Evidence map›Paper›PMID 19694801›Full record

ArticleThe FEBS journal2009

A single EF-hand isolated from STIM1 forms dimer in the absence and presence of Ca2+.

Yun Huang, Yubin Zhou, Hing-Cheung Wong, Yanyi Chen, Yan Chen, Siming Wang, Adriana Castiblanco, Aimin Liu, Jenny J Yang

Open access · greenAbstract read
In one paragraph

Article in The FEBS journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.0field-weighted citation impact, top 29% 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

20 citing papers in PubMed, 45 citations in OpenAlex.

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  17. Store-Operated Calcium Channels.Physiological reviews · 2015
    Review
  18. Review
  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

9 authors at 1 institution in 1 country.

Yun HuangDepartment of Chemistry, Center for Drug Design and Advanced Biotechnology, Georgia State University, Atlanta, GA 30303, USA.
Yubin Zhou
Hing-Cheung Wong
Yanyi Chen
Yan Chen
Siming Wang
Adriana Castiblanco
Aimin Liu
Jenny J Yang
Georgia State University · US

Funding

Designing Magnetic Resonance Protein-based Contrast Agents with High RelaxivityR01EB007268 · NIBIB · GEORGIA STATE UNIVERSITY · PI YANG, JENNY J. · 2007 to 2015
$3.1M
NIBIB NIH HHS EB007268NIBIB NIH HHS R01 EB007268
6 · The paper itself

Abstract

Stromal interaction molecule 1 (STIM1) is responsible for activating the Ca(2+) release-activated Ca(2+) (CRAC) channel by first sensing the changes in Ca(2+) concentration in the endoplasmic reticulum ([Ca(2+)](ER)) via its luminal canonical EF-hand motif and subsequently oligomerizing to interact with the CRAC channel pore-forming subunit Orai1. In this work, we applied a grafting approach to obtain the intrinsic metal-binding affinity of the isolated EF-hand of STIM1, and further investigated its oligomeric state using pulsed-field gradient NMR and size-exclusion chromatography. The canonical EF-hand bound Ca(2+) with a dissociation constant at a level comparable with [Ca(2+)](ER) (512 +/- 15 microm). The binding of Ca(2+) resulted in a more compact conformation of the engineered protein. Our results also showed that D to A mutations at Ca(2+)-coordinating loop positions 1 and 3 of the EF-hand from STIM1 led to a 15-fold decrease in the metal-binding affinity, which explains why this mutant was insensitive to changes in Ca(2+) concentration in the endoplasmic reticulum ([Ca(2+)](ER)) and resulted in constitutive punctae formation and Ca(2+) influx. In addition, the grafted single EF-hand motif formed a dimer regardless of the presence of Ca(2+), which conforms to the EF-hand paring paradigm. These data indicate that the STIM1 canonical EF-hand motif tends to dimerize for functionality in solution and is responsible for sensing changes in [Ca(2+)](ER).

Indexed as

Amino Acid SequenceAmino Acid SubstitutionCalciumCircular DichroismCloning, MolecularDimerizationHelix-Loop-Helix MotifsHumansIn Vitro TechniquesLanthanoid Series ElementsMembrane ProteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNeoplasm ProteinsNuclear Magnetic Resonance, BiomolecularCalciumLanthanoid Series ElementsMembrane ProteinsNeoplasm ProteinsRecombinant Fusion ProteinsSTIM1 protein, humanStromal Interaction Molecule 1

Identifiers

PMID19694801
PMCPMC2866080
OpenAlexW1593637618

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Registered trials

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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.