ArticleTraffic (Copenhagen, Denmark)2005
Core formation and the acquisition of fusion competence are linked during secretory granule maturation in Tetrahymena.
Article in Traffic (Copenhagen, Denmark), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- A conserved GTPase complex gates exocytosis for defence and parasitism across alveolates.Nature microbiology · 2026Article
- Maturation stage-specific V-ATPase disassembly explains the neutral pH of mature mucocyst lysosome-related organelles in Tetrahymena thermophila.Journal of cell science · 2025Article
- Inferring gene-pathway associations from consolidated transcriptome datasets: an interactive gene network explorer forNAR genomics and bioinformatics · 2025Article
- Fast Super-Resolution Live Cell Imaging of Nuclear Membrane-Endoplasmic Reticulum Dynamics.Methods in molecular biology (Clifton, N.J.) · 2025Article
- The secretory pathway in Tetrahymena is organized for efficient constitutive secretion at ciliary pockets.iScience · 2024Article
- A novel membrane complex is required for docking and regulated exocytosis of lysosome-related organelles in Tetrahymena thermophila.PLoS genetics · 2022Article
- Remodeling the Specificity of an Endosomal CORVET Tether Underlies Formation of Regulated Secretory Vesicles in the Ciliate Tetrahymena thermophila.Current biology : CB · 2018Article
- 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
- An evolutionary balance: conservation vs innovation in ciliate membrane trafficking.Traffic (Copenhagen, Denmark) · 2017Review
- Whole Genome Sequencing Identifies a Novel Factor Required for Secretory Granule Maturation in Tetrahymena thermophila.G3 (Bethesda, Md.) · 2016Article
- Review
- Tetrahymena thermophila: a divergent perspective on membrane traffic.Journal of experimental zoology. Part B, Molecular and developmental evolution · 2014Review
- 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
- Expression, secretion and surface display of a human alkaline phosphatase by the ciliate Tetrahymena thermophila.BMC biotechnology · 2011Article
- Comprehensive analysis reveals dynamic and evolutionary plasticity of Rab GTPases and membrane traffic in Tetrahymena thermophila.PLoS genetics · 2010Article
- Independent transport and sorting of functionally distinct protein families in Tetrahymena thermophila dense core secretory granules.Eukaryotic cell · 2009Article
- The Tetrahymena thermophila phagosome proteome.Eukaryotic cell · 2006Article
- Elucidation of clathrin-mediated endocytosis in tetrahymena reveals an evolutionarily convergent recruitment of dynamin.PLoS genetics · 2005Article
Corrections and comments
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Authors and funding
5 authors.
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Abstract
The formation of dense core secretory granules is a multistage process beginning in the trans Golgi network and continuing during a period of granule maturation. Direct interactions between proteins in the membrane and those in the forming dense core may be important for sorting during this process, as well as for organizing membrane proteins in mature granules. We have isolated two mutants in dense core granule formation in the ciliate Tetrahymena thermophila, an organism in which this pathway is genetically accessible. The mutants lie in two distinct genes but have similar phenotypes, marked by accumulation of a set of granule cargo markers in intracellular vesicles resembling immature secretory granules. Sorting to these vesicles appears specific, since they do not contain detectable levels of an extraneous secretory marker. The mutants were initially identified on the basis of aberrant proprotein processing, but also showed defects in the docking of the immature granules. These defects, in core assembly and docking, were similarly conditional with respect to growth conditions, and therefore are likely to be tightly linked. In starved cells, the processing defect was less severe, and the immature granules could dock but still did not undergo stimulated exocytosis. We identified a lumenal protein that localizes to the docking-competent end of wildtype granules, but which is delocalized in the mutants. Our results suggest that dense cores have functionally distinct domains that may be important for organizing membrane proteins involved in docking and fusion.
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