Evidence map›Paper›PMID 20953164›Full record

ArticleThe EMBO journal2010

Multiple C-terminal tail Ca(2+)/CaMs regulate Ca(V)1.2 function but do not mediate channel dimerization.

Eun Young Kim, Christine H Rumpf, Filip Van Petegem, Ryan J Arant, Felix Findeisen, Elizabeth S Cooley, Ehud Y Isacoff, Daniel L Minor

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2010. 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 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

49 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. Regulation of Cardiac Cav1.2 Channels by Calmodulin.International journal of molecular sciences · 2023
    Review
  4. Regulation of Presynaptic Calcium Channels.Advances in neurobiology · 2023
    Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. NaStructure (London, England : 1993) · 2021
    Article
  10. CaThe Journal of biological chemistry · 2020
    Article
  11. Review
  12. Crystal structures of CaProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Stac Proteins Suppress CaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  15. Review
  16. Bilobal architecture is a requirement for calmodulin signaling to CaProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. Molecular moieties masking CaThe Journal of general physiology · 2018
    Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

8 authors at 4 institutions in 1 country.

Eun Young KimCardiovascular Research Institute, University of California, San Francisco, CA 94158-2330, USA.
Christine H Rumpf
Filip Van Petegem
Ryan J Arant
Felix Findeisen
Elizabeth S Cooley
Ehud Y Isacoff
Daniel L Minor
QB3 · USUniversity of California, San Francisco · USLawrence Berkeley National Laboratory · USUniversity of California, Berkeley · US

Funding

Structure and function of voltage-gated calcium channelsR01HL080050 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DANIEL L MINOR · 2005 to 2026
$9.8M
STRUCTURAL REARRANGEMENTS IN CHANNEL GATINGR01NS035549 · NINDS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ISACOFF, EHUD · 1996 to 2013
$4.1M
NHLBI NIH HHS R01 HL080050NINDS NIH HHS R01 NS035549NINDS NIH HHS R01 NS35549
6 · The paper itself

Abstract

Interactions between voltage-gated calcium channels (Ca(V)s) and calmodulin (CaM) modulate Ca(V) function. In this study, we report the structure of a Ca(2+)/CaM Ca(V)1.2 C-terminal tail complex that contains two PreIQ helices bridged by two Ca(2+)/CaMs and two Ca(2+)/CaM-IQ domain complexes. Sedimentation equilibrium experiments establish that the complex has a 2:1 Ca(2+)/CaM:C-terminal tail stoichiometry and does not form higher order assemblies. Moreover, subunit-counting experiments demonstrate that in live cell membranes Ca(V)1.2s are monomers. Thus, contrary to previous proposals, the crystallographic dimer lacks physiological relevance. Isothermal titration calorimetry and biochemical experiments show that the two Ca(2+)/CaMs in the complex have different properties. Ca(2+)/CaM bound to the PreIQ C-region is labile, whereas Ca(2+)/CaM bound to the IQ domain is not. Furthermore, neither of lobes of apo-CaM interacts strongly with the PreIQ domain. Electrophysiological studies indicate that the PreIQ C-region has a role in calcium-dependent facilitation. Together, the data show that two Ca(2+)/CaMs can bind the Ca(V)1.2 tail simultaneously and indicate a functional role for Ca(2+)/CaM at the C-region site.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCalciumCalcium Channels, L-TypeCalmodulinCell MembraneCrystallography, X-RayDimerizationHumansModels, MolecularMolecular Sequence DataProtein Structure, TertiaryXenopusCalciumCalcium Channels, L-TypeCalmodulinL-type calcium channel alpha(1C)

Identifiers

PMID20953164
PMCPMC3020648
OpenAlexW1997670307

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.