Distinct pseudokinase domain conformations underlie divergent activation mechanisms among vertebrate MLKL orthologues

The MLKL pseudokinase is the terminal effector in the necroptosis cell death pathway. Phosphorylation by its upstream regulator, RIPK3, triggers MLKL’s conversion from a dormant cytoplasmic protein into oligomers that translocate to, and permeabilize, the plasma membrane to kill cells. The precise m...

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Published inNature communications Vol. 11; no. 1; p. 3060
Main Authors Davies, Katherine A., Fitzgibbon, Cheree, Young, Samuel N., Garnish, Sarah E., Yeung, Wayland, Coursier, Diane, Birkinshaw, Richard W., Sandow, Jarrod J., Lehmann, Wil I. L., Liang, Lung-Yu, Lucet, Isabelle S., Chalmers, James D., Patrick, Wayne M., Kannan, Natarajan, Petrie, Emma J., Czabotar, Peter E., Murphy, James M.
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 19.06.2020
Nature Publishing Group
Nature Portfolio
Subjects
13/106
13/31
13/95
631/45/275
631/45/535/1266
631/80/82/2344
82/80
82/83
Activation
Animals
Apoptosis
Cell death
Chickens
Crystal structure
Crystallography, X-Ray
Cytoplasm - enzymology
Divergence
Domains
HEK293 Cells
Horses
Humanities and Social Sciences
Humans
Kinases
MAP kinase
Mice
multidisciplinary
Necroptosis
Necrosis - metabolism
Oligomers
Phosphorylation
Protein Conformation
Protein Kinases - chemistry
Rats
Receptor-Interacting Protein Serine-Threonine Kinases - chemistry
Regulatory mechanisms (biology)
Science
Science (multidisciplinary)
Selectivity
Signal Transduction
Signaling
Smegmamorpha
Swine
U937 Cells
Vertebrates
Xenopus
Online AccessGet full text

