Evidence map›Paper›PMID 24584735›Full record

ArticleScientific reports2014

Inhibition of post-translational N-glycosylation by HRD1 that controls the fate of ABCG5/8 transporter.

Shingo Suzuki, Tsuyoshi Shuto, Takashi Sato, Masayuki Kaneko, Tappei Takada, Mary Ann Suico, Douglas M Cyr, Hiroshi Suzuki, Hirofumi Kai

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

8 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
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  4. Trimerization and Genotype-Phenotype Correlation ofKidney international reports · 2020
    Article
  5. Article
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  7. Review
  8. 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

9 authors at 3 institutions in 2 countries.

Shingo Suzuki1] Department of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-Honmachi, Chuo-Ku, Kumamoto 862-0973, Japan [2].
Tsuyoshi Shuto1] Department of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-Honmachi, Chuo-Ku, Kumamoto 862-0973, Japan [2].
Takashi Sato1] Department of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-Honmachi, Chuo-Ku, Kumamoto 862-0973, Japan [2].
Masayuki KanekoDepartment of Medical Therapeutics and Molecular Therapeutics, Gifu Pharmaceutical University, 1-25-4 Daigaku-nishi, Gifu 501-1196, Japan.
Tappei TakadaDepartment of Pharmacy, The University of Tokyo Hospital, Faculty of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8655, Japan.
Mary Ann SuicoDepartment of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-Honmachi, Chuo-Ku, Kumamoto 862-0973, Japan.
Douglas M CyrDepartment of Cell and Developmental Biology, School of Medicine, 526 Taylor Hall, University of North Carolina, Chapel Hill, North Carolina 27599-7090, USA.
Hiroshi SuzukiDepartment of Pharmacy, The University of Tokyo Hospital, Faculty of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8655, Japan.
Hirofumi KaiDepartment of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-Honmachi, Chuo-Ku, Kumamoto 862-0973, Japan.
Kumamoto University · JPUniversity of Tokyo Hospital · JPUniversity of North Carolina at Chapel Hill · US

Funding

Roles for Hsp70 and Hsp40 in Membrane Protein TriageR01GM056981 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CYR, DOUGLAS M · 1998 to 2019
$6.1M
NIGMS NIH HHS R01 GM056981
6 · The paper itself

Abstract

N-glycosylation of proteins in endoplasmic reticulum is critical for protein quality control. We showed here a post-translational N-glycosylation affected by the HRD1 E3 ubiquitin ligase. Both WT- and E3-defective C329S-HRD1 decreased the level of high mannose form of ABCG8, a protein that heterodimerizes with ABCG5 to control sterol balance. Meanwhile, HRD1 increased the non-glycosylated ABCG8 regardless of its E3 activity, thereby suppressing full maturation of ABCG5/8 transporter. Pulse chase and mutational analysis indicated that HRD1 inhibits STT3B-dependent post-translational N-glycosylation of ABCG8. Whereas, HRD1 had only slight effect on the N-glycosylation status of ABCG5; rather it accelerated ABCG5 degradation in an E3 activity-dependent manner. Finally, RMA1, another E3 ubiquitin ligase, accelerated the degradation of both ABCG5 and ABCG8 via E3 activity-dependent manner. HRD1 and RMA1 may therefore be negative regulators of disease-associated transporter ABCG5/ABCG8. The findings also highlight the unexpected E3 activity-independent role of HRD1 in the regulation of N-glycosylation.

Indexed as

ATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily G, Member 5ATP Binding Cassette Transporter, Subfamily G, Member 8Feedback, PhysiologicalGlycosylationHumansLipoproteinsProtein Processing, Post-TranslationalUbiquitin-Protein LigasesABCG5 protein, humanABCG8 protein, humanATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily G, Member 5ATP Binding Cassette Transporter, Subfamily G, Member 8LipoproteinsSYVN1 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID24584735
PMCPMC3939451
OpenAlexW1992935237

What OpenQuestion holds

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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.