Evidence map›Paper›PMID 21876165›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Mechanistic basis of bell-shaped dependence of inositol 1,4,5-trisphosphate receptor gating on cytosolic calcium.

Tadashi Shinohara, Takayuki Michikawa, Masahiro Enomoto, Jun-Ichi Goto, Miwako Iwai, Toru Matsu-ura, Haruka Yamazaki, Akitoshi Miyamoto, Akio Suzuki, Katsuhiko Mikoshiba

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Dual-FRET imaging of IPScientific reports · 2019
    Article
  5. Article
  6. Coupling all-atom molecular dynamics simulations of ions in water with Brownian dynamics.Proceedings. Mathematical, physical, and engineering sciences · 2016
    Article
  7. Review
  8. Aberrant calcium signaling by transglutaminase-mediated posttranslational modification of inositol 1,4,5-trisphosphate receptors.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  9. Article
  10. Article
  11. Article
  12. 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

10 authors at 2 institutions in 1 country.

Tadashi ShinoharaLaboratory for Developmental Neurobiology, RIKEN Brain Science Institute, Wako, Saitama 351-0198, Japan.
Takayuki Michikawa
Masahiro Enomoto
Jun-Ichi Goto
Miwako Iwai
Toru Matsu-ura
Haruka Yamazaki
Akitoshi Miyamoto
Akio Suzuki
Katsuhiko Mikoshiba
RIKEN Center for Brain Science · JPJapan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The inositol 1,4,5-trisphosphate (IP(3)) receptor (IP(3)R) is an intracellular Ca(2+) release channel, and its opening is controlled by IP(3) and Ca(2+). A single IP(3) binding site and multiple Ca(2+) binding sites exist on single subunits, but the precise nature of the interplay between these two ligands in regulating biphasic dependence of channel activity on cytosolic Ca(2+) is unknown. In this study, we visualized conformational changes in IP(3)R evoked by various concentrations of ligands by using the FRET between two fluorescent proteins fused to the N terminus of individual subunits. IP(3) and Ca(2+) have opposite effects on the FRET signal change, but the combined effect of these ligands is not a simple summative response. The bell-shaped Ca(2+) dependence of FRET efficiency was observed after the subtraction of the component corresponding to the FRET change evoked by Ca(2+) alone from the FRET changes evoked by both ligands together. A mutant IP(3)R containing a single amino acid substitution at K508, which is critical for IP(3) binding, did not exhibit this bell-shaped Ca(2+) dependence of the subtracted FRET efficiency. Mutation at E2100, which is known as a Ca(2+) sensor, resulted in ∼10-fold reduction in the Ca(2+) dependence of the subtracted signal. These results suggest that the subtracted FRET signal reflects IP(3)R activity. We propose a five-state model, which implements a dual-ligand competition response without complex allosteric regulation of Ca(2+) binding affinity, as the mechanism underlying the IP(3)-dependent regulation of the bell-shaped relationship between the IP(3)R activity and cytosolic Ca(2+).

Indexed as

Ion Channel GatingAnimalsBacterial ProteinsCalciumCytosolFluorescence Resonance Energy TransferGreen Fluorescent ProteinsHeLa CellsHumansInositol 1,4,5-Trisphosphate ReceptorsLigandsLuminescent ProteinsMiceModels, BiologicalRecombinant Fusion ProteinsBacterial ProteinsCalciumenhanced cyan fluorescent proteinGreen Fluorescent ProteinsInositol 1,4,5-Trisphosphate ReceptorsLigandsLuminescent ProteinsRecombinant Fusion Proteinsyellow fluorescent protein, Bacteria

Identifiers

PMID21876165
PMCPMC3174635
OpenAlexW2037421877

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.