Evidence map›Paper›PMID 18046316›Full record

ArticleKidney international2008

Interactions of the growth-related, type IIc renal sodium/phosphate cotransporter with PDZ proteins.

R Villa-Bellosta, M Barac-Nieto, S Y Breusegem, N P Barry, M Levi, V Sorribas

Open access · bronzeAbstract read
In one paragraph

Article in Kidney international, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Renal cell markers: lighthouses for managing renal diseases.American journal of physiology. Renal physiology · 2021
    Article
  7. Mechanisms of phosphate transport.Nature reviews. Nephrology · 2019
    Review
  8. Visualizing the regulation of SLC34 proteins at the apical membrane.Pflugers Archiv : European journal of physiology · 2019
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. NHERF-1 and the regulation of renal phosphate reabsoption: a tale of three hormones.American journal of physiology. Renal physiology · 2012
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

6 authors at 3 institutions in 3 countries.

R Villa-BellostaLaboratory of Molecular Toxicology, Department of Toxicology, University of Zaragoza, Zaragoza, Spain.
M Barac-Nieto
S Y Breusegem
N P Barry
M Levi
V Sorribas
Universidad de Zaragoza · ESUniversity of Colorado Anschutz Medical Campus · USUniversity of Colorado Health · US

Funding

Regulation of Renal Phosphate Transport by LipidsR01DK066029 · NIDDK · UNIVERSITY OF COLORADO DENVER · PI LEVI, MOSHE · 2005 to 2013
$3.2M
NIDDK NIH HHS R01 DK066029NIDDK NIH HHS R01 DK066029-01
6 · The paper itself

Abstract

Despite similar molecular structures, the growth-related sodium/phosphate cotransporter NaPiIIc is regulated differently than the main NaPiIIa phosphate transporter. Using two-hybrid systems and immunoprecipitation, we identified several proteins that interact with NaPiIIc that might account for this differential regulation. NaPiIIc interacted with the PDZ domain-containing sodium-hydrogen exchange-regulating factor (NHERF) 1 and NHERF3 through novel binding motifs in its C terminus. NaPiIIc from brush-border membranes coprecipitated with both NHERF1 and NHERF3, with more NHERF3 co-precipitated in rats fed a low-phosphorus diet. NaPiIIc colocalizes with both NHERF1 and NHERF3 in brush-border membranes of rats fed either a low- or high-phosphorus diet. When mouse NaPiIIc was transfected into opossum kidney cells, it was localized mainly in apical microvilli and the trans-Golgi. Both confocal and total internal reflection microscopy show that NaPiIIc colocalizes with NHERF1 and NHERF3 in the apical microvilli, and this was not altered by truncation of the last three amino acids of NaPiIIc. Interactions of NaPiIIc with NHERF1 and NHERF3 were modulated by the membrane-associated 17 kDa protein (MAP17) similarly to NaPiIIa, but only the MAP17-NaPiIIc-NHERF3 complexes were internalized to the trans-Golgi. Our study shows that NaPiIIc interacts with a limited number of PDZ domain proteins, and the mechanisms and consequences of such interactions differ from those of NaPiIIa.

Indexed as

PDZ DomainsAnimalsDietGene LibraryImmunoprecipitationKidney CortexMembrane ProteinsMicePhosphoproteinsPhosphorusProtein Interaction MappingRatsSodium-Hydrogen ExchangersSodium-Phosphate Cotransporter Proteins, Type IIaSodium-Phosphate Cotransporter Proteins, Type IIcTransfectionMembrane ProteinsPDZK1IP1 protein, humanPhosphoproteinsPhosphorussodium-hydrogen exchanger regulatory factorSodium-Hydrogen ExchangersSodium-Phosphate Cotransporter Proteins, Type IIaSodium-Phosphate Cotransporter Proteins, Type IIc

Identifiers

PMID18046316
PMCPMC2738937
OpenAlexW2059946041

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.