Evidence map›Paper›PMID 18848351›Full record

ArticleCell2008

Lrp4 is a receptor for Agrin and forms a complex with MuSK.

Natalie Kim, Amy L Stiegler, Thomas O Cameron, Peter T Hallock, Andrea M Gomez, Julie H Huang, Stevan R Hubbard, Michael L Dustin, Steven J Burden

Open access · greenAbstract read
In one paragraph

Article in Cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 371 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
371citing papers in PubMed, 3 pooled it
23.2field-weighted citation impact, top 1% 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

371 citing papers in PubMed, 3 syntheses or guidelines pooled it, 666 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Congenital myasthenic syndromes.Orphanet journal of rare diseases · 2019
    Pooled it
  4. Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Muscles (Basel, Switzerland) · 2026
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Observational
  17. Observational
  18. Article
  19. Article
  20. Review

311 more citing papers are in PubMed but not listed here.

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

9 authors at 1 institution in 1 country.

Natalie KimMolecular Neurobiology Program, Skirball Institute of Biomolecular Medicine, Helen and Martin Kimmel Center for Biology and Medicine, NYU Medical School, New York, NY 10016, USA.
Amy L Stiegler
Thomas O Cameron
Peter T Hallock
Andrea M Gomez
Julie H Huang
Stevan R Hubbard
Michael L Dustin
Steven J Burden
New York University · US

Funding

Vaccine FacilityP30CA016087 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ADRIANA HEGUY · 1985 to 2026
$83.1M
SIGNALING BY MUSK, A COMPONENT OF THE AGRIN RECEPTORR01NS036193 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI BURDEN, STEVEN · 1998 to 2012
$5.5M
Signaling by MuSK, a component of the Agrin receptor.R37NS036193 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI BURDEN, STEVEN · 2013 to 2019
$4.5M
Structure-Function Studies of the Receptor Tyrosine Kinase MuSKR01NS053414 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI HUBBARD, STEVAN R. · 2006 to 2009
$1.3M
Chemokine Receptor Chimeras by Synthetic Gene LibraryR21GM075180 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DUSTIN, MICHAEL LORAN · 2006 to 2007
$416k
NCI NIH HHS P30 CA016087NIGMS NIH HHS R21 GM075180NINDS NIH HHS NS53414NINDS NIH HHS R01 NS036193NINDS NIH HHS R01 NS053414NINDS NIH HHS R37 NS036193
6 · The paper itself

Abstract

Neuromuscular synapse formation requires a complex exchange of signals between motor neurons and skeletal muscle fibers, leading to the accumulation of postsynaptic proteins, including acetylcholine receptors in the muscle membrane and specialized release sites, or active zones in the presynaptic nerve terminal. MuSK, a receptor tyrosine kinase that is expressed in skeletal muscle, and Agrin, a motor neuron-derived ligand that stimulates MuSK phosphorylation, play critical roles in synaptic differentiation, as synapses do not form in their absence, and mutations in MuSK or downstream effectors are a major cause of a group of neuromuscular disorders, termed congenital myasthenic syndromes (CMS). How Agrin activates MuSK and stimulates synaptic differentiation is not known and remains a fundamental gap in our understanding of signaling at neuromuscular synapses. Here, we report that Lrp4, a member of the LDLR family, is a receptor for Agrin, forms a complex with MuSK, and mediates MuSK activation by Agrin.

Indexed as

AgrinAnimalsCell LineLDL-Receptor Related ProteinsMiceModels, BiologicalMyoblastsNeuromuscular JunctionPhosphorylationPrecursor Cells, B-LymphoidReceptor Protein-Tyrosine KinasesReceptors, LDLAgrinLDL-Receptor Related ProteinsLrp4 protein, mouseMuSK protein, mouseReceptor Protein-Tyrosine KinasesReceptors, LDL

Identifiers

PMID18848351
PMCPMC2933840
OpenAlexW1984522719

What OpenQuestion holds

Textmetadata
LicenceTDM
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.