Affinage · Plasmodium

Showing PF3D7_1423800 — VPS3 is a alias.

VPS3

PF3D7_1423800 · vacuolar protein sorting-associated protein 3, 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

VPS3 (PF3D7_1423800) is a CORVET-specific component of the Vps-C endosomal tethering machinery in Plasmodium falciparum (PMID:40626728). It was first recognized through comparative genomics as an ancient, pan-eukaryotically conserved CORVET/HOPS-associated subunit retained across apicomplexan genomes, expressed in patterns consistent with functioning as part of a minimal multisubunit tethering complex (PMID:24086721). Direct biochemical evidence places VPS3 within the parasite's Vps-C complex: immunoprecipitation and mass spectrometry identified it as an interactor of PfVps16, the P. falciparum ortholog of the Vps16 core subunit (PMID:40626728). Beyond its physical membership in this complex, the specific molecular function, substrates, and cellular role of VPS3 itself have not been experimentally characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2013 Low

    Establishing whether the CORVET tethering machinery is conserved in apicomplexans was the first question; comparative genomics showed VPS3 is retained as an ancient, conserved Vps-C-associated subunit in P. falciparum, framing it as candidate endosomal machinery.

    Evidence Comparative genomic/bioinformatic analysis across twelve apicomplexan genomes and outgroup taxa

    PMID:24086721

    Open questions at the time
    • Bioinformatic prediction only; no biochemical or genetic experiment performed on the VPS3 protein
    • Complex membership inferred from conservation, not demonstrated in the parasite
    • No localization or interaction data
  2. 2025 Medium

    Whether VPS3 physically resides in the parasite Vps-C complex, rather than merely being predicted to, was addressed by pulling it down alongside a core subunit, providing the first direct biochemical placement within the tethering machinery.

    Evidence Immunoprecipitation and mass spectrometry identifying VPS3 as a PfVps16 interactor

    PMID:40626728

    Open questions at the time
    • Single method (co-IP/MS) without reciprocal pull-down validation
    • No functional mutagenesis, knockdown, or knockout to test VPS3's role
    • Whether VPS3 defines a CORVET versus HOPS assignment functionally is not tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • The specific molecular function of VPS3 beyond complex membership remains unknown, including its contribution to vesicle tethering, essentiality, and cellular localization in the parasite.
  • No genetic loss-of-function phenotype for VPS3
  • No subcellular localization data for VPS3
  • No defined role in a specific endosomal trafficking pathway

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
PFVPS16
Complex memberships
CORVET complexVps-C core tethering complex

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2013 VPS3 (PF3D7_1423800) was identified as a subunit of the CORVET complex with an ancient pan-eukaryotic origin; bioinformatic analysis across twelve apicomplexan genomes demonstrated that VPS3 is conserved in Plasmodium falciparum as part of the CORVET/HOPS VpsC-associated machinery, and that those subunits identified appear to be expressed with similar patterns to fully conserved MTC proteins, suggesting function as minimal complexes or with analogous partners. Comparative genomic/bioinformatic analysis across twelve apicomplexan genomes and outgroup taxa PloS one Low 24086721
2025 VPS3 (PF3D7_1423800), the CORVET-specific component, was identified as an interactor of PfVps16 (the P. falciparum ortholog of Vps16) by immunoprecipitation followed by mass spectrometry, placing VPS3 within the P. falciparum Vps-C tethering complex. Immunoprecipitation and mass spectrometry (co-IP/MS) mSphere Medium 40626728

Source papers

Stage 0 corpus · 2 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2013 Comparative genomic analysis of multi-subunit tethering complexes demonstrates an ancient pan-eukaryotic complement and sculpting in Apicomplexa. PloS one 54 24086721
2025 The Plasmodium falciparum homolog of Vps16 interacts with the core members of the Vps-C tethering complex. mSphere 0 40626728