A signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD

The Arabidopsis ER-α-mannosidase I MNS3 generates N-glycan structures typical of ER-resident glycoproteins. Here Schoberer et al. identify a novel motif that anchors MNS3 to the cis-Golgi, spatially separating MNS3 from ER-localized mannose trimming associated with the ER-associated degradation path...

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Autores principales: Jennifer Schoberer, Julia König, Christiane Veit, Ulrike Vavra, Eva Liebminger, Stanley W. Botchway, Friedrich Altmann, Verena Kriechbaumer, Chris Hawes, Richard Strasser
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Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/ae45cf92025043e39d2f6156ceaa447d
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spelling oai:doaj.org-article:ae45cf92025043e39d2f6156ceaa447d2021-12-02T14:39:16ZA signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD10.1038/s41467-019-11686-92041-1723https://doaj.org/article/ae45cf92025043e39d2f6156ceaa447d2019-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11686-9https://doaj.org/toc/2041-1723The Arabidopsis ER-α-mannosidase I MNS3 generates N-glycan structures typical of ER-resident glycoproteins. Here Schoberer et al. identify a novel motif that anchors MNS3 to the cis-Golgi, spatially separating MNS3 from ER-localized mannose trimming associated with the ER-associated degradation pathway.Jennifer SchobererJulia KönigChristiane VeitUlrike VavraEva LiebmingerStanley W. BotchwayFriedrich AltmannVerena KriechbaumerChris HawesRichard StrasserNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Jennifer Schoberer
Julia König
Christiane Veit
Ulrike Vavra
Eva Liebminger
Stanley W. Botchway
Friedrich Altmann
Verena Kriechbaumer
Chris Hawes
Richard Strasser
A signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD
description The Arabidopsis ER-α-mannosidase I MNS3 generates N-glycan structures typical of ER-resident glycoproteins. Here Schoberer et al. identify a novel motif that anchors MNS3 to the cis-Golgi, spatially separating MNS3 from ER-localized mannose trimming associated with the ER-associated degradation pathway.
format article
author Jennifer Schoberer
Julia König
Christiane Veit
Ulrike Vavra
Eva Liebminger
Stanley W. Botchway
Friedrich Altmann
Verena Kriechbaumer
Chris Hawes
Richard Strasser
author_facet Jennifer Schoberer
Julia König
Christiane Veit
Ulrike Vavra
Eva Liebminger
Stanley W. Botchway
Friedrich Altmann
Verena Kriechbaumer
Chris Hawes
Richard Strasser
author_sort Jennifer Schoberer
title A signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD
title_short A signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD
title_full A signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD
title_fullStr A signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD
title_full_unstemmed A signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD
title_sort signal motif retains arabidopsis er-α-mannosidase i in the cis-golgi and prevents enhanced glycoprotein erad
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/ae45cf92025043e39d2f6156ceaa447d
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