Evidence map›Paper›PMID 22000518›Full record

ArticleStructure (London, England : 1993)2011

Structural basis of the Ca2+ inhibitory mechanism of Drosophila Na+/Ca2+ exchanger CALX and its modification by alternative splicing.

Mousheng Wu, Shuilong Tong, Jennifer Gonzalez, Vasanthi Jayaraman, John L Spudich, Lei Zheng

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. CALX-CBD1 CaBiophysical journal · 2020
    Article
  5. Article
  6. TheFrontiers in cellular neuroscience · 2018
    Article
  7. Spontaneous CaFrontiers in molecular neuroscience · 2017
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Ca2+ regulation of ion transport in the Na+/Ca2+ exchanger.The Journal of biological chemistry · 2012
    Review
  13. Article
  14. 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

6 authors.

Mousheng WuCenter for Membrane Biology, Department of Biochemistry and Molecular Biology, The University of Texas Houston Medical School, Houston, TX 77030, USA.
Shuilong Tong
Jennifer Gonzalez
Vasanthi Jayaraman
John L Spudich
Lei Zheng

Funding

Structure/Function of Microbial Sensory RhodopsinsR37GM027750 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI SPUDICH, JOHN LEE · 2003 to 2012
$6.0M
Ca2+ Transport Mechanism of CaCA Protein FamilyR01GM097290 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI ZHENG, LEI · 2011 to 2015
$1.7M
Vibrational Spectroscopic Investigations of Glutamate ReceptorR01GM073102 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI JAYARAMAN, VASANTHI · 2006 to 2010
$1.2M
Conformational Changes In Glutamate ReceptorF31GM082023 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MCGEHEE, JENNIFER · 2007 to 2009
$71k
NIGMS NIH HHS F31 GM082023NIGMS NIH HHS GM082023-01NIGMS NIH HHS R01 GM073102NIGMS NIH HHS R01GM073102NIGMS NIH HHS R01 GM097290NIGMS NIH HHS R01GM097290NIGMS NIH HHS R37 GM027750NIGMS NIH HHS R37GM27750
6 · The paper itself

Abstract

The Na(+)/Ca(2+) exchanger CALX promotes Ca(2+) efflux in Drosophila sensory neuronal cells to facilitate light-mediated Ca(2+) homeostasis. CALX activity is negatively regulated by specific Ca(2+) interaction within its two intracellular Ca(2+) regulatory domains CBD1 and CBD2, yet how the Ca(2+) binding is converted to molecular motion to operate the exchanger is unknown. Here, we report crystal structures of the entire Ca(2+) regulatory domain CBD12 from two alternative splicing isoforms, CALX 1.1 and 1.2, exhibiting distinct regulatory Ca(2+) dependency. The structures show an open V-shaped conformation with four Ca(2+) ions bound on the CBD domain interface, confirmed by LRET analysis. The structures together with Ca(2+)-binding analysis support that the Ca(2+) inhibition of CALX is achieved by interdomain conformational changes induced by Ca(2+) binding at CBD1. The conformational difference between the two isoforms also indicates that alternative splicing adjusts the interdomain orientation angle to modify the Ca(2+) regulatory property of the exchangers.

Indexed as

Alternative SplicingAmino Acid SequenceAnimalsAntiportersBinding SitesCalciumChromatography, GelCloning, MolecularDrosophilaDrosophila ProteinsEscherichia coliFluorescenceModels, MolecularMolecular Sequence DataProtein BindingProtein ConformationAntiportersCalciumCalx protein, DrosophilaDrosophila ProteinsProtein IsoformsSodium-Calcium Exchanger

Identifiers

PMID22000518
PMCPMC3197212

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.