Evidence map›Paper›PMID 15901899›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

P2Y1 receptor signaling is controlled by interaction with the PDZ scaffold NHERF-2.

Sami R Fam, Maryse Paquet, Amanda M Castleberry, Heide Oller, C Justin Lee, Stephen F Traynelis, Yoland Smith, C Chris Yun, Randy A Hall

Abstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

49 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. G protein-coupled receptors: what a difference a 'partner' makes.International journal of molecular sciences · 2014
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Detection and characterization of receptor interactions with PDZ domains.Methods in molecular biology (Clifton, N.J.) · 2011
    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

9 authors at 2 institutions in 1 country.

Sami R FamDepartment of Pharmacology, Yerkes National Primate Research Center, and Division of Digestive Disease, Emory University School of Medicine, Atlanta, GA 30322, USA.
Maryse Paquet
Amanda M Castleberry
Heide Oller
C Justin Lee
Stephen F Traynelis
Yoland Smith
C Chris Yun
Randy A Hall
Emory National Primate Research CenterEmory University · US

Funding

Regulation of NHE3 by glucocorticoids, SGK1 and NHERF2R01DK061418 · NIDDK · EMORY UNIVERSITY · PI YUN, CHANGHYON CHRIS · 2003 to 2015
$4.0M
NIDDK NIH HHS R01 DK061418
6 · The paper itself

Abstract

P2Y(1) purinergic receptors (P2Y(1)Rs) mediate rises in intracellular Ca(2+) in response to ATP, but the duration and characteristics of this Ca(2+) response are known to vary markedly in distinct cell types. We screened the P2Y(1)R carboxyl terminus against a recently created proteomic array of PDZ (PSD-95/Drosophila Discs large/ZO-1 homology) domains and identified a previously unrecognized, specific interaction with the second PDZ domain of the scaffold NHERF-2 (Na(+)/H(+) exchanger regulatory factor type 2). Furthermore, we found that P2Y(1)R and NHERF-2 associate in cells, allowing NHERF-2-mediated tethering of P2Y(1)R to key downstream effectors such as phospholipase Cbeta. Finally, we found that coexpression of P2Y(1)R with NHERF-2 in glial cells prolongs P2Y(1)R-mediated Ca(2+) signaling, whereas disruption of the P2Y(1)R-NHERF-2 interaction by point mutations attenuates the duration of P2Y(1)R-mediated Ca(2+) responses. These findings reveal that NHERF-2 is a key regulator of the cellular activity of P2Y(1)R and may therefore determine cell-specific differences in P2Y(1)R-mediated signaling.

Indexed as

Blotting, WesternBrainCalciumCell LineCytoskeletal ProteinsHumansImmunohistochemistryImmunoprecipitationMicroscopy, ElectronNeurogliaPhosphoproteinsProtein Array AnalysisProtein BindingProtein Structure, TertiaryReceptors, Purinergic P2Receptors, Purinergic P2Y1CalciumCytoskeletal ProteinsP2RY1 protein, humanPhosphoproteinsReceptors, Purinergic P2Receptors, Purinergic P2Y1sodium-hydrogen exchanger regulatory factorSodium-Hydrogen Exchangers

Identifiers

PMID15901899
PMCPMC1142356
OpenAlexW2000272692

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.