Evidence map›Paper›PMID 21880917›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2011

Kalirin binds the NR2B subunit of the NMDA receptor, altering its synaptic localization and function.

Drew D Kiraly, Fouad Lemtiri-Chlieh, Eric S Levine, Richard E Mains, Betty A Eipper

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

50 citing papers in PubMed, 78 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Drew D KiralyDepartment of Neuroscience, University of Connecticut Health Center, Farmington, Connecticut 06030, USA.
Fouad Lemtiri-Chlieh
Eric S Levine
Richard E Mains
Betty A Eipper
UConn Health · US

Funding

Dissecting the role of one neuronal RhoGEF amongst many: the Kalirin-7 null mouseR01DA023082 · NIDA · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI MAINS, RICHARD E · 2008 to 2012
$1.6M
GDP/GTP Exchange Factors: Nucleus Accumbens PlasticityR01DA015464 · NIDA · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI EIPPER, ELIZABETH ANNE · 2004 to 2008
$1.6M
Neuroscience Training at University of Connecticut Health CenterT32NS041224 · NINDS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI EIPPER, ELIZABETH ANNE · 2001 to 2010
$1.3M
MEDICAL SCIENTIST TRAINING PROGRAMT32GM008607 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI KREAM, BARBARA E · 1999 to 2006
$896k
Constructing a Conditional Kalirin Null MouseR21DA018274 · NIDA · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI MAINS, RICHARD E · 2004 to 2005
$290k
Kalirin-7 is essential in cocaine signaling: focus on nucleus accumbensF30DA026706 · NIDA · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI KIRALY, DREW · 2011 to 2013
$108k
NIDA NIH HHS DA-15464NIDA NIH HHS DA-18274NIDA NIH HHS DA-23082NIDA NIH HHS DA-26706NIDA NIH HHS F30 DA026706NIDA NIH HHS R01 DA015464NIDA NIH HHS R01 DA023082NIDA NIH HHS R21 DA018274NIGMS NIH HHS T32 GM008607NINDS NIH HHS T32 NS041224
6 · The paper itself

Abstract

The ability of dendritic spines to change size and shape rapidly is critical in modulating synaptic strength; these morphological changes are dependent upon rearrangements of the actin cytoskeleton. Kalirin-7 (Kal7), a Rho guanine nucleotide exchange factor localized to the postsynaptic density (PSD), modulates dendritic spine morphology in vitro and in vivo. Kal7 activates Rac and interacts with several PSD proteins, including PSD-95, DISC-1, AF-6, and Arf6. Mice genetically lacking Kal7 (Kal7(KO)) exhibit deficient hippocampal long-term potentiation (LTP) as well as behavioral abnormalities in models of addiction and learning. Purified PSDs from Kal7(KO) mice contain diminished levels of NR2B, an NMDA receptor subunit that plays a critical role in LTP induction. Here we demonstrate that Kal7(KO) animals have decreased levels of NR2B-dependent NMDA receptor currents in cortical pyramidal neurons as well as a specific deficit in cell surface expression of NR2B. Additionally, we demonstrate that the genotypic differences in conditioned place preference and passive avoidance learning seen in Kal7(KO) mice are abrogated when animals are treated with an NR2B-specific antagonist during conditioning. Finally, we identify a stable interaction between the pleckstrin homology domain of Kal7 and the juxtamembrane region of NR2B preceding its cytosolic C-terminal domain. Binding of NR2B to a protein that modulates the actin cytoskeleton is important, as NMDA receptors require actin integrity for synaptic localization and function. These studies demonstrate a novel and functionally important interaction between the NR2B subunit of the NMDA receptor and Kalirin, proteins known to be essential for normal synaptic plasticity.

Indexed as

Analysis of VarianceAnimalsAnimals, NewbornAvoidance LearningCerebral CortexDisks Large Homolog 4 ProteinElectric StimulationExcitatory Amino Acid AntagonistsExcitatory Postsynaptic PotentialsGreen Fluorescent ProteinsGuanine Nucleotide Exchange FactorsGuanylate KinasesImmunoprecipitationIn Vitro TechniquesLocomotionMembrane ProteinsDisks Large Homolog 4 ProteinDlg4 protein, mouseExcitatory Amino Acid AntagonistsGreen Fluorescent ProteinsGuanine Nucleotide Exchange FactorsGuanylate KinasesifenprodilKALRN protein, mouseMembrane ProteinsNR2B NMDA receptorPhenolsPiperidinesReceptors, N-Methyl-D-AspartateRo 25-6981

Identifiers

PMID21880917
PMCPMC3172699
OpenAlexW1968727599

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.