Affinage · Plasmodium

Showing PF3D7_1352400 — NUP176 is a alias.

NUP176

PF3D7_1352400 · nucleoporin NUP176, 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

NUP176 (PF3D7_1352400) is a Plasmodium-specific constituent of the nuclear pore complex (NPC), identified by TurboID proximity labeling with the nucleoporin NUP313 as bait and confirmed at the NPC by GFP tagging in P. berghei, where deletion attempts indicate it is essential for parasite survival (PMID:36040030). It lacks primary sequence homology to proteins outside the Plasmodium genus (PMID:36040030). Beyond its NPC membership, no catalytic activity or detailed mechanistic role has been characterized for NUP176 in the available corpus.

Mechanistic history

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

    Whether PF3D7_1352400 encodes a nuclear pore component was unknown; proximity labeling from a known nucleoporin placed it at the NPC and established it as an essential, Plasmodium-restricted parasite protein.

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

    PMID:36040030

    Open questions at the time
    • No specific molecular function or interaction interface within the NPC defined
    • Essentiality inferred from failed deletion rather than a conditional knockdown phenotype
    • Stoichiometry and position within the NPC architecture unresolved
  2. 2026 Low

    Whether NUP176 engages factors involved in nucleocytoplasmic trafficking was untested; co-purification with the cryptochrome-like protein PfDPL placed NUP176 among NPC constituents associating with PfDPL.

    Evidence Co-purification/pulldown with MS using PfDPL as bait in P. falciparum

    PMID:41986327

    Open questions at the time
    • Single co-purification with no NUP176-specific functional follow-up or reciprocal validation
    • Direct versus indirect (whole-NPC) association with PfDPL not distinguished
    • No mechanistic role in trafficking assigned to NUP176 itself

Open questions

Synthesis pass · forward-looking unresolved questions
  • The specific molecular function of NUP176 within the NPC, its direct binding partners, and its role in nucleocytoplasmic transport remain undefined.
  • No structural model or defined domain function
  • No direct interaction partners established beyond NPC co-membership
  • No conditional loss-of-function phenotype characterizing its essential role

Mechanism profile

Synthesis pass · controlled-vocabulary classification
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 NUP176 (PF3D7_1352400) 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 in P. berghei. GFP tagging confirmed its NPC localization. Gene deletion attempts indicate NUP176 is essential for parasite survival. NUP176 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
2026 NUP176 (PF3D7_1352400) co-purified with the P. falciparum cryptochrome-like protein PfDPL in a pulldown experiment, placing NUP176 among nuclear-pore constituents associating with PfDPL. This association suggests NUP176 may participate in nucleocytoplasmic trafficking; however, the paper only experimentally establishes co-purification and does not directly assign a mechanistic role to NUP176 itself. Co-purification/pulldown followed by mass spectrometry (PfDPL as bait) Nature communications Low 41986327

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
2026 GID/CTLH E3 ligase complex control cell fate programs for sexual development of Plasmodium falciparum. Nature communications 0 41986327