Evidence map›Paper›PMID 21233207›Full record

ArticleThe Journal of biological chemistry2011

Beta-subunits promote the expression of Ca(V)2.2 channels by reducing their proteasomal degradation.

Dominic Waithe, Laurent Ferron, Karen M Page, Kanchan Chaggar, Annette C Dolphin

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 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

79 citing papers in PubMed, 122 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Pin1 promotes human CaCell communication and signaling : CCS · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Active Zone Trafficking of CaV2/UNC-2 Channels Is Independent of β/CCB-1 and α2δ/UNC-36 Subunits.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Article
  11. EMC chaperone-CaNature · 2023
    Article
  12. Regulation of Presynaptic Calcium Channels.Advances in neurobiology · 2023
    Article
  13. Article
  14. Calcium Channels in Retinal Function and Disease.Annual review of vision science · 2022
    Review
  15. Review
  16. Review
  17. Review
  18. The life cycle of voltage-gated CaNeuronal signaling · 2021
    Review
  19. Review
  20. Article

19 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

5 authors at 1 institution in 1 country.

Dominic WaitheDepartment of Neuroscience, Physiology and Pharmacology, University College London, Gower St., London WC1E 6BT, United Kingdom.
Laurent Ferron
Karen M Page
Kanchan Chaggar
Annette C Dolphin
University College London · GB

Funding

High throughput NAPPA-proteoimmunomics and Vibrio cholerae vaccine developmentU01AI077883 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI RYAN, EDWARD T. · 2008 to 2012
$5.6M
British Heart FoundationNIAID NIH HHS U01 AI077883Wellcome TrustWellcome Trust 077883
6 · The paper itself

Abstract

The β-subunits of voltage-gated calcium channels regulate their functional expression and properties. Two mechanisms have been proposed for this, an effect on gating and an enhancement of expression. With respect to the effect on expression, β-subunits have been suggested to enhance trafficking by masking an unidentified endoplasmic reticulum (ER) retention signal. Here we have investigated whether, and how, β-subunits affect the level of Ca(V)2.2 channels within somata and neurites of cultured sympathetic neurons. We have used YFP-Ca(V)2.2 containing a mutation (W391A), that prevents binding of β-subunits to its I-II linker and found that expression of this channel was much reduced compared with WT CFP-Ca(V)2.2 when both were expressed in the same neuron. This effect was particularly evident in neurites and growth cones. The difference between the levels of YFP-Ca(V)2.2(W391A) and CFP-Ca(V)2.2(WT) was lost in the absence of co-expressed β-subunits. Furthermore, the relative reduction of expression of Ca(V)2.2(W391A) compared with the WT channel was reversed by exposure to two proteasome inhibitors, MG132 and lactacystin, particularly in the somata. In further experiments in tsA-201 cells, we found that proteasome inhibition did not augment the cell surface Ca(V)2.2(W391A) level but resulted in the observation of increased ubiquitination, particularly of mutant channels. In contrast, we found no evidence for selective retention of Ca(V)2.2(W391A) in the ER, in either the soma or growth cones. In conclusion, there is a marked effect of β-subunits on Ca(V)2.2 expression, particularly in neurites, but our results point to protection from proteasomal degradation rather than masking of an ER retention signal.

Indexed as

AcetylcysteineAmino Acid SubstitutionAnimalsCalcium Channels, N-TypeChlorocebus aethiopsCOS CellsCysteine Proteinase InhibitorsEndoplasmic ReticulumGene Expression RegulationLeupeptinsMutation, MissenseNerve Tissue ProteinsNeuritesProteasome Endopeptidase ComplexProteasome InhibitorsRabbitsAcetylcysteinebenzyloxycarbonylleucyl-leucyl-leucine aldehydeCacna1b protein, ratCalcium Channels, N-TypeCysteine Proteinase InhibitorslactacystinLeupeptinsNerve Tissue ProteinsProteasome Endopeptidase ComplexProteasome Inhibitors

Identifiers

PMID21233207
PMCPMC3059031
OpenAlexW1993855785

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.