Mutant/mutation
The mutant expresses a C-terminal HA, mScarlet or pCP-tagged version of AKiT2

Protein (function)
From the Abstract: 
Kinetochores are multiprotein assemblies directing mitotic spindle attachment and chromosome segregation. In apicomplexan parasites, most known kinetochore components and associated regulators are apparently missing, suggesting a minimal structure with limited control over chromosome segregation. In this study, we use interactomics combined with deep homology searches to identify six divergent eukaryotic components, in addition to a set of eight apicomplexan kinetochore proteins (AKiTs) that bear no detectable sequence similarity to known proteins. The nanoscale  organization of the apicomplexan kinetochore includes four subdomains, each displaying different evolutionary rates across the phylum. Functional analyses confirm  AKiTs are essential for mitosis and reveal architectures parallel to biorientation at  metaphase.

PBANKA_0414300 - NUF2; PBANKA_0405800 - SKA2
PBANKA_0812300 and PBANKA_1362400: in complex with SKA2 (SKA1; SKA3)
PBANKA_0621300 - Apicomplexan Kinetochore protein 1 (AKiT1)
AKit2 - AKiT6: PBANKA_1202800 (AKiT2); PBANKA_0612200  (AKiT3), PBANKA_1310500 (AKiT4), PBANKA_1243900  (AKiT5), PBANKA_0522000  (AKiT6)
AKiT7-9: PBANKA_0612300 (AKiT7), PBANKA_0213200 (AKiT8), PBANKA_1307000 (AKit9)
AKiT10-11: PBANKA_0406000 (AKiT10), PBANKA_0803900 (AKiT11)

Phenotype
See below

Additional information
From the Abstract: 
Kinetochores are multiprotein assemblies directing mitotic spindle attachment and chromosome segregation. In apicomplexan parasites, most known kinetochore components and associated regulators are apparently missing, suggesting a minimal structure with limited control over chromosome segregation. In this study, we use interactomics combined with deep homology searches to identify six divergent eukaryotic components, in addition to a set of eight apicomplexan kinetochore proteins (AKiTs) that bear no detectable sequence similarity to known proteins. The nanoscale  organization of the apicomplexan kinetochore includes four subdomains, each displaying different evolutionary rates across the phylum. Functional analyses confirm  AKiTs are essential for mitosis and reveal architectures parallel to biorientation at  metaphase.

PBANKA_0414300 - NUF2; PBANKA_0405800 - SKA2
In agreement with previously localized Plasmodium centromeres and kinetochores, location and movement of NUF2 and SKA2 fusion proteins was restricted to the nuclear periphery during progression of asexual blood-stage divisions. SKA2 and NUF2 fusion proteins showed very different localizations during sexual development. Whilst “rod-like bridges”, as previously described for components of the NDC80/NUF2 complex, were visible for NUF2 during the three rounds of DNA replication and mitosis that occur at microgametogenesis – SKA2 signal at kinetochore foci was not clearly detectable. A similar dichotomy was seen post-activation of the macrogametocyte, NUF2 spreading sparingly across the cytoplasm compared to SKA2 residing primarily in the nucleus. However, 24-hours post-fertilization and meiosis, both fusion proteins united as four  distinct nuclear foci in fully developed banana-shaped ookinetes. 

PBANKA_0812300 and PBANKA_1362400: in complex with SKA2
Both tagged PBANKA_0812300 and PBANKA_1362400 proteins showed localization patterns highly similar to that of SKA2 in the malaria parasite, colocalizing with NUF2 during asexual blood stage divisions, not detected during microgametogenesis and present as four nuclear foci in fully developed ookinetes.

PBANKA_0621300 - Apicomplexan Kinetochore protein 1 (AKiT1)
the tagged protein showed clear co-localization with NUF2 throughout asexual blood-stage divisions. In contrast to previously localized SKA components, foci were also seen  across spindle bundles during microgametogenesis. Furthermore, the protein accumulated as foci in the nuclei of female gametes prior to fertilization, suggesting  kinetochore recruitment prior to outer kinetochore NDC80/NUF2 complex assembly. Given biochemical affinities, kinetochore localization and conservation across apicomplexan organisms, the proteinwas named  Apicomplexan Kinetochore protein 1 (AKiT1). During the first round of microgametocyte mitosis, PbAKiT1 localized along the spindle as pairs of kinetochore foci.

AKit2 - AKiT6: PBANKA_1202800 (AKiT2); PBANKA_0612200  (AKiT3), PBANKA_1310500 (AKiT4), PBANKA_1243900  (AKiT5), PBANKA_0522000  (AKiT6)
Along with AKiT1, 5 proteins of unknown function were most abundant across PbAKiT1 immunoprecipitates. Each taggedhypothetical protein showed PbAKiT1-like localization patterns, colocalizing with NUF2 during blood-stage and microgametocyte mitosis, also present as foci in activated female macrogametes and accumulating as four puncta in fully developed ookinetes.

AKiT7-9: PBANKA_0612300 (AKiT7), PBANKA_0213200 (AKiT8), PBANKA_1307000 (AKiT9)  
Three proteins of unknown function formed a distinct enrichment profile compared to AKiTs 1 - 6. Each tagged protein showed characteristic kinetochore localizations, with  that encoded by PBANKA_0612300 displaying an additional localization reminiscent of  the nuclear membrane during sexual development.

AKiT10-11: PBANKA_0406000 (AKiT10), PBANKA_0803900 (AKiT11)
Principle components 2 and 3 further resolved AKiT clustering, with the distinction of AKiTs 1 - 6 relative to AKiT9, itself clustering with histones H3 and H4, the histone modifier SPT16, and two additional proteins of unknown function (Gene IDs: PBANKA_0406000 and PBANKA_0803900) that we named AKiT10 and AKiT11.

From the paper:
'Taken together, our immuno-affinity purification strategy has identified 4 biochemically stable compartments at the Plasmodium kinetochore (Table S4). Between compartments, more labile interactions were also detected between the outer kinetochore NDC80/NUF2 complex and PbAKiT1, itself closely associated with 5 additional AKiT proteins. AKiT1 - 6 also interact with AKiT9 - 11, which, given their association with proteins known to interact with DNA, likely form the most centromere proximal kinetochore sub-domain identified in this study.'

Other mutants