Evidence map›Paper›PMID 23940795›Full record

ArticlePloS one2013

Phosphorylation of the actin binding protein Drebrin at S647 is regulated by neuronal activity and PTEN.

Patricia Kreis, Rita Hendricusdottir, Louise Kay, Ismini E Papageorgiou, Michiel van Diepen, Till Mack, Jonny Ryves, Adrian Harwood, Nicholas R Leslie, Oliver Kann and 2 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. PEBP1/RKIP behavior: a mirror of actin-membrane organization.Cellular and molecular life sciences : CMLS · 2020
    Article
  8. Review
  9. PTEN in Autism and Neurodevelopmental Disorders.Cold Spring Harbor perspectives in medicine · 2019
    Review
  10. Article
  11. PTEN Inhibition in Human Disease Therapy.Molecules (Basel, Switzerland) · 2018
    Review
  12. Article
  13. Article
  14. Drebrin and Spermatogenesis.Advances in experimental medicine and biology · 2017
    Article
  15. Article
  16. Review
  17. Review
  18. PTEN regulates cilia through Dishevelled.Nature communications · 2015
    Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 6 institutions in 2 countries.

Patricia KreisMRC Centre for Developmental Neurobiology, King's College London, London, United Kingdom.
Rita Hendricusdottir
Louise Kay
Ismini E Papageorgiou
Michiel van Diepen
Till Mack
Jonny Ryves
Adrian Harwood
Nicholas R Leslie
Oliver Kann
Maddy Parsons
Britta J Eickholt
King's College London · GBCardiff University · GBHeidelberg University · DECharité - Universitätsmedizin Berlin · DENovartis (United Kingdom) · GBUniversity of Dundee · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F015321/1Biotechnology and Biological Sciences Research Council BB/I022392/1Medical Research Council G0801865Medical Research Council G0802289Medical Research Council G0901899
6 · The paper itself

Abstract

Defects in actin dynamics affect activity-dependent modulation of synaptic transmission and neuronal plasticity, and can cause cognitive impairment. A salient candidate actin-binding protein linking synaptic dysfunction to cognitive deficits is Drebrin (DBN). However, the specific mode of how DBN is regulated at the central synapse is largely unknown. In this study we identify and characterize the interaction of the PTEN tumor suppressor with DBN. Our results demonstrate that PTEN binds DBN and that this interaction results in the dephosphorylation of a site present in the DBN C-terminus--serine 647. PTEN and pS647-DBN segregate into distinct and complimentary compartments in neurons, supporting the idea that PTEN negatively regulates DBN phosphorylation at this site. We further demonstrate that neuronal activity increases phosphorylation of DBN at S647 in hippocampal neurons in vitro and in ex vivo hippocampus slices exhibiting seizure activity, potentially by inducing rapid dissociation of the PTEN:DBN complex. Our results identify a novel mechanism by which PTEN is required to maintain DBN phosphorylation at dynamic range and signifies an unusual regulation of an actin-binding protein linked to cognitive decline and degenerative conditions at the CNS synapse.

Indexed as

ActinsAnimalsCells, CulturedEmbryo, MammalianHEK293 CellsHumansMaleNeuronsNeuropeptidesPC12 CellsPhosphorylationProtein KinasesPTEN PhosphohydrolaseRatsRats, Sprague-DawleySerineActinsdrebrinsNeuropeptidesProtein KinasesPTEN PhosphohydrolasePten protein, ratSerine

Identifiers

PMID23940795
PMCPMC3733845
OpenAlexW2149999139

What OpenQuestion holds

Textmetadata
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.