Evidence map›Paper›PMID 31983435›Full record

ArticleBiochemical and biophysical research communications2020

CaMKIIα phosphorylation of Shank3 modulates ABI1-Shank3 interaction.

Tyler L Perfitt, Philip E Stauffer, Keeley L Spiess, Roger J Colbran

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.7field-weighted citation impact, top 37% 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

5 citing papers in PubMed, 10 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

4 authors at 1 institution in 1 country.

Tyler L PerfittDepartment of Molecular Physiology & Biophysics, Vanderbilt University School of Medicine, Nashville, TN, 37232-0615, USA.
Philip E StaufferDepartment of Molecular Physiology & Biophysics, Vanderbilt University School of Medicine, Nashville, TN, 37232-0615, USA.
Keeley L SpiessDepartment of Molecular Physiology & Biophysics, Vanderbilt University School of Medicine, Nashville, TN, 37232-0615, USA.
Roger J ColbranDepartment of Molecular Physiology & Biophysics, Vanderbilt University School of Medicine, Nashville, TN, 37232-0615, USA; Vanderbilt Brain Institute, Vanderbilt University School of Medicine, Nashville, TN, 37232-0615, USA; Vanderbilt-Kennedy Center for Research on Human Development, Vanderbilt University School of Medicine, Nashville, TN, 37232-0615, USA. Electronic address: roger.colbran@vanderbilt.edu.
Vanderbilt University · US

Funding

MULTIDISCIPLINARY TRAINING IN MOLECULAR ENDOCRINOLOGYT32DK007563 · NIDDK · VANDERBILT UNIVERSITY · PI Richard M O'Brien · 1988 to 2026
$15.9M
Research Project: Sensory and Multisensory Contributions to AutismU54HD083211 · NICHD · VANDERBILT UNIVERSITY MEDICAL CENTER · PI DYKENS, ELISABETH MAY · 2015 to 2019
$7.1M
Mechanisms of CaM Kinase II Signal TransductionR01MH063232 · NIMH · VANDERBILT UNIVERSITY · PI COLBRAN, ROGER J · 2001 to 2015
$5.4M
CaMKII, endocannabinoids, synaptic plasticity and motor functionR01NS078291 · NINDS · VANDERBILT UNIVERSITY · PI COLBRAN, ROGER J · 2012 to 2016
$1.8M
NICHD NIH HHS U54 HD083211NIDDK NIH HHS T32 DK007563NIMH NIH HHS R01 MH063232NINDS NIH HHS R01 NS078291
6 · The paper itself

Abstract

Protein-protein interactions can be modulated by phosphorylation of either binding partner, thereby altering subcellular localization and/or physiological function. Shank3, a master postsynaptic scaffolding protein that controls the developmental maturation of excitatory synapses, was recently shown to be phosphorylated by Protein Kinase A (PKA) at Ser685 in vivo. Mutation of Shank3 Ser685 was shown to modulate the binding of Abelson interactor 1 (ABI1), a component of the WAVE regulatory complex for actin remodeling, but a direct effect of Ser685 phosphorylation on ABI1 binding was not investigated. Here, we demonstrate that Ca

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2CattleCyclic AMP-Dependent Protein KinasesHEK293 CellsHumansMiceMutationNerve Tissue ProteinsPhosphorylationPhosphoserineProtein BindingAdaptor Proteins, Signal TransducingCalcium-Calmodulin-Dependent Protein Kinase Type 2Cyclic AMP-Dependent Protein KinasesNerve Tissue ProteinsPhosphoserineShank3 protein, ratCaMKIIαPKAProtein phosphorylationShank3

Identifiers

PMID31983435
PMCPMC7064404
OpenAlexW3001624657

What OpenQuestion holds

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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 OpenQuestion graph.