Evidence map›Paper›PMID 7667292›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

The G-protein-coupled receptor phosphatase: a protein phosphatase type 2A with a distinct subcellular distribution and substrate specificity.

J A Pitcher, E S Payne, C Csortos, A A DePaoli-Roach, R J Lefkowitz

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.8field-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

45 citing papers in PubMed, 176 citations in OpenAlex.

  1. Article
  2. Renal ATCirculation research · 2022
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Regulation of GPCR Trafficking by Ubiquitin.Progress in molecular biology and translational science · 2015
    Review
  9. Article
  10. Review
  11. Article
  12. Roles of proteolysis in regulation of GPCR function.British journal of pharmacology · 2013
    Review
  13. Article
  14. Article
  15. Review
  16. Protein phosphatase 2A mediates resensitization of the neurokinin 1 receptor.American journal of physiology. Cell physiology · 2011
    Article
  17. Article
  18. Article
  19. Review
  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

5 authors at 1 institution in 1 country.

J A PitcherHoward Hughes Medical Research Institute, Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA.
E S Payne
C Csortos
A A DePaoli-Roach
R J Lefkowitz
Indiana University – Purdue University Indianapolis · US

Funding

Molecular Regulation of Cardiovascular 7 TM ReceptorsR01HL016037 · NHLBI · DUKE UNIVERSITY · PI ROBERT J LEFKOWITZ · 1985 to 2026
$14.5M
STRUCTURE &REGULATION OF TYPE 1 PROTEIN PHOSPHATASESR01DK036569 · NIDDK · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI DEPAOLI-ROACH, ANNA A · 1986 to 2004
$1.3M
THE CALPAIN-CALPASTATIN SYSTEM IN CARDIOVASCULAR TISSUES--ROLE IN CELL CYCLEP01HL006308 · NHLBI · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI DE PAOLI- ROACH, ANNA A · 1985 to 1997
–
MOLECULAR PROPERTIES OF CARDIAC ADRENERGIC RECEPTORSR37HL016037 · NHLBI · DUKE UNIVERSITY · PI LEFKOWITZ, ROBERT J · 1986 to 1995
–
NHLBI NIH HHS HL16037NHLBI NIH HHS P01 HL06308NIDDK NIH HHS DK36569
6 · The paper itself

Abstract

Phosphorylation of G-protein-coupled receptors plays an important role in regulating their function. In this study the G-protein-coupled receptor phosphatase (GRP) capable of dephosphorylating G-protein-coupled receptor kinase-phosphorylated receptors is described. The GRP activity of bovine brain is a latent oligomeric form of protein phosphatase type 2A (PP-2A) exclusively associated with the particulate fraction. GRP activity is observed only when assayed in the presence of protamine or when phosphatase-containing fractions are subjected to freeze/thaw treatment under reducing conditions. Consistent with its identification as a member of the PP-2A family, the GRP is potently inhibited by okadaic acid but not by I-2, the specific inhibitor of protein phosphatase type 1. Solubilization of the membrane-associated GRP followed by gel filtration in the absence of detergent yields a 150-kDa peak of latent receptor phosphatase activity. Western blot analysis of this phosphatase reveals a likely subunit composition of AB alpha C. PP-2A of this subunit composition has previously been characterized as a soluble enzyme, yet negligible soluble GRP activity was observed. The subcellular distribution and substrate specificity of the GRP suggests significant differences between it and previously characterized forms of PP-2A.

Indexed as

AnimalsBlotting, WesternBrainCattleCell MembraneChromatography, GelGTP-Binding ProteinsHumansPhosphoprotein PhosphatasesReceptor Protein-Tyrosine KinasesReceptors, Cell SurfaceSpodopteraSubcellular FractionsSubstrate SpecificityGTP-Binding ProteinsPhosphoprotein PhosphatasesReceptor Protein-Tyrosine KinasesReceptors, Cell Surface

Identifiers

PMID7667292
PMCPMC41153
OpenAlexW2064264293

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.