Evidence map›Paper›PMID 24566975›Full record

ArticlePflugers Archiv : European journal of physiology2014

CaV2.2 channel cell surface expression is regulated by the light chain 1 (LC1) of the microtubule-associated protein B (MAP1B) via UBE2L3-mediated ubiquitination and degradation.

María A Gandini, Daniel R Henríquez, Lizbeth Grimaldo, Alejandro Sandoval, Christophe Altier, Gerald W Zamponi, Ricardo Felix, Christian González-Billault

Abstract read
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In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. The MAP1B Binding Domain of NaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
  5. MAP1B Light Chain Modulates Synaptic Transmission via AMPA Receptor Intracellular Trapping.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  6. Article
  7. Review
  8. Article
  9. Spinal Fbxo3-Dependent Fbxl2 Ubiquitination of Active Zone Protein RIM1α Mediates Neuropathic Allodynia through CaV2.2 Activation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
    Article
  10. Article
  11. Review
  12. Article
  13. The axonal cytoskeleton: from organization to function.Frontiers in molecular neuroscience · 2015
    Review
  14. Article
  15. 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

8 authors at 4 institutions in 3 countries.

María A GandiniDepartment of Cell Biology, Center for Research and Advanced Studies of the National Polytechnic Institute, (Cinvestav-IPN), Avenida IPN 2508, Colonia Zacatenco, Mexico DF, 07360, Mexico.
Daniel R Henríquez
Lizbeth Grimaldo
Alejandro Sandoval
Christophe Altier
Gerald W Zamponi
Ricardo Felix
Christian González-Billault
Instituto Politécnico Nacional · MXUniversity of Calgary · CAUniversity of Chile · CLAutonomous University of Tlaxcala · MX

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Microtubule-associated protein B is a cytoskeleton protein consisting of heavy and light (LC) chains that play important roles in the regulation of neuronal morphogenesis and function. LC1 is also well known to interact with diverse ionotropic receptors at postsynapse. Much less is known, however, regarding the role of LC1 at presynaptic level where voltage-gated N-type Ca(2+) channels couple membrane depolarization to neurotransmitter release. Here, we investigated whether LC1 interacts with the N-type channels. Co-localization analysis revealed spatial proximity of the two proteins in hippocampal neurons. The interaction between LC1 and the N-type channel was demonstrated using co-immunoprecipitation experiments and in vitro pull-down assays. Detailed biochemical analysis suggested that the interaction occurs through the N-terminal of LC1 and the C-terminal of the pore-forming CaVα1 subunit of the channels. Patch-clamp studies in HEK-293 cells revealed a significant decrease in N-type currents upon LC1 expression, without apparent changes in kinetics. Recordings performed in the presence of MG132 prevented the actions of LC1 suggesting enhanced channel proteasomal degradation. Interestingly, using the yeast two-hybrid system and immunoprecipitation assays in HEK-293 cells, we revealed an interaction between LC1 and the ubiquitin-conjugating enzyme UBE2L3. Furthermore, we found that the LC1/UBE2L3 complex could interact with the N-type channels, suggesting that LC1 may act as a scaffold protein to increase UBE2L3-mediated channel ubiquitination. Together these results revealed a novel functional coupling between LC1 and the N-type channels.

Indexed as

Calcium Channels, N-TypeCell MembraneCells, CulturedHEK293 CellsHippocampusHumansImmunoprecipitationMicrotubule-Associated ProteinsNeuronsProteasome Endopeptidase ComplexProteolysisTwo-Hybrid System TechniquesUbiquitinUbiquitinationUbiquitin-Conjugating EnzymesCACNA1B protein, humanCalcium Channels, N-TypeMAP1B protein, humanMicrotubule-Associated ProteinsProteasome Endopeptidase ComplexUBE2L3 protein, humanUbiquitinUbiquitin-Conjugating Enzymes

Identifiers

PMID24566975
OpenAlexW2054870472

What OpenQuestion holds

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Registered trials

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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.