Affinage · Toxoplasma gondii

DYRK1

putative cell-cycle-associated protein kinase DYRK · UniProt S8F8Y6

Audit flag: flagged
Annotated
2026-09-11
1 papers in source corpus 1 papers cited in narrative 1 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DYRK1 is a kinase implicated in the control of daughter parasite assembly during Toxoplasma gondii division, where it functions as a putative partner of the plant-like protein phosphatase PPKL (PMID:37398039). It was identified as a functional partner of PPKL by reciprocal Co-immunoprecipitation and proximity labeling, and complete knockout of DYRK1 phenocopies loss of PPKL, uncoupling division from DNA duplication: DNA replication proceeds normally while daughter parasite formation is severely defective (PMID:37398039). This genetic epistasis places DYRK1 in a PPKL-associated signaling pathway for daughter cell assembly. Beyond this single-study association (PMID:37398039), no direct substrates, catalytic characterization, or biochemical reconstitution of the DYRK1–PPKL relationship have been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 1 step
  1. 2023 Medium

    It was unknown which factors cooperate with the phosphatase PPKL to drive daughter parasite formation; identifying DYRK1 as a PPKL partner whose loss phenocopies PPKL depletion established a candidate kinase-phosphatase signaling module controlling division.

    Evidence Co-immunoprecipitation, proximity labeling, and complete gene knockout with phenotypic readout of daughter parasite formation in Toxoplasma gondii (preprint)

    PMID:37398039

    Open questions at the time
    • Functional relationship inferred from phenocopy rather than direct biochemical reconstitution of a DYRK1-PPKL interaction
    • No DYRK1 substrates or phosphorylation targets identified
    • Single lab, preprint status, and no confirmation of catalytic activity or the molecular basis of cortical cytoskeleton/daughter cell defects

Open questions

Synthesis pass · forward-looking unresolved questions
  • The direct substrates of DYRK1, the biochemical nature of its coupling to PPKL, and the mechanism by which it controls cortical cytoskeleton organization during daughter cell assembly remain unknown.
  • No identified phosphorylation substrates
  • No structural or reconstituted evidence for a DYRK1-PPKL complex
  • Mechanism linking DYRK1 activity to daughter parasite formation uncharacterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
PPKL (PLANT-LIKE PROTEIN PHOSPHATASE) [#0]

Evidence

Reading pass · 1 per-paper finding extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2023 DYRK1 was identified as a potential functional partner of the plant-like protein phosphatase PPKL via Co-Immunoprecipitation and proximity labeling, and complete knockout of DYRK1 phenocopies the loss of PPKL (uncoupling of division with normal DNA duplication but severe defects in forming daughter parasites), strongly suggesting a functional relationship between these two signaling proteins in daughter parasite development. Co-Immunoprecipitation, proximity labeling, and complete gene knockout with phenotypic readout (daughter parasite formation defects) bioRxivpreprint Medium 37398039

Source papers

Stage 0 corpus · 1 paper · ranked by NIH iCite citations
Year Title Journal Citations PMID
2023 The protein phosphatase PPKL is a key regulator of daughter parasite development in Toxoplasma gondii. bioRxiv : the preprint server for biology 2 37398039