Evidence map›Paper›PMID 28644885›Full record

ArticlePloS one2017

Organic anion transporting polypeptide 1B3 can form homo- and hetero-oligomers.

Yuchen Zhang, Kelli H Boxberger, Bruno Hagenbuch

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

18 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. AssessingPharmaceutics · 2023
    Article
  6. Interaction of Human OATP1B1 with PDZK1 Is Required for Its Trafficking to the Hepatocyte Plasma Membrane.Drug metabolism and disposition: the biological fate of chemicals · 2023
    Article
  7. Article
  8. Free Cholesterol Affects the Function and Localization of Human NaInternational journal of molecular sciences · 2022
    Article
  9. Article
  10. Localization of Xenobiotic Transporters Expressed at the Human Blood-Testis Barrier.Drug metabolism and disposition: the biological fate of chemicals · 2022
    Article
  11. Article
  12. Review
  13. OATP1B3 Expression and Function is Modulated by Coexpression with OCT1, OATP1B1, and NTCP.Drug metabolism and disposition: the biological fate of chemicals · 2020
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. 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

3 authors at 1 institution in 1 country.

Yuchen ZhangDepartment of Pharmacology, Toxicology and Therapeutics, the University of Kansas Medical Center, Kansas City, Kansas, United States of America.
Kelli H BoxbergerDepartment of Pharmacology, Toxicology and Therapeutics, the University of Kansas Medical Center, Kansas City, Kansas, United States of America.
Bruno HagenbuchDepartment of Pharmacology, Toxicology and Therapeutics, the University of Kansas Medical Center, Kansas City, Kansas, United States of America.ORCID http://orcid.org/0000-0002-2938-8630
University of Kansas Medical Center · US

Funding

Pilot Grants ProgramP30GM118247 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI JAESCHKE, HARTMUT W. · 2016 to 2020
$5.5M
Molecular Characterization of Hepatic Organic Anion Transporting PolypeptidesR01GM077336 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI HAGENBUCH, BRUNO · 2007 to 2019
$3.7M
NIGMS NIH HHS P30 GM118247NIGMS NIH HHS R01 GM077336
6 · The paper itself

Abstract

OATP1B3 is a 12 transmembrane domain protein expressed at the basolateral membrane of human hepatocytes where it mediates the uptake of numerous drugs and endogenous compounds. Previous western blot results suggest the formation of OATP1B3 multimers. In order to better understand the function of OATP1B3 under normal physiological conditions, we investigated its oligomerization status. We transiently transfected OATP1B3 with a C-terminal His-, FLAG- or HA-tag in HEK293 cells and used co-immunoprecipitation and a Proximity Ligation Assay to detect interactions between the different constructs. All three constructs retained similar transport rates as wild-type OATP1B3. Immunofluorescence experiments indicated that in contrast to wild-type, His- and FLAG-tagged OATP1B3, where the C-terminal end is on the cytoplasmic side of the membrane, the C-terminal end of HA-tagged OATP1B3 is extracellular. After cross-linking, anti-FLAG antibodies were able to pull down FLAG-tagged OATP1B3 (positive control) and co-transfected His- or HA-tagged OATP1B3, demonstrating the formation of homo-oligomers and suggesting that the C-terminal part is not involved in oligomer formation. We confirmed co-localization of His- and FLAG-tagged OATP1B3 in transfected HEK293 cells with the Proximity Ligation Assay. Transport studies with a non-functional OATP1B3 mutant suggest that the individual subunits and not the whole oligomer are the functional units in the homo-oligomers. In addition, we also detected OATP1B3-FLAG co-localization with OATP1B1-His or NTCP-His, suggesting that OATP1B3 also hetero-oligomerizes with other transport proteins. Using the Proximity Ligation Assay with transporter specific antibodies, we demonstrate close association of OATP1B3 with NTCP in frozen human liver tissue. These findings demonstrate that OATP1B3 can form homo- and hetero-oligomers and suggest a potential co-regulation of the involved transporters.

Indexed as

Blotting, WesternCytoplasmExtracellular SpaceFluorescent Antibody TechniqueHEK293 CellsHumansImmunoprecipitationLiver-Specific Organic Anion Transporter 1MutationOrganic Anion Transporters, Sodium-DependentOrganic Anion Transporters, Sodium-IndependentProtein DomainsProtein MultimerizationSolute Carrier Organic Anion Transporter Family Member 1B3SymportersTransfectionLiver-Specific Organic Anion Transporter 1Organic Anion Transporters, Sodium-DependentOrganic Anion Transporters, Sodium-IndependentSLCO1B1 protein, humanSLCO1B3 protein, humansodium-bile acid cotransporterSolute Carrier Organic Anion Transporter Family Member 1B3Symporters

Identifiers

PMID28644885
PMCPMC5482489
OpenAlexW2710342185

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.