ArticleEukaryotic cell2002
New class of cargo protein in Tetrahymena thermophila dense core secretory granules.
Article in Eukaryotic cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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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
11 citing papers in PubMed.
- Inferring gene-pathway associations from consolidated transcriptome datasets: an interactive gene network explorer forNAR genomics and bioinformatics · 2025Article
- TheMolecular biology of the cell · 2023Article
- Diversification of CORVET tethers facilitates transport complexity inJournal of cell science · 2020Article
- An endosomal syntaxin and the AP-3 complex are required for formation and maturation of candidate lysosome-related secretory organelles (mucocysts) inMolecular biology of the cell · 2017Article
- Whole Genome Sequencing Identifies a Novel Factor Required for Secretory Granule Maturation in Tetrahymena thermophila.G3 (Bethesda, Md.) · 2016Article
- An aspartyl cathepsin, CTH3, is essential for proprotein processing during secretory granule maturation in Tetrahymena thermophila.Molecular biology of the cell · 2014Article
- Lysosomal sorting receptors are essential for secretory granule biogenesis in Tetrahymena.The Journal of cell biology · 2013Article
- Conservation and innovation in Tetrahymena membrane traffic: proteins, lipids, and compartments.Methods in cell biology · 2012Review
- Independent transport and sorting of functionally distinct protein families in Tetrahymena thermophila dense core secretory granules.Eukaryotic cell · 2009Article
- Genetic, genomic, and functional analysis of the granule lattice proteins in Tetrahymena secretory granules.Molecular biology of the cell · 2005Article
- Core formation and the acquisition of fusion competence are linked during secretory granule maturation in Tetrahymena.Traffic (Copenhagen, Denmark) · 2005Article
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Authors and funding
3 authors.
Funding
Abstract
Regulated exocytosis of dense core secretory granules releases biologically active proteins in a stimulus-dependent fashion. The packaging of the cargo within newly forming granules involves a transition: soluble polypeptides condense to form water-insoluble aggregates that constitute the granule cores. Following exocytosis, the cores generally disassemble to diffuse in the cell environment. The ciliates Tetrahymena thermophila and Paramecium tetraurelia have been advanced as genetically manipulatable systems for studying exocytosis via dense core granules. However, all of the known granule proteins in these organisms condense to form the architectural units of lattices that are insoluble both before and after exocytosis. Using an approach designed to detect new granule proteins, we have now identified Igr1p (induced during granule regeneration). By structural criteria, it is unrelated to the previously characterized lattice-forming proteins. It is distinct in that it is capable of dissociating from the insoluble lattice following secretion and therefore represents the first diffusible protein identified in ciliate granules.
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