{
  "abstract": "Biological membranes are laterally heterogeneous and contain specialized microdomains called lipid rafts. Lipid rafts serve as organizational platforms that cluster signaling molecules or modulate membrane protein conformation through their unique lipid environment. There are specific lipid raft marker proteins whose functions remain obscure. One of these proteins is flotillin which has been linked to endocytosis. Here, we investigated the regulation and function of FloA, the sole flotillin homolog in the model fungus Aspergillus nidulans. FloA expression is specifically upregulated in response to calcium stress, which is a regulatory pattern also conserved in Aspergillus fumigatus. BioID proximity labeling revealed that A. nidulans FloA physically interacts with proteins in the endocytic pathway as well as another lipid raft marker, the plasma membrane H+-ATPase PmaA. Under calcium stress, PmaA undergoes internalization from the cytoplasmic membrane. However, when floA is deleted, PmaA internalization is prevented, resulting in cell death. This phenotype of the ΔfloA strain could be mimicked by treating the cells with an endocytosis inhibitor during calcium stress. Together, we demonstrate that FloA is essential for the internalization of PmaA during calcium stress, a process that prevents intracellular calcium overload and promotes cell viability. Our results also provide further evidence for flotillin-assisted endocytosis. Author summary: Lipids and proteins in a cell membrane can cluster together in small regions often called “lipid rafts”, which help the cell interact with its surroundings. Lipid rafts can bring receptors together or influence how membrane proteins behave. Flotillin is a protein often found within lipid rafts, but its exact role is not well understood. Instead of using complex mammalian systems, we studied flotillins in the fungus Aspergillus nidulans, which is a simpler model organism that allows for a better understanding of cellular processes. We found that more flotillins are produced when the fungus is exposed to calcium stress. When flotillins were missing, the cells were unable to remove the protein PmaA from the cell membrane during calcium stress. As a result, the fungus could not cope with the calcium stress and eventually died. Therefore, we propose that flotillins are important for the fungus to reorganize its membranes and coping with calcium stress.",
  "abstract_shown": true,
  "affiliations": [
    "Department of Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute (Leibniz-HKI), Jena, Germany",
    "Institute for Microbiology, Friedrich Schiller University Jena, Jena, Germany",
    "Cluster of Excellence Balance of the Microverse, Friedrich Schiller University Jena, Jena Germany"
  ],
  "article_type": "Research Article",
  "arxiv": null,
  "author_total": 6,
  "authors": [
    {
      "affs": [
        0,
        1,
        2
      ],
      "name": "Moemi Kawashima",
      "orcid": "0009-0006-7210-7175"
    },
    {
      "affs": [
        0
      ],
      "name": "Thomas Krüger",
      "orcid": "0000-0001-8984-3853"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Maira Rosin",
      "orcid": "0000-0002-4263-4541"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Sophie Tröger-Görler"
    },
    {
      "affs": [
        0
      ],
      "name": "Thorsten Heinekamp",
      "orcid": "0000-0001-9503-9634"
    },
    {
      "affs": [
        0,
        1,
        2
      ],
      "name": "Axel A. Brakhage",
      "orcid": "0000-0002-8814-4193"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/dj63rkxrk88vv.bib",
  "cited_by": 0,
  "doi": "10.1371/journal.pgen.1012147",
  "fulltext_url": "https://journals.plos.org/plosgenetics/article?id=10.1371/journal.pgen.1012147",
  "id": "dj63rkxrk88vv",
  "issns": [
    "1553-7404",
    "1553-7390"
  ],
  "landing_url": "https://journals.plos.org/plosgenetics/article?id=10.1371/journal.pgen.1012147",
  "language": "en",
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "heading",
      "Animal Studies"
    ],
    [
      "heading",
      "Aspergillus"
    ],
    [
      "heading",
      "Aspergillus Fumigatus"
    ],
    [
      "heading",
      "Aspergillus Nidulans"
    ],
    [
      "heading",
      "Biochemistry"
    ],
    [
      "heading",
      "Biology and Life Sciences"
    ],
    [
      "heading",
      "Cell Biology"
    ],
    [
      "heading",
      "Cell Membranes"
    ],
    [
      "heading",
      "Cell Processes"
    ],
    [
      "heading",
      "Cellular Structures and Organelles"
    ],
    [
      "heading",
      "Endocytosis"
    ],
    [
      "heading",
      "Eukaryota"
    ],
    [
      "heading",
