Evidence map›Paper›PMID 23626724›Full record

ArticlePloS one2013

The calmodulin-binding, short linear motif, NSCaTE is conserved in L-type channel ancestors of vertebrate Cav1.2 and Cav1.3 channels.

Valentina Taiakina, Adrienne N Boone, Julia Fux, Adriano Senatore, Danielle Weber-Adrian, J Guy Guillemette, J David Spafford

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 32 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 13% 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

32 citing papers in PubMed, 1 synthesis or guideline pooled it, 47 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Regulation of Cardiac Cav1.2 Channels by Calmodulin.International journal of molecular sciences · 2023
    Review
  9. Article
  10. Article
  11. Conserved biophysical features of the CaThe Journal of biological chemistry · 2020
    Article
  12. Article
  13. CaThe Journal of biological chemistry · 2020
    Article
  14. Article
  15. Article
  16. Review
  17. Conservation of cardiac L-type CaJournal of molecular and cellular cardiology · 2018
    Article
  18. Bilobal architecture is a requirement for calmodulin signaling to CaProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Valentina TaiakinaDepartment of Chemistry, University of Waterloo, Waterloo, Canada.
Adrienne N Boone
Julia Fux
Adriano Senatore
Danielle Weber-Adrian
J Guy Guillemette
J David Spafford
University of Waterloo · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NSCaTE is a short linear motif of (xWxxx(I or L)xxxx), composed of residues with a high helix-forming propensity within a mostly disordered N-terminus that is conserved in L-type calcium channels from protostome invertebrates to humans. NSCaTE is an optional, lower affinity and calcium-sensitive binding site for calmodulin (CaM) which competes for CaM binding with a more ancient, C-terminal IQ domain on L-type channels. CaM bound to N- and C- terminal tails serve as dual detectors to changing intracellular Ca(2+) concentrations, promoting calcium-dependent inactivation of L-type calcium channels. NSCaTE is absent in some arthropod species, and is also lacking in vertebrate L-type isoforms, Cav1.1 and Cav1.4 channels. The pervasiveness of a methionine just downstream from NSCaTE suggests that L-type channels could generate alternative N-termini lacking NSCaTE through the choice of translational start sites. Long N-terminus with an NSCaTE motif in L-type calcium channel homolog LCav1 from pond snail Lymnaea stagnalis has a faster calcium-dependent inactivation than a shortened N-termini lacking NSCaTE. NSCaTE effects are present in low concentrations of internal buffer (0.5 mM EGTA), but disappears in high buffer conditions (10 mM EGTA). Snail and mammalian NSCaTE have an alpha-helical propensity upon binding Ca(2+)-CaM and can saturate both CaM N-terminal and C-terminal domains in the absence of a competing IQ motif. NSCaTE evolved in ancestors of the first animals with internal organs for promoting a more rapid, calcium-sensitive inactivation of L-type channels.

Indexed as

Amino Acid MotifsAnimalsBinding SitesBiological EvolutionCalcium Channels, L-TypeCalmodulinConserved SequenceGene ExpressionGenes, ReporterGreen Fluorescent ProteinsHEK293 CellsHumansMolecular Sequence DataPatch-Clamp TechniquesPhylogenyProtein BindingCACNA1D protein, humanCalcium Channels, L-TypeCalmodulinGreen Fluorescent ProteinsL-type calcium channel alpha(1C)

Identifiers

PMID23626724
PMCPMC3634016
OpenAlexW1972450594

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.