Evidence map›Paper›PMID 8922419›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1996

Emergence of activity-dependent, bidirectional control of microtubule-associated protein MAP2 phosphorylation during postnatal development.

E M Quinlan, S Halpain

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 90 citations in OpenAlex.

  1. Differential regulation of MAP2 by phosphorylation events in proline-rich versus C-terminal domains.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023
    Article
  2. More than a marker: potential pathogenic functions of MAP2.Frontiers in molecular neuroscience · 2022
    Article
  3. Article
  4. Article
  5. Article
  6. Mesoscale Architecture Shapes Initiation and Richness of Spontaneous Network Activity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  7. Article
  8. Article
  9. Article
  10. Intrinsic disorder in scaffold proteins: getting more from less.Progress in biophysics and molecular biology · 2008
    Review
  11. Article
  12. Article
  13. Article
  14. Bilirubin, formed by activation of heme oxygenase-2, protects neurons against oxidative stress injury.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  15. Review
  16. Role of MAP kinase in neurons.Molecular neurobiology · 1998
    Review
  17. Experience-dependent modifications in MAP2 phosphorylation in rat olfactory bulb.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1997
    Article
  18. Review
  19. Article
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

2 authors at 2 institutions in 1 country.

E M QuinlanDepartment of Neuroscience, University of Virginia, Charlottesville 22908, USA.
S Halpain
Scripps Research Institute · USUniversity of Virginia · US

Funding

CYTOSKELETAL TARGETS OF NEURONAL SIGNALINGR01MH050861 · NIMH · SCRIPPS RESEARCH INSTITUTE, THE · PI HALPAIN, SHELLEY L · 1998 to 2006
$2.5M
CYTOSKELETAL TARGETS OF NEURONAL SIGNALINGR29MH050861 · NIMH · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HALPAIN, SHELLEY L · 1994 to 1998
–
NIMH NIH HHS MH50861NIMH NIH HHS R01 MH050861NIMH NIH HHS R29 MH050861NINDS NIH HHS NS07199
6 · The paper itself

Abstract

Pronounced changes in neuronal morphology occur as synapses mature; however, little is known about how synaptic transmission regulates the developing neuronal cytoskeleton. The postsynaptic, microtubule-associated protein MAP2 is a target of multiple, calcium-dependent signaling pathways activated by synaptic transmission. Here we demonstrate that MAP2 phosphorylation is differentially regulated across development. In 32P-labeled hippocampal slices prepared from adult rats, depolarization stimulated a bidirectional change in the phosphorylation of immunoprecipitated MAP2. A transient increase was mediated by metabotropic glutamate receptors (mGluRs) and stimulation of mitogen-activated protein kinases (MAPKs), Ca2+/calmodulin-dependent protein kinases (CaMKs), and protein kinase C (PKC). This increase was followed by a persistent dephosphorylation mediated by NMDA receptors and activation of protein phosphatase 2B (PP2B or calcineurin). In contrast, depolarization of neonatal hippocampal slices stimulated exclusively a net increase in MAP2 phosphorylation, which was attenuated by inhibitors of MAPKs, but not CaMKs or PKC. Furthermore, although incubation in NMDA induced a time-dependent decrease in MAP2 phosphorylation in both adults and neonates, this effect was both less robust and less sensitive to calcineurin inhibitors in neonates than in adults. These data indicate that the mechanisms coupling glutamate release to MAP2 dephosphorylation are relatively lacking in the neonatal hippocampus. Highly phosphorylated MAP2 is impaired in its ability to stabilize microtubules and actin filament bundles in vitro. The neonatal propensity toward glutamate-stimulated MAP2 phosphorylation may serve to reduce cytoskeletal stability and permit dendritic arborization early in postnatal development. In mature neurons, the bidirectional control of MAP2 phosphorylation may participate in activity-dependent synaptic remodeling.

Indexed as

AgingAnimalsAnimals, NewbornCalcineurinCalmodulin-Binding ProteinsFemaleHippocampusIn Vitro TechniquesMicrotubule-Associated ProteinsModels, NeurologicalNerve Tissue ProteinsPhosphoprotein PhosphatasesPhosphorylationProtein KinasesRatsRats, Sprague-DawleyCalcineurinCalmodulin-Binding ProteinsMicrotubule-Associated ProteinsNerve Tissue ProteinsPhosphoprotein PhosphatasesProtein KinasesReceptors, Metabotropic GlutamateReceptors, N-Methyl-D-Aspartate

Identifiers

PMID8922419
PMCPMC6579079
OpenAlexW1565722988

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.