Evidence map›Paper›PMID 21965686›Full record

ArticleThe Journal of biological chemistry2011

Molecular determinants of CaV2.1 channel regulation by calcium-binding protein-1.

Alexandra P Few, Evanthia Nanou, Todd Scheuer, William A Catterall

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.2field-weighted citation impact, top 26% 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

12 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Review
  3. Calcium sensor regulation of the CaV2.1 Ca2+ channel contributes to short-term synaptic plasticity in hippocampal neurons.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  4. Article
  5. Calcium channels and short-term synaptic plasticity.The Journal of biological chemistry · 2013
    Review
  6. Protein phosphatase 2A dephosphorylates CaBP4 and regulates CaBP4 function.Investigative ophthalmology & visual science · 2013
    Article
  7. Article
  8. Fine-tuning synaptic plasticity by modulation of Ca(V)2.1 channels with Ca2+ sensor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  9. Article
  10. Article
  11. Article
  12. 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.

Alexandra P FewDepartment of Pharmacology, School of Medicine, University of Washington, Seattle, Washington 98195-7280.
Evanthia NanouDepartment of Pharmacology, School of Medicine, University of Washington, Seattle, Washington 98195-7280.
Todd ScheuerDepartment of Pharmacology, School of Medicine, University of Washington, Seattle, Washington 98195-7280.
William A CatterallDepartment of Pharmacology, School of Medicine, University of Washington, Seattle, Washington 98195-7280. Electronic address: wcatt@uw.edu.
University of Washington · US

Funding

MOLECULAR PROPERTIES OF VOLTAGE-SENSITIVE CHANNELSR01NS022625 · NINDS · UNIVERSITY OF WASHINGTON · PI CATTERALL, WILLIAM A · 1985 to 2019
$6.2M
CaM and nCaBP modulation of Cav2.1 and neurotransmissionF31MH078345 · NIMH · UNIVERSITY OF WASHINGTON · PI FEW, ALEXANDRA P · 2006 to 2007
$61k
NIMH NIH HHS F31 MH078345NINDS NIH HHS R01 NS022625NINDS NIH HHS R01 NS22625
6 · The paper itself

Abstract

Presynaptic Ca(V)2.1 channels, which conduct P/Q-type Ca(2+) currents, initiate synaptic transmission at most synapses in the central nervous system. Regulation of Ca(V)2.1 channels by CaM contributes significantly to short term facilitation and rapid depression of synaptic transmission. Short term synaptic plasticity is diverse in form and function at different synapses, yet CaM is ubiquitously expressed. Differential regulation of Ca(V)2.1 channels by CaM-like Ca(2+) sensor (CaS) proteins differentially affects short term synaptic facilitation and rapid synaptic depression in transfected sympathetic neuron synapses. Here, we define the molecular determinants for differential regulation of Ca(V)2.1 channels by the CaS protein calcium-binding protein-1 (CaBP1) by analysis of chimeras in which the unique structural domains of CaBP1 are inserted into CaM. Our results show that the N-terminal domain, including its myristoylation site, and the second EF-hand, which is inactive in Ca(2+) binding, are the key molecular determinants of differential regulation of Ca(V)2.1 channels by CaBP1. These findings give insight into the molecular code by which CaS proteins differentially regulate Ca(V)2.1 channel function and provide diversity of form and function of short term synaptic plasticity.

Indexed as

Gene Expression RegulationCalciumCalcium-Binding ProteinsCalcium Channels, N-TypeCalmodulinCell LineElectrophysiologyHumansModels, BiologicalNeuronal PlasticityNeuronsProtein BindingProtein Structure, TertiaryRecombinant Fusion ProteinsSynaptic TransmissionCalciumCalcium-Binding ProteinsCalcium Channels, N-TypeCalmodulinRecombinant Fusion Proteins

Identifiers

PMID21965686
PMCPMC3234952
OpenAlexW2088616460

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.