Cryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate

The core FADD:Caspase-8 complex and its regulatory partners, such as the cell death inhibitor c-FLIP, coordinate cell fate. Here authors present the structure of full-length procaspase-8 in a complex with FADD and reveal how recruitment of c-FLIPS into this complex inhibits Caspase-8 activity.

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Autores principales:	Joanna L. Fox, Michelle A. Hughes, Xin Meng, Nikola A. Sarnowska, Ian R. Powley, Rebekah Jukes-Jones, David Dinsdale, Timothy J. Ragan, Louise Fairall, John W. R. Schwabe, Nobuhiro Morone, Kelvin Cain, Marion MacFarlane
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/cbf43a167d5c47dbbf9efdc46a691fd7
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spelling	oai:doaj.org-article:cbf43a167d5c47dbbf9efdc46a691fd72021-12-02T10:44:18ZCryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate10.1038/s41467-020-20806-92041-1723https://doaj.org/article/cbf43a167d5c47dbbf9efdc46a691fd72021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20806-9https://doaj.org/toc/2041-1723The core FADD:Caspase-8 complex and its regulatory partners, such as the cell death inhibitor c-FLIP, coordinate cell fate. Here authors present the structure of full-length procaspase-8 in a complex with FADD and reveal how recruitment of c-FLIPS into this complex inhibits Caspase-8 activity.Joanna L. FoxMichelle A. HughesXin MengNikola A. SarnowskaIan R. PowleyRebekah Jukes-JonesDavid DinsdaleTimothy J. RaganLouise FairallJohn W. R. SchwabeNobuhiro MoroneKelvin CainMarion MacFarlaneNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-17 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Joanna L. Fox Michelle A. Hughes Xin Meng Nikola A. Sarnowska Ian R. Powley Rebekah Jukes-Jones David Dinsdale Timothy J. Ragan Louise Fairall John W. R. Schwabe Nobuhiro Morone Kelvin Cain Marion MacFarlane Cryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate
description	The core FADD:Caspase-8 complex and its regulatory partners, such as the cell death inhibitor c-FLIP, coordinate cell fate. Here authors present the structure of full-length procaspase-8 in a complex with FADD and reveal how recruitment of c-FLIPS into this complex inhibits Caspase-8 activity.
format	article
author	Joanna L. Fox Michelle A. Hughes Xin Meng Nikola A. Sarnowska Ian R. Powley Rebekah Jukes-Jones David Dinsdale Timothy J. Ragan Louise Fairall John W. R. Schwabe Nobuhiro Morone Kelvin Cain Marion MacFarlane
author_facet	Joanna L. Fox Michelle A. Hughes Xin Meng Nikola A. Sarnowska Ian R. Powley Rebekah Jukes-Jones David Dinsdale Timothy J. Ragan Louise Fairall John W. R. Schwabe Nobuhiro Morone Kelvin Cain Marion MacFarlane
author_sort	Joanna L. Fox
title	Cryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate
title_short	Cryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate
title_full	Cryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate
title_fullStr	Cryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate
title_full_unstemmed	Cryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate
title_sort	cryo-em structural analysis of fadd:caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/cbf43a167d5c47dbbf9efdc46a691fd7
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Cryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate

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