Evidence map›Paper›PMID 19608738›Full record

ArticleThe Journal of biological chemistry2009

Protein kinase A increases type-2 inositol 1,4,5-trisphosphate receptor activity by phosphorylation of serine 937.

Matthew J Betzenhauser, Jenna L Fike, Larry E Wagner, David I Yule

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

41 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Structural titration reveals CaNature communications · 2023
    Article
  4. Neuronal microRNAs safeguard ER CaCellular and molecular life sciences : CMLS · 2022
    Article
  5. Review
  6. Article
  7. Article
  8. IPAmerican journal of physiology. Heart and circulatory physiology · 2021
    Article
  9. Article
  10. CaCold Spring Harbor perspectives in biology · 2020
    Review
  11. Review
  12. Research progress on the role of CaMKII in heart disease.American journal of translational research · 2020
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. βThe Journal of biological chemistry · 2017
    Article
  18. Article
  19. Article
  20. Regulation of IPCell calcium · 2017
    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

4 authors at 1 institution in 1 country.

Matthew J BetzenhauserDepartment of Pharmacology and Physiology, School of Medicine and Dentistry, University of Rochester Medical Center, Rochester, New York 14642, USA.
Jenna L Fike
Larry E Wagner
David I Yule
University of Rochester Medical Center · US

Funding

TRAINING PROGRAM IN ORAL SCIENCET32DE007202 · NIDCR · UNIVERSITY OF ROCHESTER · PI QUIVEY, ROBERT G · 1990 to 2010
$5.5M
PANCREATIC SECRETION--G PROTEIN MEDIATED CA++ SIGNALINGR01DK054568 · NIDDK · UNIVERSITY OF ROCHESTER · PI YULE, DAVID I · 1998 to 2012
$3.1M
Signaling Pathways in Salivary Gland Fluid SecretionR01DE016999 · NIDCR · UNIVERSITY OF ROCHESTER · PI SHUTTLEWORTH, TREVOR J. · 2005 to 2009
$1.8M
NIDCR NIH HHS R01 DE016999NIDCR NIH HHS R01-DE016999NIDCR NIH HHS T32-DE07202NIDDK NIH HHS R01 DK054568NIDDK NIH HHS R01-DK054568
6 · The paper itself

Abstract

Protein kinase A (PKA) phosphorylation of inositol 1,4,5-trisphosphate receptors (InsP(3)Rs) represents a mechanism for shaping intracellular Ca(2+) signals following a concomitant elevation in cAMP. Activation of PKA results in enhanced Ca(2+) release in cells that express predominantly InsP(3)R2. PKA is known to phosphorylate InsP(3)R2, but the molecular determinants of this effect are not known. We have expressed mouse InsP(3)R2 in DT40-3KO cells that are devoid of endogenous InsP(3)R and examined the effects of PKA phosphorylation on this isoform in unambiguous isolation. Activation of PKA increased Ca(2+) signals and augmented the single channel open probability of InsP(3)R2. A PKA phosphorylation site unique to the InsP(3)R2 was identified at Ser(937). The enhancing effects of PKA activation on this isoform required the phosphorylation of Ser(937), since replacing this residue with alanine eliminated the positive effects of PKA activation. These results provide a mechanism responsible for the enhanced Ca(2+) signaling following PKA activation in cells that express predominantly InsP(3)R2.

Indexed as

Amino Acid SequenceAnimalsCalciumChickensChlorocebus aethiopsCOS CellsCyclic AMP-Dependent Protein KinasesInositol 1,4,5-Trisphosphate ReceptorsMiceModels, BiologicalMolecular Sequence DataPhosphorylationProtein IsoformsSerineSignal TransductionCalciumCyclic AMP-Dependent Protein KinasesInositol 1,4,5-Trisphosphate ReceptorsProtein IsoformsSerine

Identifiers

PMID19608738
PMCPMC2757215
OpenAlexW2078941920

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.