Evidence map›Paper›PMID 22807451›Full record

ArticleThe Journal of biological chemistry2012

The polarity protein partitioning-defective 1 (PAR-1) regulates dendritic spine morphogenesis through phosphorylating postsynaptic density protein 95 (PSD-95).

Qian Wu, Victoria L DiBona, Laura P Bernard, Huaye Zhang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Neuronal connectivity, behavioral, and transcriptional alterations associated with the loss of MARK2.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Regulation of Cell Polarity by PAR-1/MARK Kinase.Current topics in developmental biology · 2017
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. 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

4 authors at 1 institution in 1 country.

Qian WuDepartment of Neuroscience and Cell Biology, UMDNJ-Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.
Victoria L DiBona
Laura P Bernard
Huaye Zhang
Johnson University · US

Funding

The PAR-6/aPKC Polarity Complex in Synaptic Assembly and FunctionR00NS065183 · NINDS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI ZHANG, HUAYE · 2011 to 2013
$738k
The PAR-6/aPKC Polarity Complex in Synaptic Assembly and FunctionK99NS065183 · NINDS · UNIVERSITY OF VIRGINIA · PI ZHANG, HUAYE · 2009 to 2010
$180k
NINDS NIH HHS K99 NS065183NINDS NIH HHS NS065183NINDS NIH HHS R00 NS065183
6 · The paper itself

Abstract

The polarity protein PAR-1 plays an essential role in many cellular contexts, including embryogenesis, asymmetric cell division, directional migration, and epithelial morphogenesis. Despite its known importance in different cellular processes, the role of PAR-1 in neuronal morphogenesis is less well understood. In particular, its role in the morphogenesis of dendritic spines, which are sites of excitatory synaptic inputs, has been unclear. Here, we show that PAR-1 is required for normal spine morphogenesis in hippocampal neurons. We further show that PAR-1 functions through phosphorylating the synaptic scaffolding protein PSD-95 in this process. Phosphorylation at a conserved serine residue in the KXGS motif in PSD-95 regulates spine morphogenesis, and a phosphomimetic mutant of this site can rescue the defects of kinase-dead PAR-1. Together, our findings uncover a role of PAR-1 in spine morphogenesis in hippocampal neurons through phosphorylating PSD-95.

Indexed as

Amino Acid MotifsAnimalsCells, CulturedDendritic SpinesDisks Large Homolog 4 ProteinHippocampusHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMutationPhosphorylationProtein Serine-Threonine KinasesRatsSynapsesDisks Large Homolog 4 ProteinDLG4 protein, humanDlg4 protein, ratIntracellular Signaling Peptides and ProteinsMARK1 protein, humanMark1 protein, ratMARK2 protein, humanMARK2 protein, ratMembrane ProteinsProtein Serine-Threonine Kinases

Identifiers

PMID22807451
PMCPMC3436321
OpenAlexW2016428540

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.