ArticleMolecular biology of the cell1998
Proteolytic processing and Ca2+-binding activity of dense-core vesicle polypeptides in Tetrahymena.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 41 citations in OpenAlex.
- Protrichocysts: a hybrid defense extrusive organelle bridging mechanical projection and chemical secretion in ciliates.Current research in microbial sciences · 2026Article
- 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
- 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
- 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
- Basal body duplication and maintenance require one member of the Tetrahymena thermophila centrin gene family.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
- New class of cargo protein in Tetrahymena thermophila dense core secretory granules.Eukaryotic cell · 2002Article
- An antisense approach to phenotype-based gene cloning in Tetrahymena.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Proinsulin endoproteolysis confers enhanced targeting of processed insulin to the regulated secretory pathway.Molecular biology of the cell · 2000Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Formation and discharge of dense-core secretory vesicles depend on controlled rearrangement of the core proteins during their assembly and dispersal. The ciliate Tetrahymena thermophila offers a simple system in which the mechanisms may be studied. Here we show that most of the core consists of a set of polypeptides derived proteolytically from five precursors. These share little overall amino acid identity but are nonetheless predicted to have structural similarity. In addition, sites of proteolytic processing are notably conserved and suggest that specific endoproteases as well as carboxypeptidase are involved in core maturation. In vitro binding studies and sequence analysis suggest that the polypeptides bind calcium in vivo. Core assembly and postexocytic dispersal are compartment-specific events. Two likely regulatory factors are proteolytic processing and exposure to calcium. We asked whether these might directly influence the conformations of core proteins. Results using an in vitro chymotrypsin accessibility assay suggest that these factors can induce sequential structural rearrangements. Such progressive changes in polypeptide folding may underlie the mechanisms of assembly and of rapid postexocytic release. The parallels between dense-core vesicles in different systems suggest that similar mechanisms are widespread in this class of organelles.
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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.