Evidence map›Paper›PMID 21288721›Full record

ReviewTrends in cell biology2011

Evolutionary origins of STIM1 and STIM2 within ancient Ca2+ signaling systems.

Sean R Collins, Tobias Meyer

Abstract readReview
In one paragraph

Review in Trends in cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
–field-weighted citation impact
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

52 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Regulation of Yeast Cytokinesis by Calcium.Journal of fungi (Basel, Switzerland) · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Roles of Cholesterol and PtdIns(4,5)PAdvances in experimental medicine and biology · 2023
    Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. STIM calcium sensing and conformational change.The Journal of physiology · 2020
    Review
  19. Calmodulin-mediated events during the life cycle of the amoebozoan Dictyostelium discoideum.Biological reviews of the Cambridge Philosophical Society · 2020
    Review
  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

2 authors.

Sean R CollinsDepartment of Chemical and Systems Biology, Stanford University, 318 Campus Drive, Clark Building W2.1, Stanford, CA 94305-5174, USA.
Tobias Meyer

Funding

REGULATION OF CA++/CALMODULIN KINASE BY NEUROTRANSMITTERR01GM030179 · NIGMS · STANFORD UNIVERSITY · PI MEYER, TOBIAS · 1985 to 2018
$4.9M
Lipid Second Messenger and Small GTPase Signal Integration in NeuronsR01MH064801 · NIMH · STANFORD UNIVERSITY · PI MEYER, TOBIAS · 2001 to 2011
$3.2M
NIGMS NIH HHS R01 GM030179NIMH NIH HHS R01 MH064801
6 · The paper itself

Abstract

Human stromal interaction molecule (STIM) proteins are parts of elaborate eukaryotic Ca(2+) signaling systems that include numerous plasma membrane (PM), endoplasmic reticulum (ER), and mitochondrial Ca(2+) transporters, channels and regulators. STIM2 and STIM1 function as Ca(2+) sensors with different sensitivities for ER Ca(2+). They translocate to ER-PM junctions and open PM Orai Ca(2+) influx channels when receptor-mediated Ca(2+) release lowers ER Ca(2+) levels. The resulting increase in cytosolic Ca(2+) leads to the activation of numerous Ca(2+) effector proteins that in turn regulate differentiation, cell contraction, secretion and other cell functions. In this review, we use an evolutionary perspective to survey molecular activation mechanisms in the Ca(2+) signaling system, with a particular focus on regulatory motifs and functions of the two STIM proteins. We discuss the presence and absence of STIM genes in different species, the order of appearance of STIM versus Orai, and the evolutionary addition of new signaling domains to STIM proteins.

Indexed as

Calcium SignalingEvolution, MolecularAnimalsCell Adhesion MoleculesHomeostasisHumansMembrane ProteinsNeoplasm ProteinsStromal Interaction Molecule 1Stromal Interaction Molecule 2Cell Adhesion MoleculesMembrane ProteinsNeoplasm ProteinsSTIM1 protein, humanSTIM2 protein, humanStromal Interaction Molecule 1Stromal Interaction Molecule 2

Identifiers

PMID21288721
PMCPMC3175768

What OpenQuestion holds

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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.