Evidence map›Paper›PMID 19622606›Full record

ArticleThe Journal of physiology2009

The molecular architecture of the arachidonate-regulated Ca2+-selective ARC channel is a pentameric assembly of Orai1 and Orai3 subunits.

Olivier Mignen, Jill L Thompson, Trevor J Shuttleworth

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

65 citing papers in PubMed, 118 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. p38 MAPK activation and STIM1-Orai3 association mediate TRPC6 externalization.American journal of physiology. Cell physiology · 2023
    Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Cellular and Molecular Mechanisms of Fat Taste Perception.Handbook of experimental pharmacology · 2022
    Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Role of Orai3 in the Pathophysiology of Cancer.International journal of molecular sciences · 2021
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

5 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

3 authors at 2 institutions in 2 countries.

Olivier MignenDepartment of Pharmacology and Physiology, University of Rochester Medical Center, Rochester, NY 14642, USA. trevor_shuttleworth@urmc.rochester.edu
Jill L Thompson
Trevor J Shuttleworth
University of Rochester Medical Center · USCentre National de la Recherche Scientifique · FR

Funding

RECEPTOR-REGULATED CALCIUM ENTRY IN EXOCRINE SECRETIONR01GM040457 · NIGMS · UNIVERSITY OF ROCHESTER · PI SHUTTLEWORTH, TREVOR J. · 1988 to 2017
$5.6M
NIGMS NIH HHS GM040457NIGMS NIH HHS R01 GM040457
6 · The paper itself

Abstract

The activation of Ca(2+) entry is a critical component of agonist-induced cytosolic Ca(2+) signals in non-excitable cells. Although a variety of different channels may be involved in such entry, the recent identification of the STIM and Orai proteins has focused attention on the channels in which these proteins play a key role. To date, two distinct highly Ca(2+)-selective STIM1-regulated and Orai-based channels have been identified - the store-operated CRAC channels and the store-independent arachidonic acid activated ARC channels. In contrast to the CRAC channels, where the channel pore is composed of only Orai1 subunits, both Orai1 and Orai3 subunits are essential components of the ARC channel pore. Using an approach involving the co-expression of a dominant-negative Orai1 monomer along with different preassembled concatenated Orai1 constructs, we recently demonstrated that the functional CRAC channel pore is formed by a homotetrameric assembly of Orai1 subunits. Here, we use a similar approach to demonstrate that the functional ARC channel pore is a heteropentameric assembly of three Orai1 subunits and two Orai3 subunits. Expression of concatenated pentameric constructs with this stoichiometry results in the appearance of large currents that display all the key biophysical and pharmacological features of the endogenous ARC channels. They also replicate the essential regulatory characteristics of native ARC channels including specific activation by low concentrations of arachidonic acid, complete independence of store depletion, and an absolute requirement for the pool of STIM1 that constitutively resides in the plasma membrane.

Indexed as

Arachidonic AcidCalciumCalcium ChannelsCell LineDimerizationHumansIon Channel GatingKidneyMembrane PotentialsORAI1 ProteinProtein SubunitsStructure-Activity RelationshipArachidonic AcidCalciumCalcium ChannelsORAI1 ProteinORAI1 protein, humanOrai3 protein, humanProtein Subunits

Identifiers

PMID19622606
PMCPMC2754359
OpenAlexW1588658790

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.