Evidence map›Paper›PMID 22936811›Full record

ArticleThe Journal of biological chemistry2012

Complex regulation of voltage-dependent activation and inactivation properties of retinal voltage-gated Cav1.4 L-type Ca2+ channels by Ca2+-binding protein 4 (CaBP4).

Lior Shaltiel, Christos Paparizos, Stefanie Fenske, Sami Hassan, Christian Gruner, Katrin Rötzer, Martin Biel, Christian A Wahl-Schott

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
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

38 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. L-Type Voltage-Gated CaBiochemistry · 2025
    Article
  3. Review
  4. Review
  5. Calcium-Binding Protein 4 Is Fundamental for Retinal Structure and Function.Advances in experimental medicine and biology · 2025
    Review
  6. Article
  7. Review
  8. Article
  9. Translational pediatrics · 2024
    Article
  10. Regulation of Presynaptic Calcium Channels.Advances in neurobiology · 2023
    Article
  11. Calcium Channels in Retinal Function and Disease.Annual review of vision science · 2022
    Review
  12. A novel missense creatine mutant ofTranslational pediatrics · 2022
    Article
  13. Cav1.4 dysfunction and congenital stationary night blindness type 2.Pflugers Archiv : European journal of physiology · 2021
    Review
  14. Review
  15. Review
  16. Calcium Sensors in Neuronal Function and Dysfunction.Cold Spring Harbor perspectives in biology · 2019
    Review
  17. Splicing of an automodulatory domain in CaThe Journal of general physiology · 2018
    Article
  18. Review
  19. Channeling Vision: CaBioMed research international · 2018
    Review
  20. Article
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

8 authors at 1 institution in 1 country.

Lior ShaltielCenter for Integrated Protein Science CIPS-M, Department Pharmazie, Ludwig-Maximilians-Universität München, D-81377 München, Germany.
Christos Paparizos
Stefanie Fenske
Sami Hassan
Christian Gruner
Katrin Rötzer
Martin Biel
Christian A Wahl-Schott
Ludwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cav1.4 L-type Ca(2+) channels are crucial for synaptic transmission in retinal photoreceptors and bipolar neurons. Recent studies suggest that the activity of this channel is regulated by the Ca(2+)-binding protein 4 (CaBP4). In the present study, we explored this issue by examining functional effects of CaBP4 on heterologously expressed Cav1.4. We show that CaBP4 dramatically increases Cav1.4 channel availability. This effect crucially depends on the presence of the C-terminal ICDI (inhibitor of Ca(2+)-dependent inactivation) domain of Cav1.4 and is absent in a Cav1.4 mutant lacking the ICDI. Using FRET experiments, we demonstrate that CaBP4 interacts with the IQ motif of Cav1.4 and that it interferes with the binding of the ICDI domain. Based on these findings, we suggest that CaBP4 increases Cav1.4 channel availability by relieving the inhibitory effects of the ICDI domain on voltage-dependent Cav1.4 channel gating. We also functionally characterized two CaBP4 mutants that are associated with a congenital variant of human night blindness and other closely related nonstationary retinal diseases. Although both mutants interact with Cav1.4 channels, the functional effects of CaBP4 mutants are only partially preserved, leading to a reduction of Cav1.4 channel availability and loss of function. In conclusion, our study sheds new light on the functional interaction between CaBP4 and Cav1.4. Moreover, it provides insights into the mechanism by which CaBP4 mutants lead to loss of Cav1.4 function and to retinal disease.

Indexed as

Amino Acid MotifsAnimalsCalcium-Binding ProteinsCalcium ChannelsCalcium Channels, L-TypeHEK293 CellsHumansMiceMutationNerve Tissue ProteinsNight BlindnessProtein Structure, TertiaryRetinaRetinal DiseasesCABP4 protein, humanCabp4 protein, mouseCACNA1F protein, humanCacna1f protein, mouseCalcium-Binding ProteinsCalcium ChannelsCalcium Channels, L-TypeNerve Tissue Proteins

Identifiers

PMID22936811
PMCPMC3476298
OpenAlexW1978225079

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.