Evidence map›Paper›PMID 20632170›Full record

ReviewUrological research2010

Role of NHERF and scaffolding proteins in proximal tubule transport.

Rochelle Cunningham, Rajatsubhra Biswas, Deborah Steplock, Shirish Shenolikar, Edward Weinman

Abstract readReview
PubMed Publisher
In one paragraph

Review in Urological research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.4field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Loss of the NaThe American journal of pathology · 2019
    Article
  8. Review
  9. Review
  10. Article
  11. Dynamic NHERF interaction with TRPC4/5 proteins is required for channel gating by diacylglycerol.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. PTH and Vitamin D.Comprehensive Physiology · 2016
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Genetic disorders of phosphate regulation.Pediatric nephrology (Berlin, Germany) · 2012
    Review
  19. MAP17, a ROS-dependent oncogene.Frontiers in oncology · 2012
    Article
  20. 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

5 authors at 2 institutions in 1 country.

Rochelle CunninghamDivision of Nephrology, Department of Medicine, University of Maryland, School of Medicine, Room N3W143, UHM, 22 South Greene Street, Baltimore, MD 21201, USA. rcunning@medicine.umaryland.edu
Rajatsubhra Biswas
Deborah Steplock
Shirish Shenolikar
Edward Weinman
University of Maryland, Baltimore · USDuke Medical Center · US

Funding

SODIUM-H+ TRANSPORT IN RENAL APICAL MEMBRANESR01DK055881 · NIDDK · WEST VIRGINIA UNIVERSITY · PI WEINMAN, EDWARD J · 1999 to 2012
$4.6M
NHERF-1 and dopamine-mediated regulation of renal phosphate transport.I01BX000103 · VA · BALTIMORE VA MEDICAL CENTER · PI WEINMAN, EDWARD J · 2009 to 2013
–
BLRD VA I01 BX000103NIDDK NIH HHS DK55881NIDDK NIH HHS R01 DK055881
6 · The paper itself

Abstract

Eukaryotic cells coordinate specific responses to hormones and growth factors by spatial and temporal organization of "signaling components." Through the formation of multiprotein complexes, cells are able to generate "signaling components" that transduce hormone signals through proteins, such as PSD-95/Dlg/ZO-1(PDZ)-containing proteins that associate by stable and dynamic interactions. The PDZ homology domain is a common protein interaction domain in eukaryotes and with greater than 500 PDZ domains identified, it is the most abundant protein interaction domain in eukaryotic cells. The NHERF (sodium hydrogen exchanger regulatory factor) proteins are PDZ domain-containing proteins that play an important role in maintaining and regulating cell function. NHERF-1 was initially identified as a brush border membrane-associated phosphoprotein essential for the cAMP/PKA-induced inhibition of the sodium hydrogen exchanger isoform 3 (NHE3). Mouse, rabbit and human renal proximal tubules also express NHERF-2 (E3KARP), a structurally related protein, which in model cell systems also binds NHE3 and mediates its inhibition by cAMP. PDZK1 (NHERF-3) and IKEPP (NHERF-4) were later identified and found to have similar homology domains, leading to their recent reclassification. Although studies have revealed similar binding partners and overlapping functions for the NHERF proteins, it is clear that there is a significant amount of specificity between them. This review focuses primarily on NHERF-1, as the prototypical PDZ protein and will give a brief summary of its role in phosphate transport and the development of some forms of nephrolithiasis.

Indexed as

AnimalsHumansKidney Tubules, ProximalMiceMicroscopy, ConfocalPDZ DomainsPhosphatesPhosphoproteinsProtein BindingRabbitsSignal TransductionSodium-Hydrogen ExchangersPhosphatesPhosphoproteinssodium-hydrogen exchanger regulatory factorSodium-Hydrogen Exchangers

Identifiers

PMID20632170
OpenAlexW1992454880

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.