| 2006 |
MORN1 localizes to ring structures at the apical and posterior ends of the inner membrane complex (IMC) and to the centrocone (a specialized nuclear structure organizing the mitotic spindle). Time-lapse imaging showed these structures are highly dynamic during division. Overexpression of MORN1 caused specific defects in nuclear segregation and daughter cell formation. Biochemically, recombinant MORN1 is soluble in bacteria, but in the parasite it associates with the cytoskeleton after detergent extraction, consistent with a role as a linker between membrane regions and the cytoskeleton. |
YFP fusion screen, time-lapse live imaging, overexpression with phenotypic readout, detergent fractionation/cytoskeletal association assay |
Journal of cell science |
High |
16684814
|
| 2008 |
MORN1 localizes to the posterior ring of the IMC of multiple daughters during T. gondii endopolygeny, Eimeria schizogony, and P. falciparum schizogony, and P. falciparum MORN1 protein peaks in late schizogony. In sexual stages, MORN1 is organized as a ring-like structure where microgametes bud from the microgametocyte, and is present near flagellar basal bodies and mitochondrion in mature microgametes, indicating a conserved role in IMC assembly across asexual and sexual development. |
Immunolocalization (antibody reactivity), expression analysis across developmental stages in T. gondii, Eimeria spp., and P. falciparum |
Eukaryotic cell |
Medium |
18310354
|
| 2010 |
Conditional ablation of MORN1 in T. gondii results in failure to assemble the basal complex (none of the known basal complex components localize correctly), formation of double- to multi-headed 'Janus' parasites with two complete apical complexes but no basal complex, and failure to efficiently constrict and divide the apicoplast. Cell cycle progression (mother cytoskeleton disassembly, repeated budding) continues despite these defects. Deletion of a single MORN domain abrogated function, and the linker between MORN domains 6 and 7 was identified as critical, defining MORN1 as essential for basal complex assembly and apicoplast segregation. |
Conditional null mutant (inducible knockdown), immunofluorescence for basal complex markers, domain-deletion analysis |
PloS one |
High |
20808817
|
| 2010 |
Knockout of TgMORN1 (ΔTgMORN1) using Cre-LoxP grossly disrupted the structure of the basal complex and caused cytokinesis defects. ΔTgMORN1 parasites showed significant growth impairment in vitro and greatly attenuated virulence in mice, establishing that TgMORN1 is required for maintaining structural integrity of the parasite posterior end and that cytoskeleton integrity is essential for virulence. |
Cre-LoxP knockout, in vitro growth assay, mouse virulence model |
PLoS pathogens |
High |
20140195
|
| 2012 |
Subcellular fractionation combined with affinity purification of the MORN1 complex identified the protein composition of the basal complex. Two new basal complex components were identified, one uniquely associating with the basal complex only in mature parasites. MORN1 was confirmed to act as a scaffolding protein for basal complex assembly. |
Subcellular fractionation, affinity purification (MORN1 co-purification/pulldown), mass spectrometry |
Cytoskeleton (Hoboken, N.J.) |
Medium |
23027733
|
| 2016 |
Yeast two-hybrid screen using TgMORN1 as bait identified the HAD phosphatase HAD2a as a direct interaction partner. HAD2a co-localizes with MORN1 at the basal complex during contraction and is required for basal complex assembly and cytokinesis, suggesting that MORN1-associated phosphorylation regulates basal complex structure and/or contractile function. |
Yeast two-hybrid screen with TgMORN1 as bait, co-localization by immunofluorescence, conditional knockout of HAD2a, in vitro phosphatase activity assay |
Cellular microbiology |
Medium |
26840427
|
| 2020 |
Crystal structures, SAXS, and EM of MORN1 from Trypanosoma brucei, Toxoplasma gondii, and Plasmodium falciparum revealed that MORN repeats are protein-protein interaction modules (not lipid-binding modules as previously assumed). All three ortholog structures dimerize via their C-termini in an antiparallel configuration, and dimers can adopt extended or V-shaped quaternary structures depending on specific interface residues. No evidence for membrane or lipid vesicle binding was found, though individual phospholipid interactions were detected. |
Macromolecular X-ray crystallography, SAXS, electron microscopy, in vitro lipid-binding assays |
PloS one |
High |
33296386
|
| 2022 |
Reciprocal proximity-based biotinylation (BioID) proteomics using MORN1 as a landmark identified four architecturally distinct basal complex (BC) subcomplexes with dynamic composition. MORN1, together with BCC4, was found to form a 'rubber band' that sequesters the basal end of the assembling daughter cytoskeleton, constituting the essential cell-division function of the BC. |
Reciprocal BioID proximity biotinylation, conditional expression disruption, spatiotemporal immunofluorescence analysis |
Nature communications |
High |
35941170
|
| 2026 |
SPR-MS target identification and AI-driven analysis identified TgMORN1 as the highest-scoring target of Licochalcone A. RNAi silencing of TgMORN1 attenuated the anti-proliferative effect of Lico A. Western blotting, NanoDSF, and SPR supported direct binding between Lico A and TgMORN1, with residues S168 and D203 implicated in modulating TgMORN1 thermal stability. |
SPR-MS target identification, RNAi knockdown, NanoDSF thermal stability assay, SPR binding assay, Western blotting |
Biomolecules |
Medium |
41897346
|