Affinage · Plasmodium

CACYBP

PF3D7_1238100 · calcyclin binding protein, putative

Annotated
2026-09-08
2 papers in source corpus 2 papers cited in narrative 2 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

CACYBP (PF3D7_1238100) is a component of the Plasmodium falciparum SCF (PfSCF) ubiquitin E3 ligase complex, associating with PfCullin-1, PfRbx1, PfSkp1, and PfFBXO1, as established by immunoprecipitation and in vitro interaction assays coupled with a functional ubiquitination assay (PMID:38416790). In P. yoelii nigeriensis, the ortholog is a ~27 kDa protein expressed across all blood stages that adopts both monomer and dimer forms (PMID:36707015). Beyond its membership in the PfSCF complex (PMID:38416790) and these basic molecular properties of the P. yoelii nigeriensis ortholog (PMID:36707015), no substrate, catalytic contribution, or specific molecular function of CACYBP itself has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2023 Low

    To provide any biochemical footing for an uncharacterized parasite protein, the basic molecular properties of the CACYBP ortholog were defined, establishing its expression pattern and oligomeric behavior.

    Evidence Cloning, recombinant protein purification, and Western blot of parasite lysate in P. yoelii nigeriensis

    PMID:36707015

    Open questions at the time
    • Single lab establishing only size, oligomeric state, and stage expression; no functional mechanism established
    • No binding partners or complex context defined for the ortholog
    • Functional significance of monomer/dimer interconversion unknown
  2. 2024 Medium

    To place CACYBP in a defined molecular pathway, it was tested for association with a candidate ubiquitin ligase, establishing it as a member of a functional SCF E3 ligase complex.

    Evidence Immunoprecipitation, in vitro protein-protein interaction assay, and ubiquitination assay in P. falciparum

    PMID:38416790

    Open questions at the time
    • The specific role of CACYBP within the PfSCF complex (e.g. substrate recognition, scaffolding, or regulation) is not defined
    • No CACYBP-dependent ubiquitination substrate identified
    • Single-lab characterization without reciprocal in vivo validation of CACYBP's requirement for complex activity

Open questions

Synthesis pass · forward-looking unresolved questions
  • What distinct molecular function CACYBP contributes to the PfSCF complex, and whether it targets specific substrates for ubiquitination, remains unestablished.
  • No substrate or CACYBP-specific catalytic/adaptor role defined
  • No structural model of CACYBP within the complex
  • No genetic loss-of-function phenotype for CACYBP itself

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
PfSCF ubiquitin E3 ligase complex (PfCullin-1, PfRbx1, PfSkp1, PfFBXO1, CACYBP)

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2024 CACYBP (PF3D7_1238100) was identified as a component of the functional P. falciparum SCF (PfSCF) ubiquitin E3 ligase complex, comprising PfCullin-1, PfRbx1, PfSkp1, PfFBXO1, and calcyclin binding protein (CACYBP), as confirmed by immunoprecipitation and in vitro protein-protein interaction assays. Immunoprecipitation, in vitro protein-protein interaction assay, and ubiquitination assay PLoS pathogens Medium 38416790
2023 CACYBP (ortholog PyCacyBP) in Plasmodium yoelii nigeriensis is expressed as an approximately 27 kDa protein across all blood stages and exists in both monomer and dimer forms, as determined by molecular characterization of the recombinant protein in parasite lysate. Cloning, recombinant protein purification, SDS-PAGE/Western blot of parasite lysate, biophysical characterization Experimental parasitology Low 36707015

Source papers

Stage 0 corpus · 2 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2024 Plasmodium falciparum contains functional SCF and CRL4 ubiquitin E3 ligases, and CRL4 is critical for cell division and membrane integrity. PLoS pathogens 12 38416790
2023 Molecular and immunological characterization of the calcyclin binding protein in rodent malaria parasite. Experimental parasitology 0 36707015