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Article

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

Nature communications - 26 Jan 2018

Hirata Tetsuya, Mishra Sushil K, Nakamura Shota, Saito Kazunobu, Motooka Daisuke, Takada Yoko, Kanzawa Noriyuki, Murakami Yoshiko, Maeda Yusuke, Fujita Morihisa, Yamaguchi Yoshiki, Kinoshita Taroh

Abstract excerpt

Many eukaryotic proteins are anchored to the cell surface via the glycolipid glycosylphosphatidylinositol (GPI). Mammalian GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications, which are added via a yet unresolved process. Here we identify the Golgi-resident GPI-GalNAc transferase PGAP4 and show by mass spectrometry that PGAP4 knockout cells lose GPI-GalNAc structures....

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Source

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Identifiers

PMID: 29374258
DOI: 10.1038/s41467-017-02799-0
PMCID: PMC5785973

Genes

GPI
PGAP4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain.PMID 29374258Read ↗

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