Evidence map›Paper›PMID 21184741›Full record

ArticleBiochemical and biophysical research communications2011

Posttranslational negative regulation of glycosylated and non-glycosylated BCRP expression by Derlin-1.

Takashi Sugiyama, Tsuyoshi Shuto, Shingo Suzuki, Takashi Sato, Tomoaki Koga, Mary Ann Suico, Hiroyuki Kusuhara, Yuichi Sugiyama, Douglas M Cyr, Hirofumi Kai

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Multidrug efflux transporter ABCG2: expression and regulation.Cellular and molecular life sciences : CMLS · 2021
    Review
  4. Pancreatic Cancer and Therapy: Role and Regulation of Cancer Stem Cells.International journal of molecular sciences · 2021
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Impaired N-linked glycosylation of uptake and efflux transporters in human non-alcoholic fatty liver disease.Liver international : official journal of the International Association for the Study of the Liver · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Human ABCG2: structure, function, and its role in multidrug resistance.International journal of biochemistry and molecular biology · 2012
    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

10 authors at 3 institutions in 2 countries.

Takashi SugiyamaDepartment of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Global COE Cell Fate Regulation Research and Education Unit, Kumamoto University, 5-1 Oe-Honmachi, Kumamoto 862-0973, Japan.
Tsuyoshi Shuto
Shingo Suzuki
Takashi Sato
Tomoaki Koga
Mary Ann Suico
Hiroyuki Kusuhara
Yuichi Sugiyama
Douglas M Cyr
Hirofumi Kai
Kumamoto University · JPThe University of Tokyo · 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

Human breast cancer resistance protein (BCRP)/MXR/ABCG2 is a well-recognized ABC half-transporter that is highly expressed at the apical membrane of many normal tissues and cancer cells. BCRP facilitates disposition of endogenous and exogenous harmful xenobiotics to protect cells/tissues from xenobiotic-induced toxicity. Despite the enormous impact of BCRP in the physiological and pathophysiological regulation of the transport of a wide variety of substrates, little is known about the factors that regulate posttranslational expression of BCRP. Here, we identified Derlin-1, a member of a family of proteins that bears homology to yeast Der1p, as a posttranslational regulator of BCRP expression. Overexpression of Derlin-1 suppressed ER to Golgi transport of wild-type (WT) BCRP that is known to be efficiently trafficked to the plasma membrane. On the other hand, protein expression of N596Q variant of BCRP, N-linked glycosylation-deficient mutant that preferentially undergoes ubiquitin-mediated ER-associated degradation (ERAD), was strongly suppressed by the overexpression of Derlin-1, whereas knockdown of Derlin-1 stabilized N596Q protein, suggesting a negative regulatory role of Derlin-1 for N596Q protein expression. Notably, knockdown of Derlin-1 also stabilized the expression of tunicamycin-induced deglycosylated WT BCRP protein, implying the importance of glycosylation state for the recognition of BCRP by Derlin-1. Thus, our data demonstrate that Derlin-1 is a negative regulator for both glycosylated and non-glycosylated BCRP expression and provide a novel posttranslational regulatory mechanism of BCRP by Derlin-1.

Indexed as

ATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily G, Member 2Endoplasmic ReticulumGlycosylationHumansMembrane ProteinsNeoplasm ProteinsProtein Processing, Post-TranslationalABCG2 protein, humanATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily G, Member 2DERL1 protein, humanMembrane ProteinsNeoplasm Proteins

Identifiers

PMID21184741
PMCPMC4457448
OpenAlexW2078754096

What OpenQuestion holds

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LicenceTDM
Read underepoch 390

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.