Fig. 4: Kinase-like domain dimerization is a conserved step of RIP3-induced MLKL activation among mammalian species. | Cell Death & Disease

Fig. 4: Kinase-like domain dimerization is a conserved step of RIP3-induced MLKL activation among mammalian species.

From: The MLKL kinase-like domain dimerization is an indispensable step of mammalian MLKL activation in necroptosis signaling

Fig. 4

A Sequences alignment of MLKL orthologs in four vertebrate species. The identical and conserved residues were highlighted in yellow and cyan respectively. Dimer interface residues of human MLKL showed in Fig. 2 are indicated by red arrows. B The overall structure of the dimeric mouse RIP3-MLKL complex (RIP3: blue or brown and MLKL: carrot or silver). The dotted box indicates the interface of the mouse MLKL kinase-like domain dimer. C Phosphomimic mutation promotes kinase-like domain dimerization in both human and mouse MLKL. Flag-tagged wild-types and phosphomimic mutants (S345D on mouse MLKL or S357ES358D on human MLKL) MLKL kinase-like domain proteins were exogenously expressed in HEK293T cells. Then whole-cell lysates were mixed with DMSO or crosslinker DSG as described in the MATERIALS AND METHODS. The samples were analyzed by western blotting using an anti-Flag antibody.

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