Affinage · Plasmodium

NUP335

PF3D7_0317300 · nucleoporin NUP335, 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

NUP335 (PF3D7_0317300) is an essential, Plasmodium-specific component of the nuclear pore complex (NPC), identified in P. berghei by TurboID proximity labeling with the nucleoporin NUP313 as bait and confirmed to localize to the NPC by GFP tagging; gene deletion attempts indicate it is essential for parasite survival, and it lacks primary sequence homology to proteins outside the Plasmodium genus (PMID:36040030). Beyond its membership in the NPC and a single co-purification with the nuclear envelope protein SUN1 during male gametogenesis in P. berghei (PMID:40392232), no direct molecular function, substrate, or mechanism has been characterized for NUP335 itself in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2022 Medium

    Whether PF3D7_0317300 is part of the Plasmodium nuclear pore was unknown; proximity labeling from a known nucleoporin bait placed it within the NPC and established it as an essential, genus-restricted component.

    Evidence TurboID proximity labeling with NUP313 bait, affinity purification/mass spectrometry, GFP live imaging, and gene deletion attempts in P. berghei

    PMID:36040030

    Open questions at the time
    • No direct biochemical activity or transport function assigned to NUP335 itself
    • Structural position within the NPC and direct binding partners not resolved
    • Essentiality inferred from failed deletion, not from conditional knockdown
  2. 2025 Low

    Whether the NUP335-containing NPC physically associates with the nuclear envelope LINC-like machinery was untested; co-purification with SUN1 placed NUP335 in proximity to the SUN1 complex during male gametogenesis.

    Evidence Interactomics/co-purification with mass spectrometry, live-cell imaging, and ultrastructural expansion microscopy in P. berghei, in a study focused on SUN1 and ALLAN

    PMID:40392232

    Open questions at the time
    • Single incidental co-purification within a SUN1/ALLAN-focused study; no direct functional experiment on NUP335
    • No reciprocal pulldown or direct interaction validation for NUP335
    • Functional consequence of the NPC-SUN1 association for NUP335 not tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • The direct molecular function of NUP335, its structural role within the NPC, and its specific binding partners remain unresolved beyond membership in the pore complex.
  • No defined molecular activity for NUP335
  • No mapped direct protein-protein interfaces within the NPC
  • No conditional depletion to define its role in nucleocytoplasmic transport or nuclear organization

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
NUP313 (PROXIMITY-LABELING BAIT)SUN1 (CO-PURIFICATION)
Complex memberships
Nuclear pore complex (NPC)

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2022 NUP335 (PF3D7_0317300) was identified as a component of the Plasmodium nuclear pore complex (NPC) by TurboID proximity labeling followed by affinity purification and mass spectrometry, using NUP313 as bait. GFP tagging confirmed NPC localization. Gene deletion attempts indicate NUP335 is essential to parasite survival. NUP335 lacks primary sequence homology with proteins outside the Plasmodium genus. TurboID proximity labeling, affinity purification, mass spectrometry, GFP tagging (live imaging), gene deletion attempts mBio Medium 36040030
2025 NUP335 (PF3D7_0317300) co-purified with SUN1, a conserved nuclear envelope protein, placing NUP335 in proximity to the SUN1-ALLAN complex at the nuclear envelope during male gametogenesis in P. berghei. This co-purification was detected by interactomics and suggests NUP335-containing nuclear pores are associated with the SUN1 complex that coordinates MTOC dynamics at the nuclear envelope. Interactomics (co-purification/mass spectrometry), live-cell imaging, ultrastructural expansion microscopy eLife Low 40392232

Source papers

Stage 0 corpus · 2 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2022 TurboID Identification of Evolutionarily Divergent Components of the Nuclear Pore Complex in the Malaria Model Plasmodium berghei. mBio 14 36040030
2025 A novel SUN1-ALLAN complex coordinates segregation of the bipartite MTOC across the nuclear envelope during rapid closed mitosis in Plasmodium berghei. eLife 0 40392232