Evidence map›Paper›PMID 7835334›Full record

ArticleThe EMBO journal1995

A role for soluble NSF attachment proteins (SNAPs) in regulated exocytosis in adrenal chromaffin cells.

A Morgan, R D Burgoyne

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 102 citations in OpenAlex.

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  9. Differential regulation of exocytosis by alpha- and beta-SNAPs.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002
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  10. SNARE proteins are highly enriched in lipid rafts in PC12 cells: implications for the spatial control of exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2001
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  12. The genome of fowlpox virus.Journal of virology · 2000
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  18. Membrane fusion protein synexin (annexin VII) as a Ca2+/GTP sensor in exocytotic secretion.Proceedings of the National Academy of Sciences of the United States of America · 1996
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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

2 authors at 1 institution in 1 country.

A MorganPhysiological Laboratory, University of Liverpool, UK.
R D Burgoyne
University of Liverpool · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Digitonin-permeabilized chromaffin cells secrete catecholamines by exocytosis in response to micromolar Ca2+ concentrations, but lose the ability to secrete in response to Ca2+ as the cells lose soluble proteins through the plasma membrane pores. Such secretory run-down can be retarded by cytosolic fractions, thus providing an assay for proteins potentially involved in the exocytotic process. We have used this assay to investigate the role of N-ethylmaleimide-sensitive fusion protein (NSF) and soluble NSF attachment proteins (SNAPs) in regulated exocytosis. Recombinant alpha- and gamma-SNAP stimulated Ca(2+)-dependent exocytosis, although recombinant NSF was ineffective, despite the fact that NSF and alpha-SNAP leak from the permeabilized cells with similar time courses. However, around one third of cellular NSF was found to be present in a non-cytosolic form and so it is possible that this is sufficient for exocytosis and that exogenous SNAPs stimulate the exocytotic mechanism by acting on the leakage-insensitive NSF. The stimulatory effect of alpha-SNAP displayed a biphasic dose-response curve and was maximal at 20 micrograms/ml. The effect of alpha-SNAP was Ca(2+)- and MgATP-dependent and was inhibited by N-ethylmaleimide and botulinum A neurotoxin, indicating a bona fide action on the exocytotic mechanism. Furthermore, Ca2+ concentrations which trigger catecholamine secretion acted to prevent the leakage of NSF and alpha-SNAP from permeabilized cells. These findings provide functional evidence for a role of SNAPs in regulated exocytosis in chromaffin cells.

Indexed as

ExocytosisVesicular Transport ProteinsAdrenal MedullaAnimalsCarrier ProteinsCattleCells, CulturedChromaffin GranulesMembrane ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsCarrier ProteinsMembrane ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsVesicular Transport Proteins

Identifiers

PMID7835334
PMCPMC398076
OpenAlexW122481163

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.