Autophosphorylation at serine 166 regulates RIP kinase 1-mediated cell death and inflammation

Receptor interacting protein kinase 1 (RIPK1) regulates cell death and inflammatory responses. Here the authors show that autophosphorylation at Ser166 is required for RIPK1-mediated cell death and inflammation in mouse models of inflammatory pathologies, making Ser166 phosphorylation a possible bio...

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Autores principales:	Lucie Laurien, Masahiro Nagata, Hannah Schünke, Tom Delanghe, Janica L. Wiederstein, Snehlata Kumari, Robin Schwarzer, Teresa Corona, Marcus Krüger, Mathieu J. M. Bertrand, Vangelis Kondylis, Manolis Pasparakis
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/2d82135048944fbfa5ea87adae76d9b0
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spelling	oai:doaj.org-article:2d82135048944fbfa5ea87adae76d9b02021-12-02T17:32:13ZAutophosphorylation at serine 166 regulates RIP kinase 1-mediated cell death and inflammation10.1038/s41467-020-15466-82041-1723https://doaj.org/article/2d82135048944fbfa5ea87adae76d9b02020-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15466-8https://doaj.org/toc/2041-1723Receptor interacting protein kinase 1 (RIPK1) regulates cell death and inflammatory responses. Here the authors show that autophosphorylation at Ser166 is required for RIPK1-mediated cell death and inflammation in mouse models of inflammatory pathologies, making Ser166 phosphorylation a possible biomarker for RIPK1-mediated inflammatory diseases.Lucie LaurienMasahiro NagataHannah SchünkeTom DelangheJanica L. WiedersteinSnehlata KumariRobin SchwarzerTeresa CoronaMarcus KrügerMathieu J. M. BertrandVangelis KondylisManolis PasparakisNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Lucie Laurien Masahiro Nagata Hannah Schünke Tom Delanghe Janica L. Wiederstein Snehlata Kumari Robin Schwarzer Teresa Corona Marcus Krüger Mathieu J. M. Bertrand Vangelis Kondylis Manolis Pasparakis Autophosphorylation at serine 166 regulates RIP kinase 1-mediated cell death and inflammation
description	Receptor interacting protein kinase 1 (RIPK1) regulates cell death and inflammatory responses. Here the authors show that autophosphorylation at Ser166 is required for RIPK1-mediated cell death and inflammation in mouse models of inflammatory pathologies, making Ser166 phosphorylation a possible biomarker for RIPK1-mediated inflammatory diseases.
format	article
author	Lucie Laurien Masahiro Nagata Hannah Schünke Tom Delanghe Janica L. Wiederstein Snehlata Kumari Robin Schwarzer Teresa Corona Marcus Krüger Mathieu J. M. Bertrand Vangelis Kondylis Manolis Pasparakis
author_facet	Lucie Laurien Masahiro Nagata Hannah Schünke Tom Delanghe Janica L. Wiederstein Snehlata Kumari Robin Schwarzer Teresa Corona Marcus Krüger Mathieu J. M. Bertrand Vangelis Kondylis Manolis Pasparakis
author_sort	Lucie Laurien
title	Autophosphorylation at serine 166 regulates RIP kinase 1-mediated cell death and inflammation
title_short	Autophosphorylation at serine 166 regulates RIP kinase 1-mediated cell death and inflammation
title_full	Autophosphorylation at serine 166 regulates RIP kinase 1-mediated cell death and inflammation
title_fullStr	Autophosphorylation at serine 166 regulates RIP kinase 1-mediated cell death and inflammation
title_full_unstemmed	Autophosphorylation at serine 166 regulates RIP kinase 1-mediated cell death and inflammation
title_sort	autophosphorylation at serine 166 regulates rip kinase 1-mediated cell death and inflammation
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/2d82135048944fbfa5ea87adae76d9b0
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Autophosphorylation at serine 166 regulates RIP kinase 1-mediated cell death and inflammation

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