Evidence map›Paper›PMID 21887368›Full record

ArticlePloS one2011

Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity.

Vikas V Dukhande, Devin M Rogers, Carlos Romá-Mateo, Jordi Donderis, Alberto Marina, Adam O Taylor, Pascual Sanz, Matthew S Gentry

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  6. Review
  7. Article
  8. Unique carbohydrate binding platforms employed by the glucan phosphatases.Cellular and molecular life sciences : CMLS · 2016
    Review
  9. Assessing the Biological Activity of the Glucan Phosphatase Laforin.Methods in molecular biology (Clifton, N.J.) · 2016
    Article
  10. Dimeric quaternary structure of human laforin.The Journal of biological chemistry · 2015
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. 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

8 authors at 2 institutions in 2 countries.

Vikas V DukhandeDepartment of Molecular and Cellular Biochemistry and Center for Structural Biology, College of Medicine, University of Kentucky, Lexington, Kentucky, United States of America.
Devin M Rogers
Carlos Romá-Mateo
Jordi Donderis
Alberto Marina
Adam O Taylor
Pascual Sanz
Matthew S Gentry
Instituto de Biomedicina de Valencia · ESUniversity of Kentucky · US

Funding

Regulation, Signaling, and Dynamics of Glucan PhosphatasesR01NS070899 · NINDS · UNIVERSITY OF KENTUCKY · PI GENTRY, MATTHEW S. · 2010 to 2019
$3.6M
Novel Model Systems Link Floridean Starch Metabolism to Lafora DiseaseR00NS061803 · NINDS · UNIVERSITY OF KENTUCKY · PI GENTRY, MATTHEW S. · 2008 to 2010
$696k
NCRR NIH HHS P20RR0202171NINDS NIH HHS R00 NS061803NINDS NIH HHS R00NS061803NINDS NIH HHS R01 NS070899NINDS NIH HHS R01NS070899
6 · The paper itself

Abstract

Lafora Disease (LD) is a fatal neurodegenerative epileptic disorder that presents as a neurological deterioration with the accumulation of insoluble, intracellular, hyperphosphorylated carbohydrates called Lafora bodies (LBs). LD is caused by mutations in either the gene encoding laforin or malin. Laforin contains a dual specificity phosphatase domain and a carbohydrate-binding module, and is a member of the recently described family of glucan phosphatases. In the current study, we investigated the functional and physiological relevance of laforin dimerization. We purified recombinant human laforin and subjected the monomer and dimer fractions to denaturing gel electrophoresis, mass spectrometry, phosphatase assays, protein-protein interaction assays, and glucan binding assays. Our results demonstrate that laforin prevalently exists as a monomer with a small dimer fraction both in vitro and in vivo. Of mechanistic importance, laforin monomer and dimer possess equal phosphatase activity, and they both associate with malin and bind glucans to a similar extent. However, we found differences between the two states' ability to interact simultaneously with malin and carbohydrates. Furthermore, we tested other members of the glucan phosphatase family. Cumulatively, our data suggest that laforin monomer is the dominant form of the protein and that it contains phosphatase activity.

Indexed as

CarbohydratesCarrier ProteinsDual-Specificity PhosphatasesHumansLafora DiseaseProtein BindingProtein MultimerizationProtein Tyrosine Phosphatases, Non-ReceptorUbiquitin-Protein LigasesCarbohydratesCarrier ProteinsDual-Specificity PhosphatasesEPM2A protein, humanNHLRC1 protein, humanProtein Tyrosine Phosphatases, Non-ReceptorUbiquitin-Protein Ligases

Identifiers

PMID21887368
PMCPMC3162602
OpenAlexW2061673750

What OpenQuestion holds

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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.