Evidence map›Paper›PMID 20731762›Full record

ArticleJournal of neurochemistry2010

Presynaptic calcium channels and α3-integrins are complexed with synaptic cleft laminins, cytoskeletal elements and active zone components.

Steven S Carlson, Gregorio Valdez, Joshua R Sanes

Open access · greenAbstract read
In one paragraph

Article in Journal of neurochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 1 pooled it
2.9field-weighted citation impact, top 10% 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

37 citing papers in PubMed, 1 synthesis or guideline pooled it, 56 citations in OpenAlex.

  1. Cell adhesion and intracellular calcium signaling in neurons.Cell communication and signaling : CCS · 2013
    Pooled it
  2. Review
  3. Neuronal Calcium Signaling and Cytoskeletal Dynamics in Neurodegeneration.International journal of molecular sciences · 2026
    Review
  4. Article
  5. Article
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  7. Review
  8. Review
  9. Article
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  13. Article
  14. Article
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  16. Article
  17. The role of laminins in the organization and function of neuromuscular junctions.Matrix biology : journal of the International Society for Matrix Biology · 2017
    Review
  18. Article
  19. Article
  20. 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

3 authors at 2 institutions in 1 country.

Steven S CarlsonDepartment of Physiology and Biophysics, University of Washington, Seattle, Washington 98195, USA. ssc1@u.washington.edu
Gregorio Valdez
Joshua R Sanes
Harvard University · USUniversity of Washington · US

Funding

Extracellular Matrix and Neuromuscular DevelopmentR37NS019195 · NINDS · HARVARD UNIVERSITY · PI SANES, JOSHUA R · 2005 to 2011
$4.0M
Synaptic Laminin and the Calcium ChannelR01NS044243 · NINDS · UNIVERSITY OF WASHINGTON · PI CARLSON, STEVEN SCOTT · 2003 to 2006
$1.0M
NINDS NIH HHS R01 NS044243NINDS NIH HHS R37 NS019195
6 · The paper itself

Abstract

At chemical synapses, synaptic cleft components interact with elements of the nerve terminal membrane to promote differentiation and regulate function. Laminins containing the β2 subunit are key cleft components, and they act in part by binding the pore-forming subunit of a pre-synaptic voltage-gated calcium channel (Ca(v)α) (Nishimune et al. 2004). In this study, we identify Ca(v)α-associated intracellular proteins that may couple channel-anchoring to assembly or stabilization of neurotransmitter release sites called active zones. Using Ca(v)α-antibodies, we isolated a protein complex from Torpedo electric organ synapses, which resemble neuromuscular junctions but are easier to isolate in bulk. We identified 10 components of the complex: six cytoskeletal proteins (α2/β2 spectrins, plectin 1, AHNAK/desmoyokin, dystrophin, and myosin 1), two active zone components (bassoon and piccolo), synaptic laminin, and a calcium channel β subunit. Immunocytochemistry confirmed these proteins in electric organ synapses, and PCR analysis revealed their expression by developing mammalian motor neurons. Finally, we show that synaptic laminins also interact with pre-synaptic integrins containing the α3 subunit. Together with our previous finding that a distinct synaptic laminin interacts with SV2 on nerve terminals (Son et al. 2000), our results identify three paths by which synaptic cleft laminins can send developmentally important signals to nerve terminals.

Indexed as

AnimalsAxonsCalcium ChannelsCaveolin 1Cytoskeletal ProteinsElectrophoresis, Polyacrylamide GelImmunohistochemistryImmunoprecipitationIntegrin alpha3LamininMiceMotor NeuronsNerve EndingsProtein BindingRabbitsRatsCalcium ChannelsCaveolin 1Cytoskeletal ProteinsIntegrin alpha3Laminin

Identifiers

PMID20731762
PMCPMC2970707
OpenAlexW1489731866

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.