ArticleGenetics2002
N-ethylmaleimide-sensitive factor is required to organize functional exocytotic microdomains in paramecium.
Article in Genetics, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
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Who cites it
5 citing papers in PubMed, 29 citations in OpenAlex.
- An evolutionary balance: conservation vs innovation in ciliate membrane trafficking.Traffic (Copenhagen, Denmark) · 2017Review
- A forward genetic screen reveals essential and non-essential RNAi factors in Paramecium tetraurelia.Nucleic acids research · 2014Article
- Molecular identification of a SNAP-25-like SNARE protein in Paramecium.Eukaryotic cell · 2008Article
- Nd6p, a novel protein with RCC1-like domains involved in exocytosis in Paramecium tetraurelia.Eukaryotic cell · 2005Article
- Random sequencing of Paramecium somatic DNA.Eukaryotic cell · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In exocytosis, secretory granules contact plasma membrane at sites where microdomains can be observed, which are sometimes marked by intramembranous particle arrays. Such arrays are particularly obvious when membrane fusion is frozen at a subterminal stage, e.g., in neuromuscular junctions and ciliate exocytotic sites. In Paramecium, a genetic approach has shown that the "rosettes" of intramembranous particles are essential for stimulated exocytosis of secretory granules, the trichocysts. The identification of two genes encoding the N-ethylmaleimide-sensitive factor (NSF), a chaperone ATPase involved in organelle docking, prompted us to analyze its potential role in trichocyst exocytosis using a gene-silencing strategy. Here we show that NSF deprivation strongly interferes with rosette assembly but does not disturb the functioning of exocytotic sites already formed. We conclude that rosette organization involves ubiquitous partners of the fusion machinery and discuss where NSF could intervene in this mechanism.
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Registered trials
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.