Evidence map›Paper›PMID 26740304›Full record

ArticleBiochemical pharmacology2016

Serum- and glucocorticoid-inducible kinase SGK2 regulates human organic anion transporters 4 via ubiquitin ligase Nedd4-2.

Haoxun Wang, Da Xu, May Fern Toh, Alan C Pao, Guofeng You

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

Article in Biochemical pharmacology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Protein Kinase SGK2 Is Induced by the βFrontiers in physiology · 2021
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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

5 authors at 2 institutions in 1 country.

Haoxun WangDepartment of Pharmaceutics, Rutgers, the State University of New Jersey, Piscataway, NJ 08854, USA.
Da XuDepartment 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.
Alan C PaoDepartment of Medicine, Stanford University, Palo Alto, CA 94304, USA.
Guofeng YouDepartment of Pharmaceutics, Rutgers, the State University of New Jersey, Piscataway, NJ 08854, USA. Electronic address: gyou@rci.rutgers.edu.
Rutgers, The State University of New Jersey · USStanford University · 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
Role of SGK2 in Sodium Transport in the KidneyF32DK065361 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI PAO, ALAN C · 2003 to 2005
$107k
NIDDK NIH HHS F32 DK065361NIGMS NIH HHS R01 GM079123NIGMS NIH HHS R01-GM079123NIGMS NIH HHS R01 GM097000
6 · The paper itself

Abstract

Human organic anion transporter 4 (hOAT4) 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. hOAT4 is abundantly expressed in the kidney and placenta. In the current study, we examined the regulation of hOAT4 by serum- and glucocorticoid-inducible kinase 2 (sgk2) in the kidney COS-7 cells. We showed that sgk2 stimulated hOAT4 transport activity. Such stimulation mainly resulted from an increased cell surface expression of the transporter, kinetically revealed as an increased maximal transport velocity Vmax without significant change in substrate-binding affinity Km. We further showed that regulation of hOAT4 activity by sgk2 was mediated by ubiquitin ligase Nedd4-2. Overexpression of Nedd4-2 enhanced hOAT4 ubiquitination, and inhibited hOAT4 transport activity, whereas overexpression of ubiquitin ligase-dead mutant Nedd4-2/C821A or siRNA knockdown of endogenous Nedd4-2 had opposite effects on hOAT4. Our co-immunoprecipitation experiment revealed that sgk2 weakened the association between hOAT4 and Nedd4-2. In conclusion, our study demonstrated for the first time that sgk2 stimulated hOAT4 transport activity by abrogating the inhibitory effect of Nedd4-2 on the transporter.

Indexed as

AnimalsChlorocebus aethiopsCOS CellsEndosomal Sorting Complexes Required for TransportHumansImmediate-Early ProteinsNedd4 Ubiquitin Protein LigasesOrganic Anion Transporters, Sodium-IndependentProtein Serine-Threonine KinasesProtein TransportSerum-Glucocorticoid Regulated KinasesUbiquitin-Protein LigasesEndosomal Sorting Complexes Required for TransportImmediate-Early ProteinsNedd4L protein, humanNedd4 protein, humanNedd4 Ubiquitin Protein LigasesOrganic Anion Transporters, Sodium-IndependentProtein Serine-Threonine KinasesSerum-Glucocorticoid Regulated KinasesSLC22A11 protein, humanUbiquitin-Protein LigasesDrug transportOrganic anion transporterRegulationSerum and glucocorticoid-inducible kinaseUbiquitinationUbiquitin ligase

Identifiers

PMID26740304
PMCPMC5166719
OpenAlexW2197127921

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.