Evidence map›Paper›PMID 18205403›Full record

ArticleBiochemistry2008

Differential regulated interactions of calcium/calmodulin-dependent protein kinase II with isoforms of voltage-gated calcium channel beta subunits.

Chad E Grueter, Sunday A Abiria, Yunji Wu, Mark E Anderson, Roger J Colbran

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 10% 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

38 citing papers in PubMed, 1 synthesis or guideline pooled it, 63 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Protein Kinases: Potential Drug Targets AgainstFrontiers in cellular and infection microbiology · 2021
    Review
  9. Neuronal L-Type Calcium Channel Signaling to the Nucleus Requires a Novel CaMKIIα-Shank3 Interaction.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  10. Article
  11. Article
  12. CaHeart rhythm · 2018
    Review
  13. A novel mechanism for CaThe Journal of biological chemistry · 2017
    Article
  14. Article
  15. Article
  16. Article
  17. LRRK2 Regulates Voltage-Gated Calcium Channel Function.Frontiers in molecular neuroscience · 2016
    Article
  18. Review
  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 2 institutions in 1 country.

Chad E GrueterDepartment of Molecular Physiology and Biophysics, Vanderbilt University Medical Center, Nashville, Tennessee 37232, USA.
Sunday A Abiria
Yunji Wu
Mark E Anderson
Roger J Colbran
Vanderbilt University Medical Center · USJohn F. Kennedy Center for the Performing Arts · US

Funding

Transcriptional remodeling in cardiac arrhythmiasP01HL046681 · NHLBI · VANDERBILT UNIVERSITY · PI GEORGE, ALFRED L. · 1992 to 2006
$8.1M
Training In Cardiovascular ResearchT32HL007411 · NHLBI · VANDERBILT UNIVERSITY · PI BECKMAN, JOSHUA A · 1985 to 2020
$7.2M
Mechanisms of CaM Kinase II Signal TransductionR01MH063232 · NIMH · VANDERBILT UNIVERSITY · PI COLBRAN, ROGER J · 2001 to 2015
$5.4M
Mitochondrial Calmodulin Kinase II in Physiology and DiseaseR01HL070250 · NHLBI · VANDERBILT UNIVERSITY · PI ANDERSON, MARK E · 2002 to 2017
$5.2M
CALMODULIN KINASE II AND EARLY AFTERDEPOLARIZATIONSR01HL062494 · NHLBI · VANDERBILT UNIVERSITY · PI ANDERSON, MARK E · 1999 to 2007
$1.8M
NHLBI NIH HHS HL062494NHLBI NIH HHS HL07411NHLBI NIH HHS HL46681NHLBI NIH HHS HL70250NHLBI NIH HHS P01 HL046681NHLBI NIH HHS R01 HL062494NHLBI NIH HHS R01 HL070250NHLBI NIH HHS T32 HL007411NIMH NIH HHS MH63232NIMH NIH HHS R01 MH063232
6 · The paper itself

Abstract

Ca2+/calmodulin-dependent protein kinase II (CaMKII) phosphorylates the beta2a subunit of voltage-gated Ca2+ channels at Thr498 to facilitate cardiac L-type Ca2+ channels. CaMKII colocalizes with beta2a in cardiomyocytes and also binds to a domain in beta2a that contains Thr498 and exhibits an amino acid sequence similarity to the CaMKII autoinhibitory domain and to a CaMKII binding domain in the NMDA receptor NR2B subunit (Grueter, C. E. et al. (2006) Mol. Cell 23, 641). Here, we explore the selectivity of the actions of CaMKII among Ca2+ channel beta subunit isoforms. CaMKII phosphorylates the beta1b, beta2a, beta3, and beta4 isoforms with similar initial rates and final stoichiometries of 6-12 mol of phosphate per mol of protein. However, activated/autophosphorylated CaMKII binds to beta1b and beta2a with a similar apparent affinity but does not bind to beta3 or beta4. Prephosphorylation of beta1b and beta2a by CaMKII substantially reduces the binding of autophosphorylated CaMKII. Residues surrounding Thr498 in beta2a are highly conserved in beta1b but are different in beta3 and beta4. Site-directed mutagenesis of this domain in beta2a showed that Thr498 phosphorylation promotes dissociation of CaMKII-beta2a complexes in vitro and reduces interactions of CaMKII with beta2a in cells. Mutagenesis of Leu493 to Ala substantially reduces CaMKII binding in vitro and in intact cells but does not interfere with beta2a phosphorylation at Thr498. In combination, these data show that phosphorylation dynamically regulates the interactions of specific isoforms of the Ca2+ channel beta subunits with CaMKII.

Indexed as

Ion Channel GatingAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium ChannelsIsoenzymesPhosphorylationPlasmidsProtein BindingRatsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium ChannelsIsoenzymes

Identifiers

PMID18205403
PMCPMC2814322
OpenAlexW2066654787

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.