subpellicular microtubule
A singlet microtubule that lies underneath the inner membrane pellicle complex and emanates from the basal ring of the conoid. [GO:0020025]
Part of: apical complex (GO:0020007)
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| alpha- and beta-tubulins | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | ESSENTIAL | Tubulin subunits that polymerize into the conventional singlet subpellicular microtubules of Toxoplasma.
|
Taxonomic distribution
NCBITaxon:5811Toxoplasma gondii — COMMON: Toxoplasma tachyzoites have 22 singlet subpellicular microtubules attached at the polar ring of the apical complex and running beneath the inner membrane complex. [DOI:10.1371/journal.ppat.0020013]
Canonical examples
NCBITaxon:5811Toxoplasma gondii — Apicomplexan model in which the 32 nm periodicity shared by isolated subpellicular microtubules and the overlying pellicular intramembranous-particle lattice was studied structurally. [DOI:10.1242/jcs.110.1.35]
Functions
- pellicle microtubule scaffold — Subpellicular microtubules form a longitudinal cortical microtubule scaffold beneath the inner membrane pellicle complex and alongside the pellicular intramembranous-particle lattice in Toxoplasma.
DOI:10.1242/jcs.110.1.35Morrissette, Murray and Roos 1997 resolved a 32 nm periodicity in isolated Toxoplasma subpellicular microtubules and the overlying pellicle particle lattice.DOI:10.1371/journal.ppat.0020013Hu et al. 2006 described the Toxoplasma subpellicular microtubules as cytoskeletal elements closely associated with the cytoplasmic face of the IMC.
Mechanism graphs
Tubulin singlets extend from the polar ring under the Toxoplasma IMC (ASSEMBLY)
Alpha- and beta-tubulins polymerize into the 22 conventional subpellicular microtubules that attach at the polar ring of the Toxoplasma apical complex, run beneath the inner membrane pellicle complex, and align with a periodic intramembranous-particle lattice.
| Subject | Predicate | Object | Evidence |
|---|---|---|---|
| alpha- and beta-tubulins | polymerize into | subpellicular microtubule |
|
| subpellicular microtubule | attaches to | basal ring of apical complex |
|
| subpellicular microtubule | lies underneath | inner membrane pellicle complex |
|
| subpellicular microtubule | associates with | pellicular intramembranous-particle lattice |
|
Discussions
- CURATION_TODO (OPEN): Resolve exact component boundaries and source-neutral groundings for subpellicular microtubule end proteins, plus-end factors, and IMC particle-lattice linkers. Morrissette, Murray and Roos resolved an intramembranous-particle lattice aligned with Toxoplasma subpellicular microtubules, and Hu et al. localized proteins such as TgDLC, TgMORN1 and TgCentrin2 near subpellicular microtubule ends or daughter scaffolds. This record leaves those factors out until exact conserved constituent, linker, marker or assembly-factor boundaries are curated.
- INTERPRETATION (RESOLVED): Keep GO:0020025 scoped to apicomplexan subpellicular microtubules rather than kinetoplastid cortical microtubule arrays that share the same plain-English name. The phrase subpellicular microtubule is also used in Trypanosoma literature, but GO:0020025 is taxon-constrained to Apicomplexa and defined by apicomplexan IMC and conoid topology. This record therefore curates only the apicomplexan structure.
- INTERPRETATION (RESOLVED): Use the exact basal SPMT-origin ring in the attachment graph. The former graph grounded the generic polar-ring name to GO:0020031, whose definition denotes the anterior conoid-fiber-origin ring. GO:0020025 and GO:0020032 identify the basal SPMT-origin topology, in agreement with the primary anatomical distinction.
Evidence
GO:0020025Gene Ontology cellular-component term for the apicomplexan subpellicular microtubule.GO:0005874Gene Ontology places subpellicular microtubules under the microtubule class.GO:0020007Gene Ontology models subpellicular microtubules as part of the apicomplexan apical complex.DOI:10.1242/jcs.110.1.35Morrissette, Murray and Roos 1997, Subpellicular microtubules associate with an intramembranous particle lattice in the protozoan parasite Toxoplasma gondii, Journal of Cell Science.DOI:10.1371/journal.ppat.0020013Hu et al. 2006, Cytoskeletal Components of an Invasion Machine--the Apical Complex of Toxoplasma gondii, PLOS Pathogens.DOI:10.1155/2014/893272Sheriff, Lim and He 2014 tracked YFP-alpha-tubulin incorporation into Trypanosoma brucei subpellicular microtubules; the article is cited here only to distinguish kinetoplastid cortical arrays from GO:0020025.GO:0020032Exact basal-ring identity for the SPMT-origin attachment site; not a synonym for the entire modern multilayer APR.
Curation history
2026-09-22T11:58:42Zcodex · CREATED_RECORD — Scaffolded by scripts/new_record.py2026-09-22T12:00:13Zcodex · EXPANDED_RECORD — Added GO microtubule parentage and apical-complex parthood, a reviewed label-only alpha/beta tubulin component, Toxoplasma gondii scope, DOI/GO evidence, a nonmechanistic cortical topology graph, and curation discussions for accessory components and the Apicomplexa-specific GO boundary.2026-09-22T12:11:53Zcodex · REVIEW_FIXES — Addressed PR #1277 review issues #1278 and #1279 by narrowing the Toxoplasma canonical-example note to the Morrissette et al. 1997 lattice evidence and adding direct Sheriff et al. 2014 evidence for excluded Trypanosoma subpellicular microtubule usage.2026-10-11T19:53:42Zcodex · ADDRESS_SAVED_REVIEW — Addressed #2254: Retargeted the SPMT attachment node and edge coherently to GO:0020032, preserving the lattice, molecular constituents and Trypanosoma boundary.
Source: data/structures/cytoskeleton/subpellicular_microtubule.yaml