      "Experimental Organism Systems"
    ],
    [
      "heading",
      "Fungal Molds"
    ],
    [
      "heading",
      "Fungal Pathogens"
    ],
    [
      "heading",
      "Fungi"
    ],
    [
      "heading",
      "Intracellular Membranes"
    ],
    [
      "heading",
      "Lipids"
    ],
    [
      "heading",
      "Medical Microbiology"
    ],
    [
      "heading",
      "Medicine and Health Sciences"
    ],
    [
      "heading",
      "Membrane Proteins"
    ],
    [
      "heading",
      "Microbial Pathogens"
    ],
    [
      "heading",
      "Microbiology"
    ],
    [
      "heading",
      "Mycology"
    ],
    [
      "heading",
      "Nuclear Physics"
    ],
    [
      "heading",
      "Nucleons"
    ],
    [
      "heading",
      "Organisms"
    ],
    [
      "heading",
      "Pathogens"
    ],
    [
      "heading",
      "Pathology and Laboratory Medicine"
    ],
    [
      "heading",
      "Physical Sciences"
    ],
    [
      "heading",
      "Physics"
    ],
    [
      "heading",
      "Protons"
    ],
    [
      "heading",
      "Research Article"
    ],
    [
      "heading",
      "Research and Analysis Methods"
    ],
    [
      "heading",
      "Secretory Pathway"
    ],
    [
      "heading",
      "Yeast and Fungal Models"
    ],
    [
      "plos",
      "/Biology and life sciences/Biochemistry/Lipids"
    ],
    [
      "plos",
      "/Biology and life sciences/Cell biology/Cell processes/Endocytosis"
    ],
    [
      "plos",
      "/Biology and life sciences/Cell biology/Cell processes/Secretory pathway/Endocytosis"
    ],
    [
      "plos",
      "/Biology and life sciences/Cell biology/Cellular structures and organelles/Cell membranes"
    ],
    [
      "plos",
      "/Biology and life sciences/Cell biology/Cellular structures and organelles/Cell membranes/Intracellular membranes"
    ],
    [
      "plos",
      "/Biology and life sciences/Cell biology/Cellular structures and organelles/Cell membranes/Membrane proteins"
    ],
    [
      "plos",
      "/Biology and life sciences/Microbiology/Medical microbiology/Microbial pathogens/Fungal pathogens/Aspergillus fumigatus"
    ],
    [
      "plos",
      "/Biology and life sciences/Mycology/Fungal pathogens/Aspergillus fumigatus"
    ],
    [
      "plos",
      "/Biology and life sciences/Organisms/Eukaryota/Fungi/Fungal molds/Aspergillus/Aspergillus fumigatus"
    ],
    [
      "plos",
      "/Biology and life sciences/Organisms/Eukaryota/Fungi/Fungal molds/Aspergillus/Aspergillus nidulans"
    ],
    [
      "plos",
      "/Medicine and health sciences/Pathology and laboratory medicine/Pathogens/Microbial pathogens/Fungal pathogens/Aspergillus fumigatus"
    ],
    [
      "plos",
      "/Physical sciences/Physics/Nuclear physics/Nucleons/Protons"
    ],
    [
      "plos",
      "/Research and analysis methods/Animal studies/Experimental organism systems/Yeast and fungal models/Aspergillus nidulans"
    ]
  ],
  "openalex": null,
  "pdf_url": "https://journals.plos.org/plosgenetics/article/file?id=10.1371/journal.pgen.1012147&type=printable",
  "pmcid": "PMC13734606",
  "pmid": "42956075",
  "published": "2026-10-29",
  "publisher": "Public Library of Science",
  "ris": "https://research.draconitic.com/paper/dj63rkxrk88vv.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:17Z",
      "native_id": "10.1371/journal.pgen.1012147",
      "source": "plos",
      "url": "https://journals.plos.org/plosgenetics/article?id=10.1371/journal.pgen.1012147"
    },
    {
      "first_seen": "2026-11-08T12:24:03Z",
      "native_id": "PMC13734606",
      "source": "pmc",
      "url": "https://doi.org/10.1371/journal.pgen.1012147"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "heading:Biochemistry",
      "subfield": "general"
    },
    {
      "field": "biology",
      "origin": "plos:cell biology",
      "subfield": "cell-biology"
    },
    {
      "field": "biology",
      "origin": "heading:Microbiology",
      "subfield": "microbiology"
    },
    {
      "field": "medicine",
      "origin": "heading:Medicine and Health Sciences",
      "subfield": "general"
    },
    {
      "field": "physics",
      "origin": "heading:Nuclear Physics",
      "subfield": "nuclear"
    }
  ],
  "title": "The lipid raft marker flotillin FloA drives relocalization of the plasma membrane H⁺-ATPase PmaA as a protective response to calcium stress",
  "title_text": "The lipid raft marker flotillin FloA drives relocalization of the plasma membrane H⁺-ATPase PmaA as a protective response to calcium stress",
  "type": "peer-reviewed",
  "updated_at": "2026-11-08T12:24:03Z",
  "url": "https://research.draconitic.com/paper/dj63rkxrk88vv",
  "venue": "PLOS Genetics",
  "versions": []
}