The brace helices of MLKL mediate interdomain communication and oligomerisation to regulate cell death by necroptosis

• Published in: Cell death and differentiation Vol. 25; no. 9; pp. 1567 - 1580
• Main Authors: Davies, Katherine A., Tanzer, Maria C., Griffin, Michael D. W., Mok, Yee Foong, Young, Samuel N., Qin, Rui, Petrie, Emma J., Czabotar, Peter E., Silke, John, Murphy, James M.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01.09.2018; Nature Publishing Group
• Subjects: 13/109; 13/31; 42/70; 631/45/173; 631/45/275; 82/16; 82/80; 82/83; 96/95; Amino Acid Sequence; Animals; Apoptosis; Apoptosis - drug effects; Biochemistry; Biomedical and Life Sciences; Cell Biology; Cell Cycle Analysis; Cell death; Cell Line; Chimeras; Doxycycline; Fibroblasts; Host specificity; Humans; Kinases; Life Sciences; MAP kinase; Mice; Mutagenesis, Site-Directed; Necroptosis; Necrosis; Phosphorylation; Protein Domains; Protein kinase; Protein Kinases - chemistry; Protein Kinases - genetics; Protein Kinases - metabolism; Protein Multimerization; Protein Structure, Tertiary; Recombinant Proteins - biosynthesis; Recombinant Proteins - chemistry; Recombinant Proteins - isolation & purification; Scattering, Small Angle; Sequence Alignment; Stem Cells; Stoichiometry; Toll-like receptors; Ultracentrifugation; X-Ray Diffraction

The programmed cell death pathway, necroptosis, relies on the pseudokinase, Mixed Lineage Kinase domain-Like (MLKL), for cellular execution downstream of death receptor or Toll-like receptor ligation. Receptor-interacting protein kinase-3 (RIPK3)-mediated phosphorylation of MLKL’s pseudokinase domai...