mucocyst
A small subcellular vesicle, surrounded by a membrane, in the pellicle of ciliate protozoans that discharges a mucus-like secretion. [GO:0036000]
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| mucocyst membrane | Lipid | part of | Reviewed label only (reviewed name; no accession asserted) | ESSENTIAL | Membrane that bounds the Tetrahymena mucocyst and encloses its regulated secretory cargo.
| ||
| granule lattice proteins | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | GRL | UNKNOWN | Major dense-core cargo proteins that coassemble into the crystalline lattice of the mucocyst lumen.
| |
| granule tip proteins | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | GRT | UNKNOWN | Dense-core granule cargo proteins that occupy a mucocyst tip domain and are transported independently from Grl lattice cargo.
| |
| MDD mucocyst docking and discharge complex | Protein complex | acts on | Reviewed label only (reviewed name; no accession asserted) | MDL1 | UNKNOWN | Mucocyst-associated membrane complex that localizes to the organelle tip and is required for efficient docking and regulated exocytosis.
|
Taxonomic distribution
NCBITaxon:5911Tetrahymena thermophila — COMMON: Mucocysts are dense-core regulated secretory organelles characterized in Tetrahymena thermophila. [DOI:10.1534/g3.116.028878]
Canonical examples
NCBITaxon:5911Tetrahymena thermophila — Ciliate model in which mucocyst dense-core cargo sorting, maturation and docking have been studied genetically and cell biologically. [DOI:10.1534/g3.116.028878]
Functions
- regulated mucocyst exocytosis — Docked mucocysts release dense-core cargo from the Tetrahymena cell surface in response to extracellular stimulation.
DOI:10.1371/journal.pgen.1010194Kuppannan et al. 2022 link the MDD complex to docking and regulated exocytosis of Tetrahymena mucocysts.DOI:10.1128/EC.00151-09Rahaman et al. 2009 describe Grl lattice expansion as a propulsive mechanism during dense-core granule release.
Mechanism graphs
Mucocyst core proteins mature before docking and discharge (FUNCTION)
A membrane-bounded Tetrahymena mucocyst stores Grl lattice and Grt tip proteins as dense-core cargo; the MDD membrane complex localizes to the mucocyst tip and supports docking and regulated exocytosis.
| Subject | Predicate | Object | Evidence |
|---|---|---|---|
| mucocyst membrane | bounds | mucocyst |
|
| mucocyst lumen | is part of | mucocyst |
|
| granule lattice proteins | coassemble into | mucocyst crystalline lattice |
|
| mucocyst crystalline lattice | is stored in | mucocyst lumen |
|
| granule tip proteins | sort independently to | mucocyst |
|
| MDD mucocyst docking and discharge complex | localizes to tip of | mucocyst |
|
| MDD mucocyst docking and discharge complex | supports | regulated exocytosis |
|
Discussions
- CURATION_TODO (OPEN): Resolve exact source-neutral family or complex groundings for the mucocyst membrane, Grl proteins, Grt proteins and MDD complex. The first mucocyst record curates the membrane, major dense-core cargo cohorts and the docking/discharge complex from Tetrahymena studies, but exact cross-taxon CURIEs for those local component classes were not curated.
- INTERPRETATION (RESOLVED): Tetrahymena maturation factors such as Mma1p, AP-3 and endosomal syntaxin were not modeled as mature mucocyst components. Mma1p and membrane-trafficking factors can be required for mucocyst biogenesis, but the first record only models cargo or machinery associated with mature docked or discharge-competent mucocysts. Proteins that act upstream in sorting or maturation should be added only if evidence places them in the mature organelle or at the assembled organelle boundary.
Evidence
GO:0036000Gene Ontology cellular-component term for mucocyst.DOI:10.1534/g3.116.028878Kontur et al. 2016, Whole Genome Sequencing Identifies a Novel Factor Required for Secretory Granule Maturation in Tetrahymena thermophila, G3 Genes|Genomes|Genetics.DOI:10.1128/EC.00151-09Rahaman et al. 2009, Independent Transport and Sorting of Functionally Distinct Protein Families in Tetrahymena thermophila Dense Core Secretory Granules, Eukaryotic Cell.DOI:10.1371/journal.pgen.1010194Kuppannan et al. 2022, A novel membrane complex is required for docking and regulated exocytosis of lysosome-related organelles in Tetrahymena thermophila, PLOS Genetics.DOI:10.1091/mbc.e17-01-0018Kaur et al. 2017, An endosomal syntaxin and the AP-3 complex are required for formation and maturation of candidate lysosome-related secretory organelles (mucocysts) in Tetrahymena thermophila, Molecular Biology of the Cell.
Curation history
2026-09-12T04:24:49Zcodex · CREATED_RECORD — Scaffolded by scripts/new_record.py2026-09-12T04:25:53Zcodex · EXPANDED_RECORD — Added secretory-granule parentage, mucocyst membrane, Grl, Grt and MDD components, Tetrahymena thermophila taxonomic scope and canonical example, regulated-exocytosis function, a mucocyst docking/discharge graph, and reviewed-label-only component grounding discussions.2026-09-12T04:30:37Zcodex · FIXED_DISCUSSION_ANCHOR — Retargeted the mucocyst maturation-factor boundary discussion from a section-level components anchor to the MDD complex component.2026-09-12T04:34:15Zcodex · ADDRESSED_PR_REVIEW — Addressed PR #579 review issues #580, #581 and #582 by retargeting the Grl coassembly edge to a crystalline-lattice node, removing the MDD abbreviation from gene_symbols, and adding direct Kaur 2017 evidence for AP-3/endosomal syntaxin boundary exclusions.