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@ARTICLE{MesnRamrez:626191,
      author       = {Mesén-Ramírez, Joëlle Paolo and Fuchs, Gwendolin and
                      Burmester, Jonas and Farias, Guilherme B. and Alape-Flores,
                      Ana María and Singla, Shamit and Alder, Arne and
                      Cubillán-Marín, José and Castro-Peña, Carolina and
                      Lemcke, Sarah and Sondermann, Holger and Prado, Mónica and
                      Spielmann, Tobias and Wilson, Danny and Gilberger, Tim},
      title        = {{HOPS}/{CORVET} tethering complexes are critical for
                      endocytosis and protein trafficking to invasion related
                      organelles in malaria parasites},
      journal      = {PLoS pathogens},
      volume       = {21},
      number       = {4},
      issn         = {1553-7366},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {PUBDB-2025-01332},
      pages        = {e1013053 -},
      year         = {2025},
      abstract     = {The tethering complexes HOPS/CORVET are central for
                      vesicular fusion through the eukaryotic endolysosomal
                      system, but the functions of these complexes in the
                      intracellular development of malaria parasites are still
                      unknown. Here we show that the HOPS/CORVET core subunits are
                      critical for the intracellular proliferation of the malaria
                      parasite Plasmodium falciparum. We demonstrate that
                      HOPS/CORVET are required for parasite endocytosis and host
                      cell cytosol uptake, as early functional depletion of the
                      complex led to developmental arrest and accumulation of
                      endosomes that failed to fuse to the digestive vacuole
                      membrane. Late depletion of the core HOPS/CORVET subunits
                      led to a severe defect in merozoite invasion as a result of
                      the mistargeting of proteins destined to the apical
                      secretory organelles, the rhoptries and micronemes.
                      Ultrastructure-expansion microscopy revealed a reduced
                      rhoptry volume and the accumulation of numerous vesicles in
                      HOPS/CORVET deficient schizonts, further supporting a role
                      of HOPS/CORVET in post-Golgi protein cargo trafficking to
                      the invasion related organelles. Hence, malaria parasites
                      have repurposed HOPS/CORVET to perform dual functions across
                      the intraerythrocytic cycle, consistent with a canonical
                      endocytic pathway for delivery of host cell material to the
                      digestive vacuole in trophozoite stages and a parasite
                      specific role in trafficking of protein cargo to the apical
                      organelles required for invasion in schizont stages.},
      cin          = {CSSB-BNITM-TG / CSSB-DESY-HS},
      ddc          = {610},
      cid          = {I:(DE-H253)CSSB-BNITM-TG-20210520 /
                      I:(DE-H253)CSSB-DESY-HS-20210521},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-H253)ALFM-20250101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40198740},
      UT           = {WOS:001462112300002},
      doi          = {10.1371/journal.ppat.1013053},
      url          = {https://bib-pubdb1.desy.de/record/626191},
}