Evidence map›Paper›PMID 25766323›Full record

ArticleCell death & disease2015

BAG3 regulates formation of the SNARE complex and insulin secretion.

V Iorio, M Festa, A Rosati, M Hahne, C Tiberti, M Capunzo, V De Laurenzi, M C Turco

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

10 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Collagen IV-β1-Integrin Influences INS-1 Cell Insulin SecretionFrontiers in cell and developmental biology · 2022
    Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. 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 3 institutions in 2 countries.

V IorioDepartment of Pharmacy, University of Salerno, via Giovanni Paolo II, 132, Fisciano, SA, Italy.ORCID 0000000178264725
M Festa1] Department of Pharmacy, University of Salerno, via Giovanni Paolo II, 132, Fisciano, SA, Italy [2] BIOUNIVERSA S.r.l., University of Salerno, via Giovanni Paolo II, 132, Fisciano, SA, Italy.
A Rosati1] Department of Pharmacy, University of Salerno, via Giovanni Paolo II, 132, Fisciano, SA, Italy [2] BIOUNIVERSA S.r.l., University of Salerno, via Giovanni Paolo II, 132, Fisciano, SA, Italy.
M HahneInstitut de Génétique Moléculaire de Montpellier, CNRS UMR5535, Montpellier, France.
C TibertiDepartment of Clinical Sciences, University of Rome Sapienza, Rome, Italy.
M CapunzoDepartment of Medicine and Surgery, University of Salerno, Via S. Allende, Baronissi, SA, Italy.
V De Laurenzi1] BIOUNIVERSA S.r.l., University of Salerno, via Giovanni Paolo II, 132, Fisciano, SA, Italy [2] Department of Experimental and Clinical Sciences, University G. D'Annunzio and Fondazione G. D'Annunzio, Ce.S.I., Chieti, Italy.
M C Turco1] BIOUNIVERSA S.r.l., University of Salerno, via Giovanni Paolo II, 132, Fisciano, SA, Italy [2] Department of Medicine and Surgery, University of Salerno, Via S. Allende, Baronissi, SA, Italy.
University of Salerno · ITCentre National de la Recherche Scientifique · FRSapienza University of Rome · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Insulin release in response to glucose stimulation requires exocytosis of insulin-containing granules. Glucose stimulation of beta cells leads to focal adhesion kinase (FAK) phosphorylation, which acts on the Rho family proteins (Rho, Rac and Cdc42) that direct F-actin remodeling. This process requires docking and fusion of secretory vesicles to the release sites at the plasma membrane and is a complex mechanism that is mediated by SNAREs. This transiently disrupts the F-actin barrier and allows the redistribution of the insulin-containing granules to more peripheral regions of the β cell, hence facilitating insulin secretion. In this manuscript, we show for the first time that BAG3 plays an important role in this process. We show that BAG3 downregulation results in increased insulin secretion in response to glucose stimulation and in disruption of the F-actin network. Moreover, we show that BAG3 binds to SNAP-25 and syntaxin-1, two components of the t-SNARE complex preventing the interaction between SNAP-25 and syntaxin-1. Upon glucose stimulation BAG3 is phosphorylated by FAK and dissociates from SNAP-25 allowing the formation of the SNARE complex, destabilization of the F-actin network and insulin release.

Indexed as

ActinsAdaptor Proteins, Signal TransducingAdultApoptosis Regulatory ProteinsFemaleFocal Adhesion Kinase 1Gene Expression RegulationGlucoseHumansInsulinInsulin-Secreting CellsInsulin SecretionMaleMiddle AgedPancreasPhosphorylationActinsAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsBAG3 protein, humanFocal Adhesion Kinase 1GlucoseInsulinPTK2 protein, humanSNAP25 protein, humanSNARE ProteinsSynaptosomal-Associated Protein 25Syntaxin 1

Identifiers

PMID25766323
PMCPMC4385931
OpenAlexW1979354965

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.