Ubiquitylation of MLKL at lysine 219 positively regulates necroptosis-induced tissue injury and pathogen clearance

Ubiquitylation of MLKL at lysine 219 positively regulates necroptosis-induced tissue injury and pathogen clearance

Necroptosis is a form of cell death characterized by membrane rupture via MLKL oligomerization, although mechanistic details remain unclear. Here, the authors show that MLKL ubiquitylation of K219 facilitates high-order membrane assembly and subsequent rupture, promoting cytotoxicity.

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Autores principales: Laura Ramos Garcia, Tencho Tenev, Richard Newman, Rachel O. Haich, Gianmaria Liccardi, Sidonie Wicky John, Alessandro Annibaldi, Lu Yu, Mercedes Pardo, Samuel N. Young, Cheree Fitzgibbon, Winnie Fernando, Naomi Guppy, Hyojin Kim, Lung-Yu Liang, Isabelle S. Lucet, Andrew Kueh, Ioannis Roxanis, Patrycja Gazinska, Martin Sims, Tomoko Smyth, George Ward, John Bertin, Allison M. Beal, Brad Geddes, Jyoti S. Choudhary, James M. Murphy, K. Aurelia Ball, Jason W. Upton, Pascal Meier
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/028b10c801d94af293be6d1707508113
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spelling oai:doaj.org-article:028b10c801d94af293be6d17075081132021-12-02T18:06:24ZUbiquitylation of MLKL at lysine 219 positively regulates necroptosis-induced tissue injury and pathogen clearance10.1038/s41467-021-23474-52041-1723https://doaj.org/article/028b10c801d94af293be6d17075081132021-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23474-5https://doaj.org/toc/2041-1723Necroptosis is a form of cell death characterized by membrane rupture via MLKL oligomerization, although mechanistic details remain unclear. Here, the authors show that MLKL ubiquitylation of K219 facilitates high-order membrane assembly and subsequent rupture, promoting cytotoxicity.Laura Ramos GarciaTencho TenevRichard NewmanRachel O. HaichGianmaria LiccardiSidonie Wicky JohnAlessandro AnnibaldiLu YuMercedes PardoSamuel N. YoungCheree FitzgibbonWinnie FernandoNaomi GuppyHyojin KimLung-Yu LiangIsabelle S. LucetAndrew KuehIoannis RoxanisPatrycja GazinskaMartin SimsTomoko SmythGeorge WardJohn BertinAllison M. BealBrad GeddesJyoti S. ChoudharyJames M. MurphyK. Aurelia BallJason W. UptonPascal MeierNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Laura Ramos Garcia
Tencho Tenev
Richard Newman
Rachel O. Haich
Gianmaria Liccardi
Sidonie Wicky John
Alessandro Annibaldi
Lu Yu
Mercedes Pardo
Samuel N. Young
Cheree Fitzgibbon
Winnie Fernando
Naomi Guppy
Hyojin Kim
Lung-Yu Liang
Isabelle S. Lucet
Andrew Kueh
Ioannis Roxanis
Patrycja Gazinska
Martin Sims
Tomoko Smyth
George Ward
John Bertin
Allison M. Beal
Brad Geddes
Jyoti S. Choudhary
James M. Murphy
K. Aurelia Ball
Jason W. Upton
Pascal Meier
Ubiquitylation of MLKL at lysine 219 positively regulates necroptosis-induced tissue injury and pathogen clearance
description Necroptosis is a form of cell death characterized by membrane rupture via MLKL oligomerization, although mechanistic details remain unclear. Here, the authors show that MLKL ubiquitylation of K219 facilitates high-order membrane assembly and subsequent rupture, promoting cytotoxicity.
format article
author Laura Ramos Garcia
Tencho Tenev
Richard Newman
Rachel O. Haich
Gianmaria Liccardi
Sidonie Wicky John
Alessandro Annibaldi
Lu Yu
Mercedes Pardo
Samuel N. Young
Cheree Fitzgibbon
Winnie Fernando
Naomi Guppy
Hyojin Kim
Lung-Yu Liang
Isabelle S. Lucet
Andrew Kueh
Ioannis Roxanis
Patrycja Gazinska
Martin Sims
Tomoko Smyth
George Ward
John Bertin
Allison M. Beal
Brad Geddes
Jyoti S. Choudhary
James M. Murphy
K. Aurelia Ball
Jason W. Upton
Pascal Meier
author_facet Laura Ramos Garcia
Tencho Tenev
Richard Newman
Rachel O. Haich
Gianmaria Liccardi
Sidonie Wicky John
Alessandro Annibaldi
Lu Yu
Mercedes Pardo
Samuel N. Young
Cheree Fitzgibbon
Winnie Fernando
Naomi Guppy
Hyojin Kim
Lung-Yu Liang
Isabelle S. Lucet
Andrew Kueh
Ioannis Roxanis
Patrycja Gazinska
Martin Sims
Tomoko Smyth
George Ward
John Bertin
Allison M. Beal
Brad Geddes
Jyoti S. Choudhary
James M. Murphy
K. Aurelia Ball
Jason W. Upton
Pascal Meier
author_sort Laura Ramos Garcia
title Ubiquitylation of MLKL at lysine 219 positively regulates necroptosis-induced tissue injury and pathogen clearance
title_short Ubiquitylation of MLKL at lysine 219 positively regulates necroptosis-induced tissue injury and pathogen clearance
title_full Ubiquitylation of MLKL at lysine 219 positively regulates necroptosis-induced tissue injury and pathogen clearance
title_fullStr Ubiquitylation of MLKL at lysine 219 positively regulates necroptosis-induced tissue injury and pathogen clearance
title_full_unstemmed Ubiquitylation of MLKL at lysine 219 positively regulates necroptosis-induced tissue injury and pathogen clearance
title_sort ubiquitylation of mlkl at lysine 219 positively regulates necroptosis-induced tissue injury and pathogen clearance
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/028b10c801d94af293be6d1707508113
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