Evidence map›Paper›PMID 29374258›Full record

ArticleNature communications2018

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

Tetsuya Hirata, Sushil K Mishra, Shota Nakamura, Kazunobu Saito, Daisuke Motooka, Yoko Takada, Noriyuki Kanzawa, Yoshiko Murakami, Yusuke Maeda, Morihisa Fujita and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.2field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 49 citations in OpenAlex.

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  8. Research progress on the mechanism of exosome-mediated virus infection.Frontiers in cellular and infection microbiology · 2024
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  18. Article
  19. Global view of human protein glycosylation pathways and functions.Nature reviews. Molecular cell biology · 2020
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 4 institutions in 2 countries.

Tetsuya HirataResearch Institute for Microbial Diseases, Osaka University, Suita, Osaka, 565-0871, Japan.
Sushil K MishraStructural Glycobiology Team, Systems Glycobiology Research Group, RIKEN Global Research Cluster, Wako, Saitama, 351-0198, Japan.ORCID http://orcid.org/0000-0002-3080-9754
Shota NakamuraResearch Institute for Microbial Diseases, Osaka University, Suita, Osaka, 565-0871, Japan.
Kazunobu SaitoResearch Institute for Microbial Diseases, Osaka University, Suita, Osaka, 565-0871, Japan.
Daisuke MotookaResearch Institute for Microbial Diseases, Osaka University, Suita, Osaka, 565-0871, Japan.
Yoko TakadaWPI Immunology Frontier Research Center, Osaka University, Suita, Osaka, 565-0871, Japan.
Noriyuki KanzawaResearch Institute for Microbial Diseases, Osaka University, Suita, Osaka, 565-0871, Japan.
Yoshiko MurakamiResearch Institute for Microbial Diseases, Osaka University, Suita, Osaka, 565-0871, Japan.
Yusuke MaedaResearch Institute for Microbial Diseases, Osaka University, Suita, Osaka, 565-0871, Japan.
Morihisa FujitaKey Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, Jiangsu, 214122, China.
Yoshiki YamaguchiStructural Glycobiology Team, Systems Glycobiology Research Group, RIKEN Global Research Cluster, Wako, Saitama, 351-0198, Japan.
Taroh KinoshitaResearch Institute for Microbial Diseases, Osaka University, Suita, Osaka, 565-0871, Japan. tkinoshi@biken.osaka-u.ac.jp.ORCID http://orcid.org/0000-0001-7166-7257
The University of Osaka · JPRIKEN · JPJiangnan University · CNNational Institutes of Natural Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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. Furthermore, we demonstrate that PGAP4, in contrast to known Golgi glycosyltransferases, is not a single-pass membrane protein but contains three transmembrane domains, including a tandem transmembrane domain insertion into its glycosyltransferase-A fold as indicated by comparative modeling. Mutational analysis reveals a catalytic site, a DXD-like motif for UDP-GalNAc donor binding, and several residues potentially involved in acceptor binding. We suggest that a juxtamembrane region of PGAP4 accommodates various GPI-anchored proteins, presenting their acceptor residue toward the catalytic center. In summary, we present insights into the structure of PGAP4 and elucidate the initial step of GPI-GalNAc biosynthesis.

Indexed as

AcetylgalactosamineAmino Acid MotifsAnimalsCatalytic DomainCHO CellsCricetulusCrystallography, X-RayGene ExpressionGenetic VectorsGlycosylphosphatidylinositolsGolgi ApparatusHumansMiceMice, KnockoutModels, MolecularMutationAcetylgalactosamineGlycosylphosphatidylinositolsN-AcetylgalactosaminyltransferasesPolypeptide N-acetylgalactosaminyltransferase

Identifiers

PMID29374258
PMCPMC5785973
OpenAlexW2800781359

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.