Evidence map›Paper›PMID 32316189›Full record

ArticleCells2020

The Lipid Raft Component Stomatin Interacts with the Na

Monique D Appelman, Marion J D Robin, Esther W M Vogels, Christie Wolzak, Winnie G Vos, Harmjan R Vos, Robert M Van Es, Boudewijn M T Burgering, Stan F J Van de Graaf

Open access · goldAbstract read
In one paragraph

Article in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
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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 1 institution in 1 country.

Monique D AppelmanAmsterdam UMC, University of Amsterdam, Tytgat Institute for Liver and Intestinal Research, Amsterdam Gastroenterology, Endocrinology and Metabolism, 1105 BK Amsterdam, The Netherlands.
Marion J D RobinAmsterdam UMC, University of Amsterdam, Tytgat Institute for Liver and Intestinal Research, Amsterdam Gastroenterology, Endocrinology and Metabolism, 1105 BK Amsterdam, The Netherlands.
Esther W M VogelsAmsterdam UMC, University of Amsterdam, Tytgat Institute for Liver and Intestinal Research, Amsterdam Gastroenterology, Endocrinology and Metabolism, 1105 BK Amsterdam, The Netherlands.
Christie WolzakAmsterdam UMC, University of Amsterdam, Tytgat Institute for Liver and Intestinal Research, Amsterdam Gastroenterology, Endocrinology and Metabolism, 1105 BK Amsterdam, The Netherlands.
Winnie G VosAmsterdam UMC, University of Amsterdam, Tytgat Institute for Liver and Intestinal Research, Amsterdam Gastroenterology, Endocrinology and Metabolism, 1105 BK Amsterdam, The Netherlands.
Harmjan R VosCenter for Molecular Medicine, Molecular Cancer Research Section, University Medical Center, 3584 CX Utrecht, The Netherlands.
Robert M Van EsCenter for Molecular Medicine, Molecular Cancer Research Section, University Medical Center, 3584 CX Utrecht, The Netherlands.
Boudewijn M T BurgeringCenter for Molecular Medicine, Molecular Cancer Research Section, University Medical Center, 3584 CX Utrecht, The Netherlands.
Stan F J Van de GraafAmsterdam UMC, University of Amsterdam, Tytgat Institute for Liver and Intestinal Research, Amsterdam Gastroenterology, Endocrinology and Metabolism, 1105 BK Amsterdam, The Netherlands.ORCID 0000-0003-4238-4359
Amsterdam University Medical Centers · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The sodium taurocholate cotransporting polypeptide (NTCP) is expressed at the basolateral membrane of hepatocytes, where it mediates the uptake of conjugated bile acids and forms the hepatocyte entry receptor for the hepatitis B and D virus. Here, we aimed to identify novel protein-protein interactions that could play a role in the regulation of NTCP. To this end, NTCP was precipitated from HA-tagged hNTCP-expressing HepG2 cells, and chloride channel CLIC-like 1 (CLCC1) and stomatin were identified as interacting proteins by mass spectrometry. Interaction was confirmed by co-immunoprecipitation. NTCP, CLCC1 and stomatin were found at the plasma membrane in lipid rafts, as demonstrated by a combination of immunofluorescence, cell surface biotinylation and isolation of detergent-resistant membranes. Neither CLCC1 overexpression nor its knockdown had an effect on NTCP function. However, both stomatin overexpression and knockdown increased NTCP-mediated taurocholate uptake while NTCP abundance at the plasma membrane was only increased in stomatin depleted cells. These findings identify stomatin as an interactor of NTCP and show that the interaction modulates bile salt transport.

Indexed as

Bile Acids and SaltsBiological Transport, ActiveCell Line, TumorCell MembraneChloride ChannelsChromatography, LiquidGene Knockdown TechniquesHepatocytesHumansLiverMembrane MicrodomainsMembrane ProteinsOrganic Anion Transporters, Sodium-DependentProtein BindingSymportersTandem Mass SpectrometryBile Acids and SaltsChloride ChannelsCLCC1 protein, humanMembrane ProteinsOrganic Anion Transporters, Sodium-Dependentsodium-bile acid cotransporterSTOM protein, humanSymportersTaurocholic AcidASBTbile acidBSEPcholestasisenterohepatic circulationlipid raftOATPprotein–protein interactiontransporter

Identifiers

PMID32316189
PMCPMC7226988
OpenAlexW3017106125

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.