Evidence map›Paper›PMID 27335683›Full record

ArticleInternational journal of biochemistry and molecular biology2016

Serum- and glucocorticoid-inducible kinase sgk2 stimulates the transport activity of human organic anion transporters 1 by enhancing the stability of the transporter.

Da Xu, Haozhe Huang, May Fern Toh, Guofeng You

Open access · greenAbstract read
In one paragraph

Article in International journal of biochemistry and molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Protein Kinase SGK2 Is Induced by the βFrontiers in physiology · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Review
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

4 authors at 1 institution in 1 country.

Da XuDepartment of Pharmaceutics, Rutgers, The State University of New Jersey Piscataway, NJ 08854, USA.
Haozhe HuangDepartment of Pharmaceutics, Rutgers, The State University of New Jersey Piscataway, NJ 08854, USA.
May Fern TohDepartment of Pharmaceutics, Rutgers, The State University of New Jersey Piscataway, NJ 08854, USA.
Guofeng YouDepartment of Pharmaceutics, Rutgers, The State University of New Jersey Piscataway, NJ 08854, USA.
Rutgers, The State University of New Jersey · US

Funding

Sumoylation: A Novel Mechanism for Regulating Drug/Xenobiotic Transporters OATsR01GM097000 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI YOU, GUOFENG · 2012 to 2020
$2.4M
Trafficking and Regulation of Drug/Xenobiotic Transporter OATR01GM079123 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI YOU, GUOFENG · 2008 to 2017
$2.2M
NIGMS NIH HHS R01 GM079123NIGMS NIH HHS R01 GM097000
6 · The paper itself

Abstract

Human organic anion transporter 1 (hOAT1) belongs to a family of organic anion transporters that play critical roles in the body disposition of clinically important drugs, including anti-viral therapeutics, anti-cancer drugs, antibiotics, antihypertensives, and anti-inflammatories. hOAT1 is abundantly expressed in the kidney and brain. In the current study, we examined the regulation of hOAT1 by serum- and glucocorticoid-inducible kinase 2 (sgk2) in the kidney COS-7 cells. We showed that sgk2 stimulated hOAT1 transport activity. Such stimulation mainly resulted from an increased cell surface expression of the transporter, kinetically revealed as an increased maximal transport velocity V max without significant change in substrate-binding affinity K m. We further showed that stimulation of hOAT1 activity by sgk2 was achieved by preventing hOAT1 degradation. Our co-immunoprecipitation experiment revealed that the effect of sgk2 on hOAT1 was through a direct interaction between these two proteins. In conclusion, our study demonstrated that sgk2 stimulates hOAT1 transport activity by enhancing the stability of the transporter. This study provides the insights into sgk2 regulation of hOAT1-mediated transport in normal physiology and disease.

Indexed as

drug transportOrganic anion transporterregulationserum and glucocorticoid-inducible kinase

Identifiers

PMID27335683
PMCPMC4913228
OpenAlexW2473393537

What OpenQuestion holds

Textmetadata
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.