Evidence map›Paper›PMID 17224403›Full record

ArticleNeuron2007

PAR-1 kinase phosphorylates Dlg and regulates its postsynaptic targeting at the Drosophila neuromuscular junction.

Yali Zhang, Huifu Guo, Helen Kwan, Ji-Wu Wang, Jon Kosek, Bingwei Lu

Open access · bronzeAbstract read
In one paragraph

Article in Neuron, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

53 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Nonionic signaling rapidly remodels postsynaptic DLG to induce retrograde homeostatic plasticity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Neuroplasticity in the transition from acute to chronic pain.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2024
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. A Presynaptic Function of Shank Protein inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  17. Article
  18. Article
  19. Article
  20. Regulation of Cell Polarity by PAR-1/MARK Kinase.Current topics in developmental biology · 2017
    Review
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

6 authors at 4 institutions in 1 country.

Yali ZhangDepartment of Pathology, Stanford University School of Medicine, GRECC/VAPAHCS, Palo Alto, CA 94304, USA.
Huifu Guo
Helen Kwan
Ji-Wu Wang
Jon Kosek
Bingwei Lu
Stanford University · USBlanchette Rockefeller Neurosciences Institute · USGeriatric Research Education and Clinical Center · USVA Palo Alto Health Care System · US

Funding

Role of PAR-1 Kinase in SynaptogenesisR01MH080378 · NIMH · STANFORD UNIVERSITY · PI LU, BINGWEI · 2009 to 2018
$4.0M
Control of Asymmetric Neural Stem Cell DivisionR01NS043167 · NINDS · STANFORD UNIVERSITY · PI LU, BINGWEI · 2003 to 2011
$2.6M
NIMH NIH HHS R01 MH080378NINDS NIH HHS NS043167NINDS NIH HHS R01 NS043167
6 · The paper itself

Abstract

Targeting of synaptic molecules to their proper location is essential for synaptic differentiation and plasticity. PSD-95/Dlg proteins have been established as key components of the postsynapse. However, the molecular mechanisms regulating the synaptic targeting, assembly, and disassembly of PSD-95/Dlg are not well understood. Here we show that PAR-1 kinase, a conserved cell polarity regulator, is critically involved in controlling the postsynaptic localization of Dlg. PAR-1 is prominently localized at the Drosophila neuromuscular junction (NMJ). Loss of PAR-1 function leads to increased synapse formation and synaptic transmission, whereas overexpression of PAR-1 has the opposite effects. PAR-1 directly phosphorylates Dlg at a conserved site and negatively regulates its mobility and targeting to the postsynapse. The ability of a nonphosphorylatable Dlg to largely rescue PAR-1-induced synaptic defects supports the idea that Dlg is a major synaptic substrate of PAR-1. Control of Dlg synaptic targeting by PAR-1-mediated phosphorylation thus constitutes a critical event in synaptogenesis.

Indexed as

AnimalsAnimals, Genetically ModifiedDrosophilaDrosophila ProteinsFluorescence Recovery After PhotobleachingGlycogen Synthase Kinase 3In Vitro TechniquesNeuromuscular JunctionPhosphorylationProtein KinasesProtein Serine-Threonine KinasesSynapsesSynaptic TransmissionTissue DistributionTumor Suppressor Proteinsdlg1 protein, DrosophilaDrosophila ProteinsGlycogen Synthase Kinase 3Par-1 protein, DrosophilaProtein KinasesProtein Serine-Threonine KinasesTumor Suppressor Proteins

Identifiers

PMID17224403
PMCPMC1855201
OpenAlexW2004921139

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.