Evidence map›Paper›PMID 21873413›Full record

ReviewPharmacological reviews2011

Regulation of G protein-coupled receptor function by Na+/H+ exchange regulatory factors.

Juan A Ardura, Peter A Friedman

Open access · bronzeAbstract readReview
In one paragraph

Review in Pharmacological reviews, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

62 citing papers in PubMed, 99 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. The Intricacies of Renal Phosphate Reabsorption-An Overview.International journal of molecular sciences · 2024
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. NaJournal of immunology (Baltimore, Md. : 1950) · 2021
    Article
  12. Review
  13. Article
  14. A Critical Role for NaJournal of immunology (Baltimore, Md. : 1950) · 2021
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Specificity of NHERF1 regulation of GPCR signaling and function in human airway smooth muscle.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  20. Article

2 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Juan A ArduraDepartment of Pharmacology & Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
Peter A Friedman
University of Pittsburgh · US

Funding

PTH Receptor: Posttranslational Modification and Recycling in BoneR01DK054171 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI FRIEDMAN, PETER A · 1998 to 2015
$6.0M
EBP50 REGULATION OF PTH RECEPTOR IN BONE AND KIDNEYR01DK069998 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI FRIEDMAN, PETER A · 2006 to 2014
$2.9M
NIDDK NIH HHS DK054171NIDDK NIH HHS DK069998NIDDK NIH HHS R01 DK054171NIDDK NIH HHS R01 DK069998
6 · The paper itself

Abstract

Many G protein-coupled receptors (GPCR) exert patterns of cell-specific signaling and function. Mounting evidence now supports the view that cytoplasmic adapter proteins contribute critically to this behavior. Adapter proteins recognize highly conserved motifs such as those for Src homology 3 (SH3), phosphotyrosine-binding (PTB), and postsynaptic density 95/discs-large/zona occludens (PDZ) docking sequences in candidate GPCRs. Here we review the behavior of the Na+/H+ exchange regulatory factor (NHERF) family of PDZ adapter proteins on GPCR signalling, trafficking, and function. Structural determinants of NHERF proteins that allow them to recognize targeted GPCRs are considered. NHERF1 and NHERF2 are capable also of modifying the assembled complex of accessory proteins such as β-arrestins, which have been implicated in regulating GPCR signaling. In addition, NHERF1 and NHERF2 modulate GPCR signaling by altering the G protein to which the receptor binds or affect other regulatory proteins that affect GTPase activity, protein kinase A, phospholipase C, or modify downstream signaling events. Small molecules targeting the site of NHERF1-GPCR interaction are being developed and may become important and selective drug candidates.

Indexed as

Guanine Nucleotide Exchange FactorsHumansMolecular StructureReceptors, G-Protein-CoupledSignal TransductionSodium-Hydrogen ExchangersGuanine Nucleotide Exchange FactorsReceptors, G-Protein-CoupledSodium-Hydrogen Exchangers

Identifiers

PMID21873413
PMCPMC3186079
OpenAlexW2163537415

What Socratic 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 Socratic graph.