Evidence map›Paper›PMID 24394417›Full record

ArticleThe Journal of biological chemistry2014

Ankyrin-B regulates Cav2.1 and Cav2.2 channel expression and targeting.

Crystal F Kline, John Scott, Jerry Curran, Thomas J Hund, Peter J Mohler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Trial
  2. Review
  3. Review
  4. Article
  5. The T-type calcium channelosome.Pflugers Archiv : European journal of physiology · 2024
    Review
  6. Article
  7. Role of CaArchives of toxicology · 2023
    Review
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  10. Review
  11. Article
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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 1 country.

Crystal F KlineFrom the Dorothy M. Davis Heart and Lung Research Institute.
John Scott
Jerry Curran
Thomas J Hund
Peter J Mohler
The Ohio State University · USThe Ohio State University Wexner Medical Center · US

Funding

Role of spectrin/ankyrin-G complex in myocyte signaling and cardiac excitabilityR01HL083422 · NHLBI · VANDERBILT UNIVERSITY · PI MOHLER, PETER J. · 2006 to 2016
$3.8M
Role of ankyrin-B in human arrhythmiaR01HL084583 · NHLBI · UNIVERSITY OF IOWA · PI MOHLER, PETER J. · 2006 to 2015
$3.4M
EHD proteins in cardiac membrane protein targeting and remodelingR01HL114383 · NHLBI · OHIO STATE UNIVERSITY · PI BOYDEN, PENELOPE ALTMAN, MOHLER, PETER J. · 2013 to 2016
$2.1M
CaMKII-dependent regulation of cardiac excitabilityR01HL114893 · NHLBI · OHIO STATE UNIVERSITY · PI HUND, THOMAS JEFFREY · 2012 to 2016
$1.9M
Spectrin-based signaling complex regulates cardiac excitabilityR00HL096805 · NHLBI · UNIVERSITY OF IOWA · PI HUND, THOMAS JEFFREY · 2010 to 2012
$747k
Spectrin-based signaling complex regulates cardiac excitabilityK99HL096805 · NHLBI · UNIVERSITY OF IOWA · PI HUND, THOMAS JEFFREY · 2009 to 2009
$107k
NHLBI NIH HHS HL083422NHLBI NIH HHS HL084583NHLBI NIH HHS HL096805NHLBI NIH HHS HL114383NHLBI NIH HHS HL114893NHLBI NIH HHS K99 HL096805NHLBI NIH HHS R00 HL096805NHLBI NIH HHS R01 HL083422NHLBI NIH HHS R01 HL084583NHLBI NIH HHS R01 HL114383NHLBI NIH HHS R01 HL114893
6 · The paper itself

Abstract

N-type and P/Q-type calcium channels are documented players in the regulation of synaptic function; however, the mechanisms underlying their expression and cellular targeting are poorly understood. Ankyrin polypeptides are essential for normal integral membrane protein expression in a number of cell types, including neurons, cardiomyocytes, epithelia, secretory cells, and erythrocytes. Ankyrin dysfunction has been linked to defects in integral protein expression, abnormal cellular function, and disease. Here, we demonstrate that ankyrin-B associates with Cav2.1 and Cav2.2 in cortex, cerebellum, and brain stem. Additionally, using in vitro and in vivo techniques, we demonstrate that ankyrin-B, via its membrane-binding domain, associates with a highly conserved motif in the DII/III loop domain of Cav2.1 and Cav2.2. Further, we demonstrate that this domain is necessary for proper targeting of Cav2.1 and Cav2.2 in a heterologous system. Finally, we demonstrate that mutation of a single conserved tyrosine residue in the ankyrin-binding motif of both Cav2.1 (Y797E) and Cav2.2 (Y788E) results in loss of association with ankyrin-B in vitro and in vivo. Collectively, our findings identify an interaction between ankyrin-B and both Cav2.1 and Cav2.2 at the amino acid level that is necessary for proper Cav2.1 and Cav2.2 targeting in vivo.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsAnkyrinsBrainCalcium Channels, N-TypeConserved SequenceHEK293 CellsHumansImmunoprecipitationMiceMice, Inbred C57BLMice, KnockoutMolecular Sequence DataProtein BindingPurkinje CellsAnk2 protein, mouseAnk3 protein, mouseAnkyrinsCacna1b protein, mouseCalcium Channels, N-TypeTyrosineAdaptor ProteinsCytoskeletonIon ChannelsMembrane TraffickingProtein SortingProtein Targeting

Identifiers

PMID24394417
PMCPMC3931084
OpenAlexW2043174693

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.