Affinage · Toxoplasma gondii

NUP37

nucleoporin complex subunit 54 · UniProt A0A125YJ23

Annotated
2026-09-10
1 papers in source corpus 1 papers cited in narrative 1 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NUP37 (TG_248500) has been identified as a component of the Toxoplasma gondii nuclear pore complex, recovered among the proteins co-purifying with the nucleoporin TgNup302 by affinity tag purification and mass spectrometry, with NPC localization confirmed for some of the co-purifying nucleoporins by structured illumination microscopy (PMID:28138739). Beyond this identification as an NPC-associated protein, nothing further about NUP37 function has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 1 step
  1. 2017 Low

    Before this work it was unknown whether Toxoplasma encodes a conserved NPC subunit corresponding to NUP37; co-purification with TgNup302 placed NUP37 within the parasite's nuclear pore complex interactome, establishing it as a candidate structural NPC component.

    Evidence Affinity tag purification and mass spectrometry of TgNup302 interactors, with reverse immunoprecipitation and structured illumination microscopy of NPC localization

    PMID:28138739

    Open questions at the time
    • NUP37 was identified only as a co-purifying protein in a single AP-MS screen, without reciprocal validation targeting NUP37 directly
    • No direct functional experiments, localization, or interaction mapping specific to NUP37 were performed
    • The stoichiometry and position of NUP37 within the NPC architecture are undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
Complex memberships
Nuclear pore complex (NPC)

Evidence

Reading pass · 1 per-paper finding extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2017 The Toxoplasma gondii nuclear pore complex (NPC), which includes NUP37 (TG_248500) as an identified component, was partially characterized via affinity tag purification and mass spectrometry of TgNup302-interacting proteins; NUP37 was among the NPC proteins identified in this interactome, and structured illuminated microscopy confirmed NPC localization of some TgNup302-interacting proteins. Affinity tag purification combined with mass spectrometry (AP-MS); reverse immunoprecipitation; structured illumination microscopy Cellular and molecular life sciences : CMLS Low 28138739

Source papers

Stage 0 corpus · 1 paper · ranked by NIH iCite citations
Year Title Journal Citations PMID
2017 Characterization of a nuclear pore protein sheds light on the roles and composition of the Toxoplasma gondii nuclear pore complex. Cellular and molecular life sciences : CMLS 13 28138739