Evidence map›Paper›PMID 17576800›Full record

ArticleThe Journal of cell biology2007

Regulation of synaptic growth and maturation by a synapse-associated E3 ubiquitin ligase at the neuromuscular junction.

Zhonghua Lu, Hyun-Soo Je, Paul Young, Jimmy Gross, Bai Lu, Guoping Feng

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
2.0field-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

39 citing papers in PubMed, 1 synthesis or guideline pooled it, 64 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. A link between agrin signalling and CaScientific reports · 2022
    Article
  6. Article
  7. Proteomic analysis identifies the E3 ubiquitin ligase Pdzrn3 as a regulatory target of Wnt5a-Ror signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. PDZ Domains as Drug Targets.Advanced therapeutics · 2019
    Review
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  15. Review
  16. Article
  17. 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

6 authors at 3 institutions in 2 countries.

Zhonghua LuDepartment of Neurobiology, Duke University Medical Center, Durham, NC 27710, USA.
Hyun-Soo Je
Paul Young
Jimmy Gross
Bai Lu
Guoping Feng
Institute of Neurobiology · BGEunice Kennedy Shriver National Institute of Child Health and Human Development · USNational Institutes of Health · US

Funding

Molecular Mechanisms Of Synapse Development &PlasticityZ01HD000714 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI LU, BAI · 1996 to 2008
$2.7M
6 · The paper itself

Abstract

The ubiquitin-proteasome pathway has been implicated in synaptic development and plasticity. However, mechanisms by which ubiquitination contributes to precise and dynamic control of synaptic development and plasticity are poorly understood. We have identified a PDZ domain containing RING finger 3 (PDZRN3) as a synapse-associated E3 ubiquitin ligase and have demonstrated that it regulates the surface expression of muscle-specific receptor tyrosine kinase (MuSK), the key organizer of postsynaptic development at the mammalian neuromuscular junction. PDZRN3 binds to MuSK and promotes its ubiquitination. Regulation of cell surface levels of MuSK by PDZRN3 requires the ubiquitin ligase domain and is mediated by accelerated endocytosis. Gain- and loss-of-function studies in cultured myotubes show that regulation of MuSK by PDZRN3 plays an important role in MuSK-mediated nicotinic acetylcholine receptor clustering. Furthermore, overexpression of PDZRN3 in skeletal muscle of transgenic mice perturbs the growth and maturation of the neuromuscular junction. These results identify a synapse-associated E3 ubiquitin ligase as an important regulator of MuSK signaling.

Indexed as

Neuromuscular JunctionAnimalsCarrier ProteinsEndocytosisMiceMice, TransgenicMuscle Fibers, SkeletalMuscle, SkeletalReceptor Protein-Tyrosine KinasesSynapsesUbiquitin-Protein LigasesZinc FingersCarrier ProteinsMuSK protein, mousePDZRN3 protein, mouseReceptor Protein-Tyrosine KinasesUbiquitin-Protein Ligases

Identifiers

PMID17576800
PMCPMC2064367
OpenAlexW2006032897

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.