Affinage · Plasmodium

LSM2

PF3D7_0520300 · U6 snRNA-associated Sm-like protein LSm2, putative

Audit flag: identity unverified
Annotated
2026-09-08
4 papers in source corpus 2 papers cited in narrative 2 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

LSM2 (PF3D7_0520300) is an Sm-like protein of P. falciparum that has been placed within the mRNA decay machinery through its co-purification with PfDOZI-associated processing body (PB)-like mRNPs in schizonts (PMID:38702310). In this context LSM2 co-immunoprecipitates with PfDOZI alongside decapping enzymes (DCP2, DCP1), other LSm proteins (LSm1-4, LSm7), and the deadenylase/CCR4-NOT-associated components NOT1, CAF1 and CAF40, and is relatively more abundant in schizont-stage PfDOZI complexes than core stress granule components, consistent with a role in mRNA decay (PMID:38702310). LSM2 has also been detected in the experimentally determined core nuclear proteome of P. falciparum (PMID:23181666). Beyond this membership in the PfDOZI mRNP and its nuclear detection, no direct functional experiments have been performed on LSM2 itself in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2012 Low

    Establishing where LSM2 resides was the first step toward assigning it a cellular role; detection in the isolated nuclear fraction placed the protein in the nucleus.

    Evidence high-accuracy mass spectrometry of isolated nuclear fractions with bioinformatic analysis, validated with transgenic lines, in P. falciparum

    PMID:23181666

    Open questions at the time
    • Large-scale proteomic inventory with no functional experiment on LSM2 specifically
    • Does not resolve subnuclear localization or associated complexes
    • Nuclear detection is not reconciled with the later cytoplasmic mRNP association
  2. 2024 Medium

    Whether LSM2 participates in mRNA metabolism was addressed by showing it is a component of PfDOZI-associated PB-like mRNPs enriched for decay machinery, implicating it in mRNA decay rather than storage.

    Evidence GFP-trap immunoprecipitation of PfDOZI::GFP followed by mass spectrometry in P. falciparum schizonts

    PMID:38702310

    Open questions at the time
    • Single Co-IP/MS experiment with no reciprocal pull-down or direct functional validation of LSM2
    • Does not establish which RNAs or complex subunits LSM2 directly contacts
    • No knockout, knockdown, or biochemical reconstitution of LSM2 function

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unknown whether LSM2 has any function beyond its membership in the PfDOZI mRNP, and no direct biochemical or genetic role has been defined for the protein.
  • No genetic ablation or phenotype for LSM2
  • No demonstration of direct RNA binding or Sm-like ring assembly by LSM2
  • No resolution of how nuclear detection relates to cytoplasmic mRNP association

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
PfDOZI-associated processing body (PB)-like mRNP

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2024 LSM2 (PF3D7_0520300) was identified as a component of PfDOZI-associated processing body (PB)-like mRNPs in P. falciparum schizonts, co-immunoprecipitating with PfDOZI alongside other mRNA decay-related proteins (DCP2, DCP1, LSm1-4, LSm7, NOT1, CAF1, CAF40); LSM2 was relatively more abundant in schizont-stage PfDOZI complexes than core stress granule components, consistent with a role in mRNA decay. GFP-trap immunoprecipitation of PfDOZI::GFP followed by mass spectrometry-based protein identification Nature communications Medium 38702310
2012 LSM2 (PF3D7_0520300) was detected in the experimentally determined core nuclear proteome of P. falciparum, indicating nuclear localization of this protein. High-accuracy mass spectrometry of isolated nuclear fractions combined with bioinformatic analysis; validated with transgenic cell lines Genome biology Low 23181666

Source papers

Stage 0 corpus · 4 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2012 Organellar proteomics reveals hundreds of novel nuclear proteins in the malaria parasite Plasmodium falciparum. Genome biology 120 23181666
2011 RNA-Seq analysis of splicing in Plasmodium falciparum uncovers new splice junctions, alternative splicing and splicing of antisense transcripts. Nucleic acids research 108 21245033
2024 The DEAD-box RNA helicase PfDOZI imposes opposing actions on RNA metabolism in Plasmodium falciparum. Nature communications 0 38702310
2009 Sm/Lsm genes provide a glimpse into the early evolution of the spliceosome. PLoS computational biology 0 19282982