The brace helices of MLKL mediate interdomain communication and oligomerisation to regulate cell death by necroptosis
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...
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Published in | Cell death and differentiation Vol. 25; no. 9; pp. 1567 - 1580 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
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London
Nature Publishing Group UK
01.09.2018
Nature Publishing Group |
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Abstract | 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 domain leads to MLKL switching from an inert to activated state, where exposure of the N-terminal four-helix bundle (4HB) ‘executioner’ domain leads to cell death. The precise molecular details of MLKL activation, including the stoichiometry of oligomer assemblies, mechanisms of membrane translocation and permeabilisation, remain a matter of debate. Here, we dissect the function of the two ‘brace’ helices that connect the 4HB to the pseudokinase domain of MLKL. In addition to establishing that the integrity of the second brace helix is crucial for the assembly of mouse MLKL homotrimers and cell death, we implicate the brace helices as a device to communicate pseudokinase domain phosphorylation event(s) to the N-terminal executioner 4HB domain. Using mouse:human MLKL chimeras, we defined the first brace helix and adjacent loop as key elements of the molecular switch mechanism that relay pseudokinase domain phosphorylation to the activation of the 4HB domain killing activity. In addition, our chimera data revealed the importance of the pseudokinase domain in conferring host specificity on MLKL killing function, where fusion of the mouse pseudokinase domain converted the human 4HB + brace from inactive to a constitutive killer of mouse fibroblasts. These findings illustrate that the brace helices play an active role in MLKL regulation, rather than simply acting as a tether between the 4HB and pseudokinase domains. |
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AbstractList | 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 domain leads to MLKL switching from an inert to activated state, where exposure of the N-terminal four-helix bundle (4HB) 'executioner' domain leads to cell death. The precise molecular details of MLKL activation, including the stoichiometry of oligomer assemblies, mechanisms of membrane translocation and permeabilisation, remain a matter of debate. Here, we dissect the function of the two 'brace' helices that connect the 4HB to the pseudokinase domain of MLKL. In addition to establishing that the integrity of the second brace helix is crucial for the assembly of mouse MLKL homotrimers and cell death, we implicate the brace helices as a device to communicate pseudokinase domain phosphorylation event(s) to the N-terminal executioner 4HB domain. Using mouse:human MLKL chimeras, we defined the first brace helix and adjacent loop as key elements of the molecular switch mechanism that relay pseudokinase domain phosphorylation to the activation of the 4HB domain killing activity. In addition, our chimera data revealed the importance of the pseudokinase domain in conferring host specificity on MLKL killing function, where fusion of the mouse pseudokinase domain converted the human 4HB + brace from inactive to a constitutive killer of mouse fibroblasts. These findings illustrate that the brace helices play an active role in MLKL regulation, rather than simply acting as a tether between the 4HB and pseudokinase domains. |
Author | Qin, Rui Tanzer, Maria C. Petrie, Emma J. Czabotar, Peter E. Davies, Katherine A. Mok, Yee Foong Young, Samuel N. Silke, John Murphy, James M. Griffin, Michael D. W. |
Author_xml | – sequence: 1 givenname: Katherine A. surname: Davies fullname: Davies, Katherine A. organization: The Walter & Eliza Hall Institute of Medical Research, Department of Medical Biology, The University of Melbourne – sequence: 2 givenname: Maria C. surname: Tanzer fullname: Tanzer, Maria C. organization: The Walter & Eliza Hall Institute of Medical Research, Department of Medical Biology, The University of Melbourne – sequence: 3 givenname: Michael D. W. surname: Griffin fullname: Griffin, Michael D. W. organization: Department of Biochemistry & Molecular Biology, The University of Melbourne – sequence: 4 givenname: Yee Foong surname: Mok fullname: Mok, Yee Foong organization: Department of Biochemistry & Molecular Biology, The University of Melbourne – sequence: 5 givenname: Samuel N. surname: Young fullname: Young, Samuel N. organization: The Walter & Eliza Hall Institute of Medical Research – sequence: 6 givenname: Rui surname: Qin fullname: Qin, Rui organization: The Walter & Eliza Hall Institute of Medical Research, School of Pharmaceutical Sciences, Tsinghua University – sequence: 7 givenname: Emma J. surname: Petrie fullname: Petrie, Emma J. organization: The Walter & Eliza Hall Institute of Medical Research, Department of Medical Biology, The University of Melbourne – sequence: 8 givenname: Peter E. surname: Czabotar fullname: Czabotar, Peter E. organization: The Walter & Eliza Hall Institute of Medical Research, Department of Medical Biology, The University of Melbourne – sequence: 9 givenname: John orcidid: 0000-0002-7611-5774 surname: Silke fullname: Silke, John email: silke@wehi.edu.au organization: The Walter & Eliza Hall Institute of Medical Research, Department of Medical Biology, The University of Melbourne – sequence: 10 givenname: James M. surname: Murphy fullname: Murphy, James M. email: jamesm@wehi.edu.au organization: The Walter & Eliza Hall Institute of Medical Research, Department of Medical Biology, The University of Melbourne |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29445128$$D View this record in MEDLINE/PubMed |
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Title | The brace helices of MLKL mediate interdomain communication and oligomerisation to regulate cell death by necroptosis |
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