Evidence map›Paper›PMID 26823285›Full record

ArticleAmerican journal of physiology. Renal physiology2016

Nedd4-2 but not Nedd4-1 is critical for protein kinase C-regulated ubiquitination, expression, and transport activity of human organic anion transporter 1.

Da Xu, Haoxun Wang, Qiang Zhang, Guofeng You

Open access · bronzeAbstract read
In one paragraph

Article in American journal of physiology. Renal physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
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  5. A single injection of periostin decreases cardiac voltage-gated NaThe Journal of veterinary medical science · 2021
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  14. PKC/Nedd4-2 Signaling Pathway Regulates the Cell Surface Expression of Drug Transporter hOAT1.Drug metabolism and disposition: the biological fate of chemicals · 2017
    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

4 authors at 1 institution in 1 country.

Da XuDepartment of Pharmaceutics, Rutgers University, Piscataway, New Jersey.
Haoxun WangDepartment of Pharmaceutics, Rutgers University, Piscataway, New Jersey.
Qiang ZhangDepartment of Pharmaceutics, Rutgers University, Piscataway, New Jersey.
Guofeng YouDepartment of Pharmaceutics, Rutgers University, Piscataway, New Jersey gyou@rci.rutgers.edu.
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) expressed at the membrane of the kidney proximal tubule cells mediates the body disposition of a diverse array of clinically important drugs, including anti-HIV therapeutics, antitumor drugs, antibiotics, antihypertensives, and antiinflammatories. Therefore, understanding the regulation of hOAT1 will provide significant insights into kidney function and dysfunction. We previously established that hOAT1 transport activity is inhibited by activation of protein kinase C (PKC) through accelerating hOAT1 internalization from cell surface into intracellular endosomes and subsequent degradation. We further established that PKC-induced hOAT1 ubiquitination is an important step preceding hOAT1 internalization. In the current study, we identified two closely related E3 ubiquitin ligases, neural precursor cell expressed, developmentally downregulated 4-1 and 4-2 (Nedd4-1 and Nedd4-2), as important regulators for hOAT1: overexpression of Nedd4-1 or Nedd4-2 enhanced hOAT1 ubiquitination, reduced the hOAT1 amount at the cell surface, and suppressed hOAT1 transport activity. In further exploring the relationship among PKC, Nedd4-1, and Nedd4-2, we discovered that PKC-dependent changes in hOAT1 ubiquitination, expression, and transport activity were significantly blocked in cells transfected with the ligase-dead mutant of Nedd4-2 (Nedd4-2/C821A) or with Nedd4-2-specific siRNA to knockdown endogenous Nedd4-2 but not in cells transfected with the ligase-dead mutant of Nedd4-1 (Nedd4-1/C867S) or with Nedd4-1-specific siRNA to knockdown endogenous Nedd4-1. In conclusion, this is the first demonstration that both Nedd4-1 and Nedd4-2 are important regulators for hOAT1 ubiquitination, expression, and function. Yet they play distinct roles, as Nedd4-2 but not Nedd4-1 is a critical mediator for PKC-regulated hOAT1 ubiquitination, expression, and transport activity.

Indexed as

AnimalsBiological TransportChlorocebus aethiopsCOS CellsEndosomal Sorting Complexes Required for TransportGene Expression RegulationGene Knockdown TechniquesHEK293 CellsHumansKidney CortexMaleMutagenesis, Site-DirectedNedd4 Ubiquitin Protein LigasesOrganic Anion Transport Protein 1Protein Kinase CRatsEndosomal Sorting Complexes Required for TransportNedd4L protein, humanNEDD4L protein, ratNedd4 protein, humanNedd4 protein, ratNedd4 Ubiquitin Protein LigasesOrganic Anion Transport Protein 1Protein Kinase CRNA, Small InterferingUbiquitin-Protein Ligasesdrug transportNedd4organic anion transporterregulationubiquitinationubiquitin ligase

Identifiers

PMID26823285
PMCPMC4867312
OpenAlexW2298665954

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.