Evidence map›Paper›PMID 21149637›Full record

ArticleMolecular pharmacology2011

The large isoforms of A-kinase anchoring protein 18 mediate the phosphorylation of inhibitor-1 by protein kinase A and the inhibition of protein phosphatase 1 activity.

Arpita Singh, John M Redden, Michael S Kapiloff, Kimberly L Dodge-Kafka

Open access · bronzeAbstract read
In one paragraph

Article in Molecular pharmacology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

27 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Review
  3. Differential Downregulation of βJournal of the American Heart Association · 2024
    Article
  4. Role of Dopamine in the Heart in Health and Disease.International journal of molecular sciences · 2023
    Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Functions and therapeutic potential of protein phosphatase 1: Insights from mouse genetics.Biochimica et biophysica acta. Molecular cell research · 2019
    Review
  13. Review
  14. Calcineurin signaling in the heart: The importance of time and place.Journal of molecular and cellular cardiology · 2017
    Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Analysis of AKAP7γ Dimerization.Journal of signal transduction · 2015
    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

4 authors at 1 institution in 1 country.

Arpita SinghPat and Jim Calhoun Center for Cardiology, University of Connecticut Health Center, Farmington, CT 06032, USA.
John M Redden
Michael S Kapiloff
Kimberly L Dodge-Kafka
UConn Health · US

Funding

Role of the mAKAP Complex in Cardiac HypertrophyR01HL075398 · NHLBI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI KAPILOFF, MICHAEL SETH · 2004 to 2014
$3.6M
mAKAP-orchestrated phosphorylation events: regulation of PDE4D3R01HL082705 · NHLBI · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI DODGE-KAFKA, KIMBERLY L · 2006 to 2010
$1.8M
NHLBI NIH HHS R01 HL075398NHLBI NIH HHS R01-HL075398NHLBI NIH HHS R01 HL082705NHLBI NIH HHS R01-HL82705
6 · The paper itself

Abstract

Inhibitor-1 (I-1) is phosphorylated on threonine residue 35 (Thr35) by the cAMP-dependent protein kinase (PKA), inducing the potent inhibition of the serine-threonine-specific protein phosphatase 1 (PP1). We now report that the formation of a signaling complex containing PKA and I-1 by the A-kinase anchoring protein 18 (AKAP18) facilitates this regulation in cells. AKAP18 directly bound I-1, and AKAP18/I-1 complexes were isolated from both rat heart extract and transfected heterologous cells. It is noteworthy that prevention of PKA binding to the AKAP18 scaffold decreased I-1 phosphorylation by 48% in cells. Moreover, the I-1 target PP1 was also associated with AKAP18 complexes. The cAMP-mediated inhibition of phosphatase activity was contingent on PKA binding to the scaffold. These observations reveal an additional level of complexity in PP1 regulation because of its association with AKAP18 multimolecular signaling complexes and suggest that targeting of AKAP18 complexes may be an alternative method to alter phosphatase activity and modulate specific substrate dephosphorylation.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCarrier ProteinsCyclic AMPCyclic AMP-Dependent Protein KinasesHEK293 CellsHumansImmunoprecipitationMyocardiumPhosphorylationProtein IsoformsProtein Phosphatase 1ProteinsRatsSignal TransductionAdaptor Proteins, Signal TransducingAkap7 protein, ratCarrier ProteinsCyclic AMPCyclic AMP-Dependent Protein Kinasesphosphoprotein phosphatase inhibitor 1Protein IsoformsProtein Phosphatase 1Proteins

Identifiers

PMID21149637
PMCPMC3061358
OpenAlexW2108352328

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.