ArticleThe Journal of cell biology1996
Granule lattice protein 1 (Grl1p), an acidic, calcium-binding protein in Tetrahymena thermophila dense-core secretory granules, influences granule size, shape, content organization, and release but not protein sorting or condensation.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 67 citations in OpenAlex.
- 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
- The secretory pathway in Tetrahymena is organized for efficient constitutive secretion at ciliary pockets.iScience · 2024Article
- TheMolecular biology of the cell · 2023Article
- An apical membrane complex for triggering rhoptry exocytosis and invasion in Toxoplasma.The EMBO journal · 2022Article
- Tetrahymena thermophila granule lattice protein 3 improves solubility of sexual stage malaria antigens expressed in Escherichia coli.Protein expression and purification · 2022Article
- A novel membrane complex is required for docking and regulated exocytosis of lysosome-related organelles in Tetrahymena thermophila.PLoS genetics · 2022Article
- ESCargo: a regulatable fluorescent secretory cargo for diverse model organisms.Molecular biology of the cell · 2020Article
- Fusion to Tetrahymena thermophila granule lattice protein 1 confers solubility to sexual stage malaria antigens in Escherichia coli.Protein expression and purification · 2019Article
- 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
- Whole Genome Sequencing Identifies a Novel Factor Required for Secretory Granule Maturation in Tetrahymena thermophila.G3 (Bethesda, Md.) · 2016Article
- Secretion of Polypeptide Crystals from Tetrahymena thermophila Secretory Organelles (Mucocysts) Depends on Processing by a Cysteine Cathepsin, Cth4p.Eukaryotic cell · 2015Article
- 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
- Constitutive secretion in Tetrahymena thermophila.Eukaryotic cell · 2010Article
- Independent transport and sorting of functionally distinct protein families in Tetrahymena thermophila dense core secretory granules.Eukaryotic cell · 2009Article
- Glutamylation on alpha-tubulin is not essential but affects the assembly and functions of a subset of microtubules in Tetrahymena thermophila.Eukaryotic cell · 2008Article
- Elucidation of clathrin-mediated endocytosis in tetrahymena reveals an evolutionarily convergent recruitment of dynamin.PLoS genetics · 2005Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The electron-dense cores of regulated secretory granules in the ciliate Tetrahymena thermophila are crystal lattices composed of multiple proteins. Granule synthesis involves a series of steps beginning with protein sorting, followed by the condensation and precise geometric assembly of the granule cargo. These steps may to various degrees be determined by the cargo proteins themselves. A prominent group of granule proteins, in ciliates as well as in vertebrate neuronal and endocrine cells, are acidic, heat-stable, and bind calcium. We focused on a protein with these characteristics named granule lattice protein 1 (Grl1p), which represents 16% of total granule contents, and we have now cloned the corresponding gene. Mutants in which the macronuclear copies of GRL1 have been disrupted continue to synthesize dense-core granules but are nonetheless defective in regulated protein secretion. To understand the nature of this defect, we characterized mutant and wild-type granules. In the absence of Grl1p, the sorting of the remaining granule proteins appears normal, and they condense to form a well-defined core. However, the condensed cores do not demonstrate a visible crystalline lattice, and are notably different from wild type in size and shape. The cellular secretion defect arises from failure of the aberrant granule cores to undergo rapid expansion and extrusion after exocytic fusion of the granule and plasma membranes. The results suggest that sorting, condensation, and precise granule assembly are distinct in their requirements for Grl1p.
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