| 2010 |
CITH (PF3D7_1474900 homolog in P. berghei) is a core component of a messenger ribonucleoprotein (mRNP) complex in female gametocytes, identified together with the RNA helicase DOZI by affinity purification coupled with mass spectrometry. This mRNP contains 16 major factors, integrates eIF4E and poly(A)-binding protein, excludes P body RNA degradation factors and translation-initiation-promoting eIF4G, and holds translationally silent transcripts. |
Affinity purification coupled with mass spectrometry (AP-MS); RNA-immunoprecipitation; global expression profiling of CITH-KO mutants |
PLoS pathogens |
High |
20169188
|
| 2010 |
Gene deletion of CITH in P. berghei produces fertilization-competent gametocytes, but zygotes fail to develop into ookinetes in a female gametocyte-mutant manner. RNA-immunoprecipitation and expression profiling of CITH-KO mutants establish CITH as a crucial repressor of maternally supplied mRNAs. |
Gene deletion (KO); RNA-immunoprecipitation; global expression profiling |
PLoS pathogens |
High |
20169188
|
| 2016 |
In P. berghei, CITH binds all nine cpw-wpc family transcripts in female gametocytes, as shown by RNA immunoprecipitation followed by RT-PCR, indicating that CITH participates in translational repression of this gene family prior to mosquito transmission. |
RNA immunoprecipitation followed by RT-PCR |
Parasitology international |
Medium |
27312996
|
| 2018 |
In P. falciparum female gametocytes, CITH is a component of stress granules and interacts with the novel seven-helix protein 7-Helix-1, as well as with DOZI and PABP1, as part of a ribonucleoprotein complex involved in translational repression. |
Co-immunoprecipitation; colocalization by fluorescence microscopy |
PLoS pathogens |
Medium |
30133543
|
| 2021 |
In P. berghei, CITH interacts with GBP2, DOZI, and ALBA4 as part of a translational repression complex, identified by immunoprecipitation coupled to mass spectrometry. |
Immunoprecipitation coupled to mass spectrometry (IP-MS) |
Frontiers in cellular and infection microbiology |
Low |
34604117
|
| 2023 |
In P. falciparum, CITH interacts with the CCCH zinc finger protein MD3, as revealed by BioID proximity labeling combined with co-immunoprecipitation, placing CITH within a regulatory complex for post-transcriptional fine-tuning of male gametocytogenesis. |
BioID proximity labeling; co-immunoprecipitation |
Molecular microbiology |
Low |
38148574
|
| 2025 |
In P. yoelii, TurboID-based proximity proteomics of the DOZI/CITH/ALBA complex across the host-to-vector transmission event reveals that CITH is part of a translationally repressive complex in female gametocytes whose spatial arrangement and composition change substantially upon fertilization. Proteins associated with the 5' and 3' ends of mRNAs are in proximity during repression and dissociate in zygotes, consistent with release of translational repression. DOZI exchanges its interaction from NOT1-G in female gametocytes to canonical NOT1 in zygotes, providing a trigger model for mRNA release. |
TurboID-based proximity proteomics (BioID); quantitative DIA-MS proteomics; transcriptomics; ultrastructure expansion microscopy; structured illumination microscopy |
PLoS pathogens |
High |
39777415
|
| 2024 |
Preprint version of the P. yoelii study: TurboID proximity proteomics of the DOZI/CITH/ALBA complex shows compositional and spatial changes across female gametocyte-to-zygote transition; CITH is part of the repressive complex that dissociates upon release of translational repression, with DOZI switching from NOT1-G to canonical NOT1 association in zygotes. |
TurboID-based proximity proteomics; DIA-MS proteomics; ultrastructure expansion microscopy; structured illumination microscopy; phosphoproteomics |
bioRxivpreprint |
Medium |
38352447
|