Evidence map›Paper›PMID 21383011›Full record

ArticleThe Journal of biological chemistry2011

CaBP1 regulates voltage-dependent inactivation and activation of Ca(V)1.2 (L-type) calcium channels.

Shimrit Oz, Vladimir Tsemakhovich, Carl J Christel, Amy Lee, Nathan Dascal

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 34 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. L-Type CaBiomolecules · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Calcium Sensors in Neuronal Function and Dysfunction.Cold Spring Harbor perspectives in biology · 2019
    Review
  12. Review
  13. Review
  14. Article
  15. Channeling Vision: CaBioMed research international · 2018
    Review
  16. C-terminal splice variants of P/Q-type CaThe Journal of biological chemistry · 2017
    Article
  17. Article
  18. Decalmodulation of Cav1 channels by CaBPs.Channels (Austin, Tex.) · 2016
    Review
  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

5 authors at 2 institutions in 2 countries.

Shimrit OzDepartment of Physiology and Pharmacology, Sackler School of Medicine, Tel Aviv University, Tel Aviv 69978, Israel.
Vladimir Tsemakhovich
Carl J Christel
Amy Lee
Nathan Dascal
Tel Aviv University · ILUniversity of Iowa · US

Funding

INTERDISCIPLINARY CARDIOVASCULAR RESEARCH FELLOWSHIPT32HL007121 · NHLBI · UNIVERSITY OF IOWA · PI LONDON, BARRY · 1985 to 2020
$15.1M
Regulation of auditory calcium channelsR01DC009433 · NIDCD · UNIVERSITY OF IOWA · PI LEE, AMY · 2009 to 2018
$3.6M
Modulation of Cav 1.3 L-type Ca2+ channels by PDZ-protein interactionsR01HL087120 · NHLBI · UNIVERSITY OF IOWA · PI LEE, AMY · 2009 to 2012
$1.4M
Regulation of auditory calcium channelsR55DC009433 · NIDCD · EMORY UNIVERSITY · PI LEE, AMY · 2008 to 2008
$100k
NHLBI NIH HHS HL087120NHLBI NIH HHS R01 HL087120NHLBI NIH HHS T32 HL007121NHLBI NIH HHS T32 HL07121NIDCD NIH HHS DC009433NIDCD NIH HHS R01 DC009433NIDCD NIH HHS R55 DC009433
6 · The paper itself

Abstract

CaBP1 is a Ca(2+)-binding protein that regulates the gating of voltage-gated (Ca(V)) Ca(2+) channels. In the Ca(V)1.2 channel α(1)-subunit (α(1C)), CaBP1 interacts with cytosolic N- and C-terminal domains and blunts Ca(2+)-dependent inactivation. To clarify the role of the α(1C) N-terminal domain in CaBP1 regulation, we compared the effects of CaBP1 on two alternatively spliced variants of α(1C) containing a long or short N-terminal domain. In both isoforms, CaBP1 inhibited Ca(2+)-dependent inactivation but also caused a depolarizing shift in voltage-dependent activation and enhanced voltage-dependent inactivation (VDI). In binding assays, CaBP1 interacted with the distal third of the N-terminal domain in a Ca(2+)-independent manner. This segment is distinct from the previously identified calmodulin-binding site in the N terminus. However, deletion of a segment in the proximal N-terminal domain of both α(1C) isoforms, which spared the CaBP1-binding site, inhibited the effect of CaBP1 on VDI. This result suggests a modular organization of the α(1C) N-terminal domain, with separate determinants for CaBP1 binding and transduction of the effect on VDI. Our findings expand the diversity and mechanisms of Ca(V) channel regulation by CaBP1 and define a novel modulatory function for the initial segment of the N terminus of α(1C).

Indexed as

Alternative SplicingAnimalsBinding SitesCalciumCalcium-Binding ProteinsCalcium ChannelsCalcium Channels, L-TypeCalmodulinFemaleGene DeletionHumansKineticsProtein BindingProtein IsoformsProtein Structure, TertiaryXenopusCa2+-binding protein-1CalciumCalcium-Binding ProteinsCalcium ChannelsCalcium Channels, L-TypeCalmodulinL-type calcium channel alpha(1C)Protein Isoforms

Identifiers

PMID21383011
PMCPMC3077595
OpenAlexW2031235320

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.