Evidence map›Paper›PMID 21297961›Full record

ArticlePloS one2011

The actin binding domain of βI-spectrin regulates the morphological and functional dynamics of dendritic spines.

Michael W Nestor, Xiang Cai, Michele R Stone, Robert J Bloch, Scott M Thompson

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

27 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  10. Ankyrins: Roles in synaptic biology and pathology.Molecular and cellular neurosciences · 2018
    Review
  11. Article
  12. Article
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  15. Inositol Hexakisphosphate Kinase-3 Regulates the Morphology and Synapse Formation of Cerebellar Purkinje Cells via Spectrin/Adducin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  16. Article
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  18. Review
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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.

Michael W NestorDepartment of Physiology, University of Maryland School of Medicine, Baltimore, Maryland, United States of America.
Xiang Cai
Michele R Stone
Robert J Bloch
Scott M Thompson
University of Maryland, Baltimore · US

Funding

TRAINING PROGRAM IN INTEGRATIVE MEMBRANE BIOLOGYT32GM008181 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE · PI RIZZO, MEGAN A, TRUDEAU, MATTHEW C · 1987 to 2022
$4.9M
Training Program in Cellular &Integrative NeuroscienceT32NS007375 · NINDS · UNIVERSITY OF MARYLAND BALTIMORE · PI KELLER, ASAF · 1994 to 2013
$4.2M
Cytoskeletal Architecture of T-Tubules in HeartR01HL075106 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI BLOCH, ROBERT J · 2004 to 2008
$1.8M
Plasticity of Hippocampal Structure and FunctionR01MH065488 · NIMH · UNIVERSITY OF MARYLAND BALTIMORE · PI THOMPSON, SCOTT M. · 2002 to 2006
$1.5M
NHLBI NIH HHS R01 HL075106NHLBI NIH HHS R01 HL75106NIGMS NIH HHS T32 GM008181NIGMS NIH HHS T32 GM08181NIMH NIH HHS R01 MH065488NIMH NIH HHS R01 MH65488NINDS NIH HHS T32 NS007375NINDS NIH HHS T32 NS07375
6 · The paper itself

Abstract

Actin microfilaments regulate the size, shape and mobility of dendritic spines and are in turn regulated by actin binding proteins and small GTPases. The βI isoform of spectrin, a protein that links the actin cytoskeleton to membrane proteins, is present in spines. To understand its function, we expressed its actin-binding domain (ABD) in CA1 pyramidal neurons in hippocampal slice cultures. The ABD of βI-spectrin bundled actin in principal dendrites and was concentrated in dendritic spines, where it significantly increased the size of the spine head. These effects were not observed after expression of homologous ABDs of utrophin, dystrophin, and α-actinin. Treatment of slice cultures with latrunculin-B significantly decreased spine head size and decreased actin-GFP fluorescence in cells expressing the ABD of α-actinin, but not the ABD of βI-spectrin, suggesting that its presence inhibits actin depolymerization. We also observed an increase in the area of GFP-tagged PSD-95 in the spine head and an increase in the amplitude of mEPSCs at spines expressing the ABD of βI-spectrin. The effects of the βI-spectrin ABD on spine size and mEPSC amplitude were mimicked by expressing wild-type Rac3, a small GTPase that co-immunoprecipitates specifically with βI-spectrin in extracts of cultured cortical neurons. Spine size was normal in cells co-expressing a dominant negative Rac3 construct with the βI-spectrin ABD. We suggest that βI-spectrin is a synaptic protein that can modulate both the morphological and functional dynamics of dendritic spines, perhaps via interaction with actin and Rac3.

Indexed as

ActinsAnimalsAnimals, NewbornBinding SitesCA1 Region, HippocampalCell ShapeDendritic SpinesMicrofilament ProteinsNerve Tissue ProteinsProtein Isoformsrac GTP-Binding ProteinsRatsSpectrinActinsMicrofilament ProteinsNerve Tissue ProteinsProtein Isoformsrac GTP-Binding ProteinsSpectrin

Identifiers

PMID21297961
PMCPMC3031527
OpenAlexW2022258246

What OpenQuestion holds

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LicenceCC BY
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.