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Abstract The MLKL pseudokinase is the terminal effector in the necroptosis cell death pathway. Phosphorylation by its upstream regulator, RIPK3, triggers MLKL’s conversion from a dormant cytoplasmic protein into oligomers that translocate to, and permeabilize, the plasma membrane to kill cells. The precise mechanisms underlying these processes are incompletely understood, and were proposed to differ between mouse and human cells. Here, we examine the divergence of activation mechanisms among nine vertebrate MLKL orthologues, revealing remarkable specificity of mouse and human RIPK3 for MLKL orthologues. Pig MLKL can restore necroptotic signaling in human cells; while horse and pig, but not rat, MLKL can reconstitute the mouse pathway. This selectivity can be rationalized from the distinct conformations observed in the crystal structures of horse and rat MLKL pseudokinase domains. These studies identify important differences in necroptotic signaling between species, and suggest that, more broadly, divergent regulatory mechanisms may exist among orthologous pseudoenzymes. The necroptotic cell death pathway involves signaling through pseudokinases. Here the authors define the structural determinants of species specificity in necroptosis signaling mediated by the essential necroptotic effector pseudokinase, Mixed Lineage Kinase Domain-Like (MLKL).
AbstractList The necroptotic cell death pathway involves signaling through pseudokinases. Here the authors define the structural determinants of species specificity in necroptosis signaling mediated by the essential necroptotic effector pseudokinase, Mixed Lineage Kinase Domain-Like (MLKL).
The MLKL pseudokinase is the terminal effector in the necroptosis cell death pathway. Phosphorylation by its upstream regulator, RIPK3, triggers MLKL’s conversion from a dormant cytoplasmic protein into oligomers that translocate to, and permeabilize, the plasma membrane to kill cells. The precise mechanisms underlying these processes are incompletely understood, and were proposed to differ between mouse and human cells. Here, we examine the divergence of activation mechanisms among nine vertebrate MLKL orthologues, revealing remarkable specificity of mouse and human RIPK3 for MLKL orthologues. Pig MLKL can restore necroptotic signaling in human cells; while horse and pig, but not rat, MLKL can reconstitute the mouse pathway. This selectivity can be rationalized from the distinct conformations observed in the crystal structures of horse and rat MLKL pseudokinase domains. These studies identify important differences in necroptotic signaling between species, and suggest that, more broadly, divergent regulatory mechanisms may exist among orthologous pseudoenzymes. The necroptotic cell death pathway involves signaling through pseudokinases. Here the authors define the structural determinants of species specificity in necroptosis signaling mediated by the essential necroptotic effector pseudokinase, Mixed Lineage Kinase Domain-Like (MLKL).
The MLKL pseudokinase is the terminal effector in the necroptosis cell death pathway. Phosphorylation by its upstream regulator, RIPK3, triggers MLKL’s conversion from a dormant cytoplasmic protein into oligomers that translocate to, and permeabilize, the plasma membrane to kill cells. The precise mechanisms underlying these processes are incompletely understood, and were proposed to differ between mouse and human cells. Here, we examine the divergence of activation mechanisms among nine vertebrate MLKL orthologues, revealing remarkable specificity of mouse and human RIPK3 for MLKL orthologues. Pig MLKL can restore necroptotic signaling in human cells; while horse and pig, but not rat, MLKL can reconstitute the mouse pathway. This selectivity can be rationalized from the distinct conformations observed in the crystal structures of horse and rat MLKL pseudokinase domains. These studies identify important differences in necroptotic signaling between species, and suggest that, more broadly, divergent regulatory mechanisms may exist among orthologous pseudoenzymes.The necroptotic cell death pathway involves signaling through pseudokinases. Here the authors define the structural determinants of species specificity in necroptosis signaling mediated by the essential necroptotic effector pseudokinase, Mixed Lineage Kinase Domain-Like (MLKL).
The MLKL pseudokinase is the terminal effector in the necroptosis cell death pathway. Phosphorylation by its upstream regulator, RIPK3, triggers MLKL's conversion from a dormant cytoplasmic protein into oligomers that translocate to, and permeabilize, the plasma membrane to kill cells. The precise mechanisms underlying these processes are incompletely understood, and were proposed to differ between mouse and human cells. Here, we examine the divergence of activation mechanisms among nine vertebrate MLKL orthologues, revealing remarkable specificity of mouse and human RIPK3 for MLKL orthologues. Pig MLKL can restore necroptotic signaling in human cells; while horse and pig, but not rat, MLKL can reconstitute the mouse pathway. This selectivity can be rationalized from the distinct conformations observed in the crystal structures of horse and rat MLKL pseudokinase domains. These studies identify important differences in necroptotic signaling between species, and suggest that, more broadly, divergent regulatory mechanisms may exist among orthologous pseudoenzymes.
Abstract The MLKL pseudokinase is the terminal effector in the necroptosis cell death pathway. Phosphorylation by its upstream regulator, RIPK3, triggers MLKL’s conversion from a dormant cytoplasmic protein into oligomers that translocate to, and permeabilize, the plasma membrane to kill cells. The precise mechanisms underlying these processes are incompletely understood, and were proposed to differ between mouse and human cells. Here, we examine the divergence of activation mechanisms among nine vertebrate MLKL orthologues, revealing remarkable specificity of mouse and human RIPK3 for MLKL orthologues. Pig MLKL can restore necroptotic signaling in human cells; while horse and pig, but not rat, MLKL can reconstitute the mouse pathway. This selectivity can be rationalized from the distinct conformations observed in the crystal structures of horse and rat MLKL pseudokinase domains. These studies identify important differences in necroptotic signaling between species, and suggest that, more broadly, divergent regulatory mechanisms may exist among orthologous pseudoenzymes.
ArticleNumber 3060
Author Coursier, Diane
Chalmers, James D.
Lucet, Isabelle S.
Fitzgibbon, Cheree
Patrick, Wayne M.
Garnish, Sarah E.
Liang, Lung-Yu
Sandow, Jarrod J.
Murphy, James M.
Yeung, Wayland
Petrie, Emma J.
Czabotar, Peter E.
Davies, Katherine A.
Kannan, Natarajan
Young, Samuel N.
Lehmann, Wil I. L.
Birkinshaw, Richard W.
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/32561735$$D View this record in MEDLINE/PubMed
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SSID ssj0000391844
Score 2.539838
Snippet The MLKL pseudokinase is the terminal effector in the necroptosis cell death pathway. Phosphorylation by its upstream regulator, RIPK3, triggers MLKL’s...
The MLKL pseudokinase is the terminal effector in the necroptosis cell death pathway. Phosphorylation by its upstream regulator, RIPK3, triggers MLKL's...
Abstract The MLKL pseudokinase is the terminal effector in the necroptosis cell death pathway. Phosphorylation by its upstream regulator, RIPK3, triggers...
The necroptotic cell death pathway involves signaling through pseudokinases. Here the authors define the structural determinants of species specificity in...
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pubmedcentral
proquest
crossref
pubmed
springer
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Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 3060
SubjectTerms 13/106
13/31
13/95
631/45/275
631/45/535/1266
631/80/82/2344
82/80
82/83
Activation
Animals
Apoptosis
Cell death
Chickens
Crystal structure
Crystallography, X-Ray
Cytoplasm - enzymology
Divergence
Domains
HEK293 Cells
Horses
Humanities and Social Sciences
Humans
Kinases
MAP kinase
Mice
multidisciplinary
Necroptosis
Necrosis - metabolism
Oligomers
Phosphorylation
Protein Conformation
Protein Kinases - chemistry
Rats
Receptor-Interacting Protein Serine-Threonine Kinases - chemistry
Regulatory mechanisms (biology)
Science
Science (multidisciplinary)
Selectivity
Signal Transduction
Signaling
Smegmamorpha
Swine
U937 Cells
Vertebrates
Xenopus
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Title Distinct pseudokinase domain conformations underlie divergent activation mechanisms among vertebrate MLKL orthologues
URI https://link.springer.com/article/10.1038/s41467-020-16823-3
https://www.ncbi.nlm.nih.gov/pubmed/32561735
https://www.proquest.com/docview/2414911891
https://search.proquest.com/docview/2415289473
https://pubmed.ncbi.nlm.nih.gov/PMC7305131
https://doaj.org/article/b93b0f25bce74b3387360f9736d00ebc
Volume 11
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