Conformational switching of the pseudokinase domain promotes human MLKL tetramerization and cell death by necroptosis
RIPK3-mediated phosphorylation of the mixed lineage kinase domain-like (MLKL) pseudokinase is thought to be the trigger for MLKL activation during necroptotic signaling. Here the authors provide evidence that the transition of human MLKL from a monomeric state to a tetramer is essential for necropto...
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2018
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oai:doaj.org-article:15857781bc14483aa8968103400661492021-12-02T15:34:44ZConformational switching of the pseudokinase domain promotes human MLKL tetramerization and cell death by necroptosis10.1038/s41467-018-04714-72041-1723https://doaj.org/article/15857781bc14483aa8968103400661492018-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-04714-7https://doaj.org/toc/2041-1723RIPK3-mediated phosphorylation of the mixed lineage kinase domain-like (MLKL) pseudokinase is thought to be the trigger for MLKL activation during necroptotic signaling. Here the authors provide evidence that the transition of human MLKL from a monomeric state to a tetramer is essential for necroptosis signalling.Emma J. PetrieJarrod J. SandowAnnette V. JacobsenBrian J. SmithMichael D. W. GriffinIsabelle S. LucetWeiwen DaiSamuel N. YoungMaria C. TanzerAhmad WardakLung-Yu LiangAngus D. CowanJoanne M. HildebrandWilhelmus J. A. KerstenGuillaume LesseneJohn SilkePeter E. CzabotarAndrew I. WebbJames M. MurphyNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-15 (2018) |
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Science Q Emma J. Petrie Jarrod J. Sandow Annette V. Jacobsen Brian J. Smith Michael D. W. Griffin Isabelle S. Lucet Weiwen Dai Samuel N. Young Maria C. Tanzer Ahmad Wardak Lung-Yu Liang Angus D. Cowan Joanne M. Hildebrand Wilhelmus J. A. Kersten Guillaume Lessene John Silke Peter E. Czabotar Andrew I. Webb James M. Murphy Conformational switching of the pseudokinase domain promotes human MLKL tetramerization and cell death by necroptosis |
description |
RIPK3-mediated phosphorylation of the mixed lineage kinase domain-like (MLKL) pseudokinase is thought to be the trigger for MLKL activation during necroptotic signaling. Here the authors provide evidence that the transition of human MLKL from a monomeric state to a tetramer is essential for necroptosis signalling. |
format |
article |
author |
Emma J. Petrie Jarrod J. Sandow Annette V. Jacobsen Brian J. Smith Michael D. W. Griffin Isabelle S. Lucet Weiwen Dai Samuel N. Young Maria C. Tanzer Ahmad Wardak Lung-Yu Liang Angus D. Cowan Joanne M. Hildebrand Wilhelmus J. A. Kersten Guillaume Lessene John Silke Peter E. Czabotar Andrew I. Webb James M. Murphy |
author_facet |
Emma J. Petrie Jarrod J. Sandow Annette V. Jacobsen Brian J. Smith Michael D. W. Griffin Isabelle S. Lucet Weiwen Dai Samuel N. Young Maria C. Tanzer Ahmad Wardak Lung-Yu Liang Angus D. Cowan Joanne M. Hildebrand Wilhelmus J. A. Kersten Guillaume Lessene John Silke Peter E. Czabotar Andrew I. Webb James M. Murphy |
author_sort |
Emma J. Petrie |
title |
Conformational switching of the pseudokinase domain promotes human MLKL tetramerization and cell death by necroptosis |
title_short |
Conformational switching of the pseudokinase domain promotes human MLKL tetramerization and cell death by necroptosis |
title_full |
Conformational switching of the pseudokinase domain promotes human MLKL tetramerization and cell death by necroptosis |
title_fullStr |
Conformational switching of the pseudokinase domain promotes human MLKL tetramerization and cell death by necroptosis |
title_full_unstemmed |
Conformational switching of the pseudokinase domain promotes human MLKL tetramerization and cell death by necroptosis |
title_sort |
conformational switching of the pseudokinase domain promotes human mlkl tetramerization and cell death by necroptosis |
publisher |
Nature Portfolio |
publishDate |
2018 |
url |
https://doaj.org/article/15857781bc14483aa896810340066149 |
work_keys_str_mv |
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