Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain

Mammalian GPI membrane anchors are modified by GalNAc to confer structural diversity but the biosynthetic pathway is poorly understood. Here, the authors identify and characterize the Golgi-resident GPI-GalNAc transferase PGAP4, providing insights into the initial step of GPI-GalNAc biosynthesis.

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Autores principales:	Tetsuya Hirata, Sushil K. Mishra, Shota Nakamura, Kazunobu Saito, Daisuke Motooka, Yoko Takada, Noriyuki Kanzawa, Yoshiko Murakami, Yusuke Maeda, Morihisa Fujita, Yoshiki Yamaguchi, Taroh Kinoshita
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/476885486e374cb9b0577fcd177b83ae
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spelling	oai:doaj.org-article:476885486e374cb9b0577fcd177b83ae2021-12-02T14:40:10ZIdentification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain10.1038/s41467-017-02799-02041-1723https://doaj.org/article/476885486e374cb9b0577fcd177b83ae2018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02799-0https://doaj.org/toc/2041-1723Mammalian GPI membrane anchors are modified by GalNAc to confer structural diversity but the biosynthetic pathway is poorly understood. Here, the authors identify and characterize the Golgi-resident GPI-GalNAc transferase PGAP4, providing insights into the initial step of GPI-GalNAc biosynthesis.Tetsuya HirataSushil K. MishraShota NakamuraKazunobu SaitoDaisuke MotookaYoko TakadaNoriyuki KanzawaYoshiko MurakamiYusuke MaedaMorihisa FujitaYoshiki YamaguchiTaroh KinoshitaNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-16 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Tetsuya Hirata Sushil K. Mishra Shota Nakamura Kazunobu Saito Daisuke Motooka Yoko Takada Noriyuki Kanzawa Yoshiko Murakami Yusuke Maeda Morihisa Fujita Yoshiki Yamaguchi Taroh Kinoshita Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain
description	Mammalian GPI membrane anchors are modified by GalNAc to confer structural diversity but the biosynthetic pathway is poorly understood. Here, the authors identify and characterize the Golgi-resident GPI-GalNAc transferase PGAP4, providing insights into the initial step of GPI-GalNAc biosynthesis.
format	article
author	Tetsuya Hirata Sushil K. Mishra Shota Nakamura Kazunobu Saito Daisuke Motooka Yoko Takada Noriyuki Kanzawa Yoshiko Murakami Yusuke Maeda Morihisa Fujita Yoshiki Yamaguchi Taroh Kinoshita
author_facet	Tetsuya Hirata Sushil K. Mishra Shota Nakamura Kazunobu Saito Daisuke Motooka Yoko Takada Noriyuki Kanzawa Yoshiko Murakami Yusuke Maeda Morihisa Fujita Yoshiki Yamaguchi Taroh Kinoshita
author_sort	Tetsuya Hirata
title	Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain
title_short	Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain
title_full	Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain
title_fullStr	Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain
title_full_unstemmed	Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain
title_sort	identification of a golgi gpi-n-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/476885486e374cb9b0577fcd177b83ae
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Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain

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