Evidence map›Paper›PMID 25344253›Full record

ArticleJournal of cell science2014

Synaptotagmin-7 links fusion-activated Ca²⁺ entry and fusion pore dilation.

Kathrin Neuland, Neeti Sharma, Manfred Frick

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2014. 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
1.2field-weighted citation impact, top 24% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. P2 Purinergic Signaling in the Distal Lung in Health and Disease.International journal of molecular sciences · 2020
    Review
  4. Article
  5. Inflammation-induced upregulation of P2XAmerican journal of physiology. Lung cellular and molecular physiology · 2019
    Article
  6. Review
  7. ATP is stored in lamellar bodies to activate vesicular P2XThe Journal of general physiology · 2018
    Article
  8. Article
  9. Review
  10. Plexin C1 deficiency permits synaptotagmin 7-mediated macrophage migration and enhances mammalian lung fibrosis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Article
  11. Article
  12. Review
  13. Article
  14. Vesicular control of fusion pore expansion.Communicative & integrative biology
    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

3 authors at 1 institution in 1 country.

Kathrin NeulandInstitute of General Physiology, University of Ulm, Albert-Einstein Allee 11, 89081 Ulm, Germany.
Neeti SharmaInstitute of General Physiology, University of Ulm, Albert-Einstein Allee 11, 89081 Ulm, Germany.
Manfred FrickInstitute of General Physiology, University of Ulm, Albert-Einstein Allee 11, 89081 Ulm, Germany manfred.frick@uni-ulm.de.
Universität Ulm · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ca(2+)-dependent regulation of fusion pore dilation and closure is a key mechanism determining the output of cellular secretion. We have recently described 'fusion-activated' Ca(2+) entry (FACE) following exocytosis of lamellar bodies in alveolar type II cells. FACE regulates fusion pore expansion and facilitates secretion. However, the mechanisms linking this locally restricted Ca(2+) signal and fusion pore expansion were still elusive. Here, we demonstrate that synaptotagmin-7 (Syt7) is expressed on lamellar bodies and links FACE and fusion pore dilation. We directly assessed dynamic changes in fusion pore diameters by analysing diffusion of fluorophores across fusion pores. Expressing wild-type Syt7 or a mutant Syt7 with impaired Ca(2+)-binding to the C2 domains revealed that binding of Ca(2+) to the C2A domain facilitates FACE-induced pore dilation, probably by inhibiting translocation of complexin-2 to fused vesicles. However, the C2A domain hampered Ca(2+)-dependent exocytosis of lamellar bodies. These findings support the hypothesis that Syt7 modulates fusion pore expansion in large secretory organelles and extend our picture that lamellar bodies contain the necessary molecular inventory to facilitate secretion during the exocytic post-fusion phase. Moreover, regulating Syt7 levels on lamellar bodies appears to be essential in order that exocytosis is not impeded during the pre-fusion phase.

Indexed as

Membrane FusionAdaptor Proteins, Vesicular TransportAlveolar Epithelial CellsAnimalsCalciumCell MembraneCell SeparationExocytosisGreen Fluorescent ProteinsNerve Tissue ProteinsProtein BindingProtein Structure, TertiaryRats, Sprague-DawleySurface-Active AgentsSynaptotagminsAdaptor Proteins, Vesicular TransportCalciumcomplexin IIGreen Fluorescent ProteinsNerve Tissue ProteinsSurface-Active AgentsSynaptotagminsCalciumExocytosisFACEFusion poreLamellar bodySynaptotagmin

Identifiers

PMID25344253
PMCPMC4265738
OpenAlexW2031988397

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.