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Fungal SPFH proteins are required for respiration, stress adaptation, and membrane scaffolding. In the yeast\n                      <jats:italic>Candida albicans<\/jats:italic>\n                      , stomatin-like protein 3 (Slp3) forms punctate foci at the plasma membrane, and\n                      <jats:italic>SLP3<\/jats:italic>\n                      overexpression causes cell death following exposure to the surfactant, SDS, and the oxidative stressor, H\n                      <jats:sub>2<\/jats:sub>\n                      O\n                      <jats:sub>2<\/jats:sub>\n                      . Here, we sought to determine the cellular localization and functionally characterize stomatin-like protein 2 (Slp2), prohibitin-1 (Phb1), prohibitin-2 (Phb2), and prohibitin-12 (Phb12) in\n                      <jats:italic>C. albicans<\/jats:italic>\n                      . Cytological and western blotting results showed that Slp2-Gfp\/Rfp and prohibitin-Gfp fusion proteins localize to the mitochondrion in yeast cells. Growth assay results did not identify any respiration defects in a panel of stomatin and prohibitin mutant strains, suggesting that SPFH respiratory function has diverged in\n                      <jats:italic>C. albicans<\/jats:italic>\n                      from other model eukaryotes. However, a\n                      <jats:italic>slp2\u0394<\/jats:italic>\n                      \/\n                      <jats:italic>\u0394<\/jats:italic>\n                      \/\n                      <jats:italic>slp3\u0394<\/jats:italic>\n                      \/\n                      <jats:italic>\u0394<\/jats:italic>\n                      double mutant strain grew poorly in the presence of 0.08% SDS, accumulated intracellular reactive oxidative species, and displayed aberrant ergosterol distribution in the plasma membrane. These phenotypes were not observed in\n                      <jats:italic>slp2\u0394<\/jats:italic>\n                      \/\n                      <jats:italic>\u0394<\/jats:italic>\n                      or\n                      <jats:italic>slp3\u0394<\/jats:italic>\n                      \/\n                      <jats:italic>\u0394<\/jats:italic>\n                      single mutants, indicating a possible indirect genetic interaction between\n                      <jats:italic>SLP2<\/jats:italic>\n                      and\n                      <jats:italic>SLP3<\/jats:italic>\n                      . In addition,\n                      <jats:italic>slp2\u0394<\/jats:italic>\n                      \/\n                      <jats:italic>\u0394<\/jats:italic>\n                      and\n                      <jats:italic>slp2\u0394<\/jats:italic>\n                      \/\n                      <jats:italic>\u0394<\/jats:italic>\n                      \/\n                      <jats:italic>slp3\u0394<\/jats:italic>\n                      \/\n                      <jats:italic>\u0394<\/jats:italic>\n                      mutant strains were slightly resistant to the antifungal drug, fluconazole. Collectively, these findings reveal the cellular localization of Slp2, Phb1, Phb2, and Phb12, highlight the significance of stomatins in\n                      <jats:italic>C. albicans<\/jats:italic>\n                      SDS stress tolerance, and, for the first time, associate stomatins with antifungal resistance.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>IMPORTANCE<\/jats:title>\n                    <jats:p>\n                      Stomatins and prohibitins coordinate respiration and stress adaptation in fungi. Invasive mycoses caused by\n                      <jats:italic>Candida albicans<\/jats:italic>\n                      are a significant cause of morbidity, and candidemia patients show high mortality rates worldwide. Mitochondria are essential for\n                      <jats:italic>C. albicans<\/jats:italic>\n                      commensalism and virulence, and mitochondrial proteins are targets for antifungal interventions.\n                      <jats:italic>C. albicans<\/jats:italic>\n                      encodes five SPFH proteins: two stomatin-like proteins and three prohibitins. We have previously shown that Slp3 is important for\n                      <jats:italic>C. albicans<\/jats:italic>\n                      adaptation to various types of environmental stress. Moreover, synthetic compounds that bind to mammalian prohibitins inhibit\n                      <jats:italic>C. albicans<\/jats:italic>\n                      filamentation and are fungicidal. However, there is limited information available regarding the remaining SPFH proteins. Our findings show that mitochondrial localization of SPFH proteins is conserved in\n                      <jats:italic>C. albicans<\/jats:italic>\n                      . In addition, we demonstrate the importance of stomatins in plasma membrane and mitochondrial stress tolerance.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1128\/spectrum.01733-24","type":"journal-article","created":{"date-parts":[[2024,12,6]],"date-time":"2024-12-06T09:02:01Z","timestamp":1733475721000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":4,"title":["Mitochondrial targeting of\n                    <i>Candida albicans<\/i>\n                    SPFH proteins and requirement of stomatins for SDS-induced stress tolerance"],"prefix":"10.1128","volume":"13","author":[{"given":"Hyunjeong","family":"Kim","sequence":"first","affiliation":[{"name":"Department of Sciences, John Jay College of the City University of New York","place":["New York, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6247-1252","authenticated-orcid":false,"given":"Marienela Y.","family":"Heredia","sequence":"additional","affiliation":[{"name":"Department of Sciences, John Jay College of the City University of New York","place":["New York, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiao","family":"Chen","sequence":"additional","affiliation":[{"name":"Department of Sciences, John Jay College of the City University of New York","place":["New York, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maisha","family":"Ahmed","sequence":"additional","affiliation":[{"name":"Department of Sciences, John Jay College of the City University of New York","place":["New York, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohammad","family":"Qasim","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cellular Biology, School of Natural Sciences, University of California","place":["Merced, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tracy L.","family":"Callender","sequence":"additional","affiliation":[{"name":"Department of Biology, Farmingdale State College of the State University of New York","place":["Farmingdale, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aaron D.","family":"Hernday","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cellular Biology, School of Natural Sciences, University of California","place":["Merced, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3978-7694","authenticated-orcid":true,"given":"Jason M.","family":"Rauceo","sequence":"additional","affiliation":[{"name":"Department of Sciences, John Jay College of the City University of New York","place":["New York, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","volume-title":"Candida and candidiasis","author":"Richard A","year":"2012","unstructured":"RichardA, CalderoneCJC, eds. 2012. 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