Evidence map›Paper›PMID 21610080›Full record

ArticleThe Journal of biological chemistry2011

Characterization of a central Ca2+/calmodulin-dependent protein kinase IIalpha/beta binding domain in densin that selectively modulates glutamate receptor subunit phosphorylation.

Yuxia Jiao, Nidhi Jalan-Sakrikar, A J Robison, Anthony J Baucum, Martha A Bass, Roger J Colbran

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

36 citing papers in PubMed, 45 citations in OpenAlex.

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  15. 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
  16. Review
  17. Activated CaMKIIMolecular pharmacology · 2018
    Article
  18. Review
  19. Article
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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

6 authors at 2 institutions in 1 country.

Yuxia JiaoDepartment of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA.
Nidhi Jalan-Sakrikar
A J Robison
Anthony J Baucum
Martha A Bass
Roger J Colbran
Vanderbilt University · USJohn F. Kennedy Center for the Performing Arts · US

Funding

Program in NeurogenomicsT32MH065215 · NIMH · VANDERBILT UNIVERSITY · PI ROGER J COLBRAN · 2002 to 2026
$6.4M
Mechanisms of CaM Kinase II Signal TransductionR01MH063232 · NIMH · VANDERBILT UNIVERSITY · PI COLBRAN, ROGER J · 2001 to 2015
$5.4M
CaMKII Anchoring in Synaptic PlasticityF31MH068129 · NIMH · VANDERBILT UNIVERSITY · PI ROBISON, ALFRED J · 2003 to 2004
$51k
NIMH NIH HHS F31 MH068129NIMH NIH HHS F32-MH068129NIMH NIH HHS R01 MH063232NIMH NIH HHS R01-MH063232NIMH NIH HHS T32 MH065215NIMH NIH HHS T32-MH065215
6 · The paper itself

Abstract

The densin C-terminal domain can target Ca(2+)/calmodulin-dependent protein kinase IIα (CaMKIIα) in cells. Although the C-terminal domain selectively binds CaMKIIα in vitro, full-length densin associates with CaMKIIα or CaMKIIβ in brain extracts and in transfected HEK293 cells. This interaction requires a second central CaMKII binding site, the densin-IN domain, and an "open" activated CaMKII conformation caused by Ca(2+)/calmodulin binding, autophosphorylation at Thr-286/287, or mutation of Thr-286/287 to Asp. Mutations in the densin-IN domain (L815E) or in the CaMKIIα/β catalytic domain (I205/206K) disrupt the interaction. The amino acid sequence of the densin-IN domain is similar to the CaMKII inhibitor protein, CaMKIIN, and a CaMKIIN peptide competitively blocks CaMKII binding to densin. CaMKII is inhibited by both CaMKIIN and the densin-IN domain, but the inhibition by densin is substrate-selective. Phosphorylation of a model peptide substrate, syntide-2, or of Ser-831 in AMPA receptor GluA1 subunits is fully inhibited by densin. However, CaMKII phosphorylation of Ser-1303 in NMDA receptor GluN2B subunits is not effectively inhibited by densin in vitro or in intact cells. Thus, densin can target multiple CaMKII isoforms to differentially modulate phosphorylation of physiologically relevant downstream targets.

Indexed as

AnimalsCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2CalmodulinHumansIsoenzymesMiceMutationPhosphorylationProtein Structure, TertiaryRatsReceptors, AMPAReceptors, N-Methyl-D-AspartateSialoglycoproteinsSwineXenopus laevisCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2CalmodulinIsoenzymesLRRC7 protein, humanLrrc7 protein, mouseLrrc7 protein, ratNR2B NMDA receptorReceptors, AMPAReceptors, N-Methyl-D-AspartateSialoglycoproteinsXenopus Proteins

Identifiers

PMID21610080
PMCPMC3137056
OpenAlexW2080867613

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.