Evidence map›Paper›PMID 20886068›Full record

ArticlePloS one2010

β2-Syntrophin is a Cdk5 substrate that restrains the motility of insulin secretory granules.

Sandra Schubert, Klaus-Peter Knoch, Joke Ouwendijk, Shabaz Mohammed, Yury Bodrov, Melanie Jäger, Anke Altkrüger, Carolin Wegbrod, Marvin E Adams, Yong Kim and 4 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 44 citations in OpenAlex.

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  12. X-ray structure of the mature ectodomain of phogrin.Journal of structural and functional genomics · 2015
    Article
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  18. Syntrophin proteins as Santa Claus: role(s) in cell signal transduction.Cellular and molecular life sciences : CMLS · 2013
    Review
  19. Article
  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

14 authors at 6 institutions in 4 countries.

Sandra SchubertMolecular Diabetology, Paul Langerhans Institute Dresden, Uniklinikum Carl Gustav Carus at Dresden University of Technology, Dresden, Germany.
Klaus-Peter Knoch
Joke Ouwendijk
Shabaz Mohammed
Yury Bodrov
Melanie Jäger
Anke Altkrüger
Carolin Wegbrod
Marvin E Adams
Yong Kim
Stanley C Froehner
Ole N Jensen
Yannis Kalaidzidis
Michele Solimena
Paul Langerhans Institute Dresden · DEMax Planck Institute of Molecular Cell Biology and Genetics · DEUniversity of Southern Denmark · DKUniversity of Washington · USLomonosov Moscow State University · RURockefeller University · US

Funding

Regulation of Syntrophin FunctionR01NS033145 · NINDS · UNIVERSITY OF WASHINGTON · PI FROEHNER, STANLEY C · 1995 to 2013
$5.2M
NINDS NIH HHS NS33145NINDS NIH HHS R01 NS033145
6 · The paper itself

Abstract

The molecular basis for the interaction of insulin granules with the cortical cytoskeleton of pancreatic β-cells remains unknown. We have proposed that binding of the granule protein ICA512 to the PDZ domain of β2-syntrophin anchors granules to actin filaments and that the phosphorylation/dephosphorylation of β2-syntrophin regulates this association. Here we tested this hypothesis by analyzing INS-1 cells expressing GFP-β2-syntrophin through the combined use of biochemical approaches, imaging studies by confocal and total internal reflection fluorescence microscopy as well as electron microscopy. Our results support the notion that β2-syntrophin restrains the mobility of cortical granules in insulinoma INS-1 cells, thereby reducing insulin secretion and increasing insulin stores in resting cells, while increasing insulin release upon stimulation. Using mass spectrometry, in vitro phosphorylation assays and β2-syntrophin phosphomutants we found that phosphorylation of β2-syntrophin on S75 near the PDZ domain decreases its binding to ICA512 and correlates with increased granule motility, while phosphorylation of S90 has opposite effects. We further show that Cdk5, which regulates insulin secretion, phosphorylates S75. These findings provide mechanistic insight into how stimulation displaces insulin granules from cortical actin, thus promoting their motility and exocytosis.

Indexed as

AnimalsBiological TransportCell Line, TumorCyclin-Dependent Kinase 5Dystrophin-Associated ProteinsFemaleInsulinInsulin-Secreting CellsInsulin SecretionIslets of LangerhansPhosphorylationProtein Structure, TertiaryRatsRats, WistarSecretory VesiclesCyclin-Dependent Kinase 5Dystrophin-Associated ProteinsInsulinsyntrophin

Identifiers

PMID20886068
PMCPMC2944849
OpenAlexW2019717932

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.