Evidence map›Paper›PMID 15635093›Full record

ArticleMolecular biology of the cell2005

EBAG9 adds a new layer of control on large dense-core vesicle exocytosis via interaction with Snapin.

Constantin Rüder, Tatiana Reimer, Ignacio Delgado-Martinez, Ricardo Hermosilla, Arne Engelsberg, Ralf Nehring, Bernd Dörken, Armin Rehm

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 16% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.

  1. Pooled it
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  17. EBAG9 tempers lymphocyte killing activity.The Journal of clinical investigation · 2009
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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 1 country.

Constantin RüderDepartment of Hematology, Oncology, and Tumor Immunology, Max-Delbrück-Center for Molecular Medicine, 13125 Berlin, Germany.
Tatiana Reimer
Ignacio Delgado-Martinez
Ricardo Hermosilla
Arne Engelsberg
Ralf Nehring
Bernd Dörken
Armin Rehm
Max Delbrück Center · DEMax Planck Institute for Biophysical Chemistry · DEFreie Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regulated exocytosis is subject to several modulatory steps that include phosphorylation events and transient protein-protein interactions. The estrogen receptor-binding fragment-associated gene9 (EBAG9) gene product was recently identified as a modulator of tumor-associated O-linked glycan expression in nonneuronal cells; however, this molecule is expressed physiologically in essentially all mammalian tissues. Particular interest has developed toward this molecule because in some human tumor entities high expression levels correlated with clinical prognosis. To gain insight into the cellular function of EBAG9, we scored for interaction partners by using the yeast two-hybrid system. Here, we demonstrate that EBAG9 interacts with Snapin, which is likely to be a modulator of Synaptotagmin-associated regulated exocytosis. Strengthening of this interaction inhibited regulated secretion of neuropeptide Y from PC12 cells, whereas evoked neurotransmitter release from hippocampal neurons remained unaltered. Mechanistically, EBAG9 decreased phosphorylation of Snapin; subsequently, association of Snapin with synaptosome-associated protein of 25 kDa (SNAP25) and SNAP23 was diminished. We suggest that the occurrence of SNAP23, Snapin, and EBAG9 also in nonneuronal cells might extend the modulatory role of EBAG9 to a broad range of secretory cells. The conjunction between EBAG9 and Snapin adds an additional layer of control on exocytosis processes; in addition, mechanistic evidence is provided that inhibition of phosphorylation has a regulatory function in exocytosis.

Indexed as

ExocytosisAdenoviridaealpha 1-AntitrypsinAnimalsAntigens, NeoplasmBrainCarrier ProteinsCell LineCell MembraneDNA, ComplementaryElectrophoresis, Polyacrylamide GelElectrophysiologyGene LibraryGlutathione TransferaseHippocampusHumansalpha 1-AntitrypsinAntigens, NeoplasmCarrier ProteinsDNA, ComplementaryEBAG9 protein, humanEBAG9 protein, ratGlutathione TransferaseNeuropeptide YNeurotransmitter AgentsPolysaccharidesRecombinant Fusion ProteinsSNAPIN protein, humanSnapin protein, ratVesicular Transport Proteins

Identifiers

PMID15635093
PMCPMC551489
OpenAlexW2117397810

What OpenQuestion holds

Textmetadata
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.