Evidence map›Paper›PMID 12829484›Full record

ArticleBiophysical journal2003

Functional and biochemical analysis of the type 1 inositol (1,4,5)-trisphosphate receptor calcium sensor.

Huiping Tu, Elena Nosyreva, Tomoya Miyakawa, Zhengnan Wang, Akiko Mizushima, Masamitsu Iino, Ilya Bezprozvanny

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

28 citing papers in PubMed, 58 citations in OpenAlex.

  1. Understanding IPCell calcium · 2023
    Review
  2. Functional determination of calcium-binding sites required for the activation of inositol 1,4,5-trisphosphate receptors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  3. The acidocalcisome inositol-1,4,5-trisphosphate receptor ofThe Journal of biological chemistry · 2019
    Article
  4. IPCellular and molecular life sciences : CMLS · 2017
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Mechanistic basis of bell-shaped dependence of inositol 1,4,5-trisphosphate receptor gating on cytosolic calcium.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  15. IP(3) receptors: toward understanding their activation.Cold Spring Harbor perspectives in biology · 2010
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
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

7 authors at 2 institutions in 2 countries.

Huiping TuDepartment of Physiology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390-9040, USA.
Elena Nosyreva
Tomoya Miyakawa
Zhengnan Wang
Akiko Mizushima
Masamitsu Iino
Ilya Bezprozvanny
The University of Texas Southwestern Medical Center · USThe University of Tokyo · JP

Funding

STRUCTURE/FUNCTION OF INOSITOL TRISPHOSPHATE RECEPTORR01NS038082 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI BEZPROZVANNY, ILYA B · 1999 to 2009
$2.6M
NINDS NIH HHS R01 NS038082NINDS NIH HHS R01 NS38082
6 · The paper itself

Abstract

Modulation of the type 1 inositol (1,4,5)-trisphosphate receptors (InsP(3)R1) by cytosolic calcium (Ca(2+)) plays an essential role in their signaling function, but structural determinants and mechanisms responsible for the InsP(3)R1 regulation by Ca(2+) are poorly understood. Using DT40 cell expression system and Ca(2+) imaging assay, in our previous study we identified a critical role of E2100 residue in the InsP(3)R1 modulation by Ca(2+). By using intrinsic tryptophan fluorescence measurements in the present study we determined that the putative InsP(3)R1 Ca(2+)-sensor region (E1932-R2270) binds Ca(2+) with 0.16 micro M affinity. We further established that E2100D and E2100Q mutations decrease Ca(2+)-binding affinity of the putative InsP(3)R1 Ca(2+)-sensor region to 1 micro M. In planar lipid bilayer experiments with recombinant InsP(3)R1 expressed in Spodoptera frugiperda cells we discovered that E2100D and E2100Q mutations shifted the peak of the InsP(3)R1 bell-shaped Ca(2+) dependence from 0.2 micro M to 1.5 micro M Ca(2+). In agreement with the biochemical data, we found that the apparent affinities of Ca(2+) activating and inhibitory sites of the InsP(3)R1 were 0.2 micro M for the wild-type channels and 1-2 micro M Ca(2+) for the E2100D and E2100Q mutants. The results obtained in our study support the hypothesis that E2100 residue forms a part of the InsP(3)R1 Ca(2+) sensor.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCalciumCalcium ChannelsCalcium SignalingCells, CulturedInositol 1,4,5-Trisphosphate ReceptorsIon Channel GatingMembrane PotentialsMolecular Sequence DataMutationProtein BindingProtein ConformationProtein Structure, TertiaryReceptors, Cytoplasmic and NuclearCalciumCalcium ChannelsInositol 1,4,5-Trisphosphate ReceptorsReceptors, Cytoplasmic and NuclearRecombinant Proteins

Identifiers

PMID12829484
PMCPMC1303085
OpenAlexW2095909835

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.