

From: MARK4 regulates NLRP3 positioning and inflammasome activation through a microtubule-dependent mechanism

Figure 3

(a) Western blots of co-immunoprecipitated full-length NLRP3 with truncated MARK4 (KD: kinase domain; CD: catalytic domain; UBA: Ubiquitin-associated domain), respectively. (b) Western blots of coimmunoprecipitated truncated NLRP3 (Pyrin Del: pyrin domain deletion; Pyrin only: pyrin domain only; NACHT: Nucleotide-binding oligomerization domain; LRR: Leucine-rich repeat) with full-length MARK4, or co-immunopreciptated MARK4 with truncated NLRP3, respectively. (c) Schematic diagram showing that MARK4 catalytic kinase domain and NLRP3 Pyrin &NACHT domain were essential for their interaction. (d) Western blots of co-immunoprecipitated NLRP3 point mutants with MARK4 respectively. Whole cell lysates were analysed as indication of transfection. (e) Purified recombinant NLRP3 (1-291aa) immobilized on the glutathione sepharose can pull down purified recombinant full-length MARK4 directly. Western blots are representatives of three independent experiments.

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