Evidence map›Paper›PMID 14685260›Full record

ArticleThe EMBO journal2004

Regulation of InsP3 receptor activity by neuronal Ca2+-binding proteins.

Nael Nadif Kasri, Anthony M Holmes, Geert Bultynck, Jan B Parys, Martin D Bootman, Katja Rietdorf, Ludwig Missiaen, Fraser McDonald, Humbert De Smedt, Stuart J Conway and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

78 citing papers in PubMed, 171 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Caldendrin Is a Repressor of PIEZO2 Channels and Touch Sensation in Mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  6. Article
  7. Dysregulated CaCells · 2022
    Review
  8. Review
  9. Article
  10. Calcium Sensors in Neuronal Function and Dysfunction.Cold Spring Harbor perspectives in biology · 2019
    Review
  11. Structure and Function of IPCold Spring Harbor perspectives in biology · 2019
    Review
  12. Review
  13. Review
  14. Article
  15. NCS-1 is a regulator of calcium signaling in health and disease.Biochimica et biophysica acta. Molecular cell research · 2018
    Review
  16. Article
  17. IPCellular and molecular life sciences : CMLS · 2017
    Review
  18. Article
  19. Article
  20. Role of calcium channels in bipolar disorder.Current psychopharmacology · 2017
    Article

18 more citing papers are in PubMed but not listed here.

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

13 authors at 4 institutions in 2 countries.

Nael Nadif KasriLaboratorium voor Fysiologie, KU Leuven, Campus Gasthuisberg O/N, Leuven, Belgium.
Anthony M Holmes
Geert Bultynck
Jan B Parys
Martin D Bootman
Katja Rietdorf
Ludwig Missiaen
Fraser McDonald
Humbert De Smedt
Stuart J Conway
Andrew B Holmes
Michael J Berridge
H Llewelyn Roderick
Babraham Institute · GBKU Leuven · BEUniversity of Cambridge · GBKing's College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inositol 1,4,5-trisphosphate receptors (InsP(3)Rs) were recently demonstrated to be activated independently of InsP(3) by a family of calmodulin (CaM)-like neuronal Ca(2+)-binding proteins (CaBPs). We investigated the interaction of both naturally occurring long and short CaBP1 isoforms with InsP(3)Rs, and their functional effects on InsP(3)R-evoked Ca(2+) signals. Using several experimental paradigms, including transient expression in COS cells, acute injection of recombinant protein into Xenopus oocytes and (45)Ca(2+) flux from permeabilised COS cells, we demonstrated that CaBPs decrease the sensitivity of InsP(3)-induced Ca(2+) release (IICR). In addition, we found a Ca(2+)-independent interaction between CaBP1 and the NH(2)-terminal 159 amino acids of the type 1 InsP(3)R. This interaction resulted in decreased InsP(3) binding to the receptor reminiscent of that observed for CaM. Unlike CaM, however, CaBPs do not inhibit ryanodine receptors, have a higher affinity for InsP(3)Rs and more potently inhibited IICR. We also show that phosphorylation of CaBP1 at a casein kinase 2 consensus site regulates its inhibition of IICR. Our data suggest that CaBPs are endogenous regulators of InsP(3)Rs tuning the sensitivity of cells to InsP(3).

Indexed as

Amino Acid SequenceAnimalsBinding SitesCalcium-Binding ProteinsCalcium ChannelsCalcium SignalingChlorocebus aethiopsCOS CellsInositol 1,4,5-TrisphosphateInositol 1,4,5-Trisphosphate ReceptorsMolecular Sequence DataNeuronsOocytesPhosphorylationReceptors, Cytoplasmic and NuclearXenopus laevisCalcium-Binding ProteinsCalcium ChannelsInositol 1,4,5-TrisphosphateInositol 1,4,5-Trisphosphate ReceptorsReceptors, Cytoplasmic and Nuclear

Identifiers

PMID14685260
PMCPMC1271747
OpenAlexW2078842725

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.