Evidence map›Paper›PMID 16274363›Full record

ArticleThe Biochemical journal2006

Agonist-evoked inositol trisphosphate receptor (IP3R) clustering is not dependent on changes in the structure of the endoplasmic reticulum.

Mark Chalmers, Michael J Schell, Peter Thorn

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

24 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Spatial-temporal patterning of CaSeminars in cell & developmental biology · 2019
    Review
  5. Structure and Function of IPCold Spring Harbor perspectives in biology · 2019
    Review
  6. All three IPScience signaling · 2018
    Article
  7. CaNature communications · 2017
    Article
  8. IPCellular and molecular life sciences : CMLS · 2017
    Review
  9. Endogenous signalling pathways and caged IPJournal of cell science · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

3 authors at 1 institution in 1 country.

Mark ChalmersDepartment of Pharmacology, University of Cambridge, Cambridge, CB2 1PD, UK.
Michael J Schell
Peter Thorn
University of Cambridge · GB

Funding

Medical Research Council G0400669
6 · The paper itself

Abstract

The size and number of IP3R (inositol 1,4,5-trisphosphate receptor) clusters located on the surface of the ER (endoplasmic reticulum) is hypothesized to regulate the propagation of Ca2+ waves in cells, but the mechanisms by which the receptors cluster are not understood. Using immunocytochemistry, live-cell imaging and heterologous expression of ER membrane proteins we have investigated IP3R clustering in the basophilic cell line RBL-2H3 following the activation of native cell-surface antigen receptors. IP3R clusters are present in resting cells, and upon receptor stimulation, form larger aggregates. Cluster formation and maintenance required the presence of extracellular Ca2+ in both resting and stimulated cells. Using transfection with a marker of the ER, we found that the ER itself also showed structural changes, leading to an increased number of 'hotspots', following antigen stimulation. Surprisingly, however, when we compared the ER hotspots and IP3R clusters, we found them to be distinct. Imaging of YFP (yellow fluorescent protein)-IP3R transfected in to living cells confirmed that IP3R clustering increased upon stimulation. Photobleaching experiments showed that the IP3R occupied a single contiguous ER compartment both before and after stimulation, suggesting a dynamic exchange of IP3R molecules between the clusters and the surrounding ER membrane. It also showed a decrease in the mobile fraction after cell activation, consistent with receptor anchoring within clusters. We conclude that IP3R clustering in RBL-2H3 cells is not simply a reflection of bulk-changes in ER structure, but rather is due to the receptor undergoing homotypic or heterotypic protein-protein interactions in response to agonist stimulation.

Indexed as

Calcium ChannelsCalcium SignalingCell LineDinitrophenolsEndoplasmic ReticulumInositol 1,4,5-Trisphosphate ReceptorsProtein BindingProtein TransportReceptors, Cytoplasmic and NuclearSerum Albumin, BovineCalcium ChannelsDinitrophenolsdinitrophenyl-bovine serum albuminInositol 1,4,5-Trisphosphate ReceptorsReceptors, Cytoplasmic and NuclearSerum Albumin, Bovine

Identifiers

PMID16274363
PMCPMC1386003
OpenAlexW2132533146

What Socratic 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 Socratic graph.