Structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy

Alkaline ceramidases (ACERs) are a class of poorly understood transmembrane enzymes controlling the homeostasis of ceramides. Here authors solve the Xray structure of human ACER3 and uncover a Ca2+ binding site providing an explanation for the known regulatory role of Ca2+ on ACER3 activity.

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Autores principales:	Ieva Vasiliauskaité-Brooks, Robert D. Healey, Pascal Rochaix, Julie Saint-Paul, Rémy Sounier, Claire Grison, Thierry Waltrich-Augusto, Mathieu Fortier, François Hoh, Essa M. Saied, Christoph Arenz, Shibom Basu, Cédric Leyrat, Sébastien Granier
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/9944c8e0584f421dad2c7d0bf7a0b051
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spelling	oai:doaj.org-article:9944c8e0584f421dad2c7d0bf7a0b0512021-12-02T14:39:08ZStructure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy10.1038/s41467-018-07864-w2041-1723https://doaj.org/article/9944c8e0584f421dad2c7d0bf7a0b0512018-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07864-whttps://doaj.org/toc/2041-1723Alkaline ceramidases (ACERs) are a class of poorly understood transmembrane enzymes controlling the homeostasis of ceramides. Here authors solve the Xray structure of human ACER3 and uncover a Ca2+ binding site providing an explanation for the known regulatory role of Ca2+ on ACER3 activity.Ieva Vasiliauskaité-BrooksRobert D. HealeyPascal RochaixJulie Saint-PaulRémy SounierClaire GrisonThierry Waltrich-AugustoMathieu FortierFrançois HohEssa M. SaiedChristoph ArenzShibom BasuCédric LeyratSébastien GranierNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ieva Vasiliauskaité-Brooks Robert D. Healey Pascal Rochaix Julie Saint-Paul Rémy Sounier Claire Grison Thierry Waltrich-Augusto Mathieu Fortier François Hoh Essa M. Saied Christoph Arenz Shibom Basu Cédric Leyrat Sébastien Granier Structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy
description	Alkaline ceramidases (ACERs) are a class of poorly understood transmembrane enzymes controlling the homeostasis of ceramides. Here authors solve the Xray structure of human ACER3 and uncover a Ca2+ binding site providing an explanation for the known regulatory role of Ca2+ on ACER3 activity.
format	article
author	Ieva Vasiliauskaité-Brooks Robert D. Healey Pascal Rochaix Julie Saint-Paul Rémy Sounier Claire Grison Thierry Waltrich-Augusto Mathieu Fortier François Hoh Essa M. Saied Christoph Arenz Shibom Basu Cédric Leyrat Sébastien Granier
author_facet	Ieva Vasiliauskaité-Brooks Robert D. Healey Pascal Rochaix Julie Saint-Paul Rémy Sounier Claire Grison Thierry Waltrich-Augusto Mathieu Fortier François Hoh Essa M. Saied Christoph Arenz Shibom Basu Cédric Leyrat Sébastien Granier
author_sort	Ieva Vasiliauskaité-Brooks
title	Structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy
title_short	Structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy
title_full	Structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy
title_fullStr	Structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy
title_full_unstemmed	Structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy
title_sort	structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/9944c8e0584f421dad2c7d0bf7a0b051
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Structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy

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