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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Detalles Bibliográficos
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
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Acceso en línea:https://doaj.org/article/476885486e374cb9b0577fcd177b83ae
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Sumario: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.