Evidence map›Paper›PMID 19269965›Full record

ArticleThe Journal of biological chemistry2009

Dynamin-dependent membrane drift recruits AMPA receptors to dendritic spines.

Frédéric Jaskolski, Belen Mayo-Martin, David Jane, Jeremy M Henley

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
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  6. Linking Nanoscale Dynamics of AMPA Receptor Organization to Plasticity of Excitatory Synapses and Learning.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Review
  7. Review
  8. Shank3 Is Part of a Zinc-Sensitive Signaling System That Regulates Excitatory Synaptic Strength.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
    Article
  9. Article
  10. Article
  11. GluN2B-Containing NMDA Receptors Regulate AMPA Receptor Traffic through Anchoring of the Synaptic Proteasome.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  12. Article
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  15. Article
  16. Review
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  18. Review
  19. How to scale down postsynaptic strength.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    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

4 authors at 2 institutions in 1 country.

Frédéric JaskolskiDepartment of Anatomy and Physiology, Medical Research Council Centre for Synaptic Plasticity, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, United Kingdom.
Belen Mayo-Martin
David Jane
Jeremy M Henley
Medical Research Council · GBUniversity of Bristol · GB

Funding

Medical Research Council G0601810Medical Research Council G0601810(80974)Medical Research Council G0601812Wellcome Trust
6 · The paper itself

Abstract

The surface expression and localization of AMPA receptors (AMPARs) at dendritic spines are tightly controlled to regulate synaptic transmission. Here we show that de novo exocytosis of the GluR2 AMPAR subunit occurs at the dendritic shaft and that new AMPARs diffuse into spines by lateral diffusion in the membrane. However, membrane topology restricts this lateral diffusion. We therefore investigated which mechanisms recruit AMPARs to spines from the shaft and demonstrated that inhibition of dynamin GTPase activity reduced lateral diffusion of membrane-anchored green fluorescent protein and super-ecliptic pHluorin (SEP)-GluR2 into spines. In addition, the activation of synaptic N-methyl-d-aspartate (NMDA) receptors enhanced lateral diffusion of SEP-GluR2 and increased the number of endogenous AMPARs in spines. The NMDA-invoked effects were prevented by dynamin inhibition, suggesting that activity-dependent dynamin-mediated endocytosis within spines generates a net inward membrane drift that overrides lateral diffusion barriers to enhance membrane protein delivery into spines. These results provide a novel mechanistic explanation of how AMPARs and other membrane proteins are recruited to spines by synaptic activity.

Indexed as

AnimalsCell MembraneDendritic SpinesDynaminsExocytosisRatsReceptors, AMPAReceptors, N-Methyl-D-AspartateDynaminsglutamate receptor ionotropic, AMPA 2Receptors, AMPAReceptors, N-Methyl-D-Aspartate

Identifiers

PMID19269965
PMCPMC2673315
OpenAlexW2100070396

